NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|67551261|ref|NP_004062|]
View 

dual specificity protein kinase CLK1 isoform 1 [Homo sapiens]

Protein Classification

dual specificity protein kinase CLK( domain architecture ID 10197762)

dual specificity protein kinase CLK (CDC-like kinase) catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates, and is involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
148-477 0e+00

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: 653.07  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 148 HLICQSGDVLSARYEIVDTLGEGAFGKVVECIDHKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTDPNSTFRCVQM 227
Cdd:cd14213   1 HLICQSGDVLRARYEIVDTLGEGAFGKVVECIDHKMGGMHVAVKIVKNVDRYREAARSEIQVLEHLNTTDPNSTFRCVQM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 228 LEWFEHHGHICIVFELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYTEAYNP 307
Cdd:cd14213  81 LEWFDHHGHVCIVFELLGLSTYDFIKENSFLPFPIDHIRNMAYQICKSVNFLHHNKLTHTDLKPENILFVQSDYVVKYNP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 308 KIKRDERTLINPDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEH 387
Cdd:cd14213 161 KMKRDERTLKNPDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFQTHDSKEH 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 388 LAMMERILGPLPKHMIQKTRKRKYFHHDRLDWDEHSSAGRYVSRRCKPLKEFMLSQDVEHERLFDLIQKMLEYDPAKRIT 467
Cdd:cd14213 241 LAMMERILGPLPKHMIQKTRKRKYFHHDQLDWDEHSSAGRYVRRRCKPLKEFMLSQDVDHEQLFDLIQKMLEYDPAKRIT 320
                       330
                ....*....|
gi 67551261 468 LREALKHPFF 477
Cdd:cd14213 321 LDEALKHPFF 330
 
Name Accession Description Interval E-value
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
148-477 0e+00

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: 653.07  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 148 HLICQSGDVLSARYEIVDTLGEGAFGKVVECIDHKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTDPNSTFRCVQM 227
Cdd:cd14213   1 HLICQSGDVLRARYEIVDTLGEGAFGKVVECIDHKMGGMHVAVKIVKNVDRYREAARSEIQVLEHLNTTDPNSTFRCVQM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 228 LEWFEHHGHICIVFELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYTEAYNP 307
Cdd:cd14213  81 LEWFDHHGHVCIVFELLGLSTYDFIKENSFLPFPIDHIRNMAYQICKSVNFLHHNKLTHTDLKPENILFVQSDYVVKYNP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 308 KIKRDERTLINPDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEH 387
Cdd:cd14213 161 KMKRDERTLKNPDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFQTHDSKEH 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 388 LAMMERILGPLPKHMIQKTRKRKYFHHDRLDWDEHSSAGRYVSRRCKPLKEFMLSQDVEHERLFDLIQKMLEYDPAKRIT 467
Cdd:cd14213 241 LAMMERILGPLPKHMIQKTRKRKYFHHDQLDWDEHSSAGRYVRRRCKPLKEFMLSQDVDHEQLFDLIQKMLEYDPAKRIT 320
                       330
                ....*....|
gi 67551261 468 LREALKHPFF 477
Cdd:cd14213 321 LDEALKHPFF 330
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
161-477 8.44e-79

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 246.29  E-value: 8.44e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261    161 YEIVDTLGEGAFGKVVECIdHKAGGRHVAVKIVK--NVDRYCEAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHGHIC 238
Cdd:smart00220   1 YEILEKLGEGSFGKVYLAR-DKKTGKLVAIKVIKkkKIKKDRERILREIKILKKLK--HPN----IVRLYDVFEDEDKLY 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261    239 IVFELL-GLSTYDFIKENGFLPfrLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQsdyteaynpkikrdertli 317
Cdd:smart00220  74 LVMEYCeGGDLFDLLKKRGRLS--EDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDE------------------- 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261    318 NPDIKVVDFGSATY--DDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPthDSKEHLAMMERIL 395
Cdd:smart00220 133 DGHVKLADFGLARQldPGEKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFP--GDDQLLELFKKIG 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261    396 GPLPKhmiqktrkrkyfhhdrldwdehssagryvsrrcKPLKEFMLSQDveherLFDLIQKMLEYDPAKRITLREALKHP 475
Cdd:smart00220 211 KPKPP---------------------------------FPPPEWDISPE-----AKDLIRKLLVKDPEKRLTAEEALQHP 252

                   ..
gi 67551261    476 FF 477
Cdd:smart00220 253 FF 254
PTZ00284 PTZ00284
protein kinase; Provisional
145-476 1.22e-61

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 208.28  E-value: 1.22e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  145 EEGHLICQSG---DVLSARYEIVDTLGEGAFGKVVECIDHKAGgRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTDPNST 221
Cdd:PTZ00284 112 EEGHFYVVLGediDVSTQRFKILSLLGEGTFGKVVEAWDRKRK-EYCAVKIVRNVPKYTRDAKIEIQFMEKVRQADPADR 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  222 FRCVQMLEWFEHH-GHICIVFELLGLSTYDFIKENGflPFRLDHIRKMAYQICKSVNFLHSN-KLTHTDLKPENILFVQS 299
Cdd:PTZ00284 191 FPLMKIQRYFQNEtGHMCIVMPKYGPCLLDWIMKHG--PFSHRHLAQIIFQTGVALDYFHTElHLMHTDLKPENILMETS 268
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  300 DYTeaYNPKIKRDertlINPD---IKVVDFGSATydDEHHS--TLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYL 374
Cdd:PTZ00284 269 DTV--VDPVTNRA----LPPDpcrVRICDLGGCC--DERHSrtAIVSTRHYRSPEVVLGLGWMYSTDMWSMGCIIYELYT 340
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  375 GFTVFPTHDSKEHLAMMERILGPLPKHMIQK--TRKRKyfhhdrldwDEHSSAG--------RYVSR--RCKPLKEfMLS 442
Cdd:PTZ00284 341 GKLLYDTHDNLEHLHLMEKTLGRLPSEWAGRcgTEEAR---------LLYNSAGqlrpctdpKHLARiaRARPVRE-VIR 410
                        330       340       350
                 ....*....|....*....|....*....|....
gi 67551261  443 QDVeherLFDLIQKMLEYDPAKRITLREALKHPF 476
Cdd:PTZ00284 411 DDL----LCDLIYGLLHYDRQKRLNARQMTTHPY 440
Pkinase pfam00069
Protein kinase domain;
161-477 9.45e-41

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 145.46  E-value: 9.45e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261   161 YEIVDTLGEGAFGKVVECIdHKAGGRHVAVKIVKNVDR---YCEAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHGHI 237
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAK-HRDTGKIVAIKKIKKEKIkkkKDKNILREIKILKKLN--HPN----IVRLYDAFEDKDNL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261   238 CIVFELL-GLSTYDFIKENGFLPfrLDHIRKMAYQICKSVNflHSNKLThtdlkpenilfvqsdyteaynpkikrdertl 316
Cdd:pfam00069  74 YLVLEYVeGGSLFDLLSEKGAFS--EREAKFIMKQILEGLE--SGSSLT------------------------------- 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261   317 inpdikvvdfgsatyddehhsTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMMERILG 396
Cdd:pfam00069 119 ---------------------TFVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPY 177
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261   397 PLPKHmiqktrkrkyfhhdrldWDEHSSAGRyvsrrckplkefmlsqdveherlfDLIQKMLEYDPAKRITLREALKHPF 476
Cdd:pfam00069 178 AFPEL-----------------PSNLSEEAK------------------------DLLKKLLKKDPSKRLTATQALQHPW 216

                  .
gi 67551261   477 F 477
Cdd:pfam00069 217 F 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
155-474 8.52e-34

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 133.21  E-value: 8.52e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 155 DVLSARYEIVDTLGEGAFGKVVECIDHKAGgRHVAVKIVK----NVDRYCEAARSEIQVLEHLNttDPNstfrCVQMLEW 230
Cdd:COG0515   3 ALLLGRYRILRLLGRGGMGVVYLARDLRLG-RPVALKVLRpelaADPEARERFRREARALARLN--HPN----IVRVYDV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 231 FEHHGHICIVFELL-GLSTYDFIKENGflPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENIlfvqsdyteaynpki 309
Cdd:COG0515  76 GEEDGRPYLVMEYVeGESLADLLRRRG--PLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANI--------------- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 310 krdertLINPD--IKVVDFGSATYDDEHHST----LVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFpthD 383
Cdd:COG0515 139 ------LLTPDgrVKLIDFGIARALGGATLTqtgtVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPF---D 209
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 384 SKEHLAMMERILgplpkhmiqktrkrkyfHHDRLDWDEHSSAgryvsrrckplkefmLSQDVEherlfDLIQKMLEYDPA 463
Cdd:COG0515 210 GDSPAELLRAHL-----------------REPPPPPSELRPD---------------LPPALD-----AIVLRALAKDPE 252
                       330
                ....*....|....*
gi 67551261 464 KRIT----LREALKH 474
Cdd:COG0515 253 ERYQsaaeLAAALRA 267
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
154-371 3.40e-11

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 65.20  E-value: 3.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  154 GDVLSARYEIVDTLGEGAFGKVvecidHKAG----GRHVAVKIVKN--------VDRY-CEA---ARseiqvLEHlnttd 217
Cdd:NF033483   2 GKLLGGRYEIGERIGRGGMAEV-----YLAKdtrlDRDVAVKVLRPdlardpefVARFrREAqsaAS-----LSH----- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  218 PNstfrCVQMLEWFEHHGHICIVFELL-GLSTYDFIKENGFLPFRlDHIRKMAyQICKSVNFLHSNKLTHTDLKPENIlf 296
Cdd:NF033483  67 PN----IVSVYDVGEDGGIPYIVMEYVdGRTLKDYIREHGPLSPE-EAVEIMI-QILSALEHAHRNGIVHRDIKPQNI-- 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  297 vqsdyteaynpkikrdertLINPD--IKVVDFG------SATYDdeHHSTLVSTRHYRAPEvilalgwsQ----PC---- 360
Cdd:NF033483 139 -------------------LITKDgrVKVTDFGiaralsSTTMT--QTNSVLGTVHYLSPE--------QarggTVdars 189
                        250
                 ....*....|.
gi 67551261  361 DVWSIGCILIE 371
Cdd:NF033483 190 DIYSLGIVLYE 200
 
Name Accession Description Interval E-value
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
148-477 0e+00

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: 653.07  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 148 HLICQSGDVLSARYEIVDTLGEGAFGKVVECIDHKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTDPNSTFRCVQM 227
Cdd:cd14213   1 HLICQSGDVLRARYEIVDTLGEGAFGKVVECIDHKMGGMHVAVKIVKNVDRYREAARSEIQVLEHLNTTDPNSTFRCVQM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 228 LEWFEHHGHICIVFELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYTEAYNP 307
Cdd:cd14213  81 LEWFDHHGHVCIVFELLGLSTYDFIKENSFLPFPIDHIRNMAYQICKSVNFLHHNKLTHTDLKPENILFVQSDYVVKYNP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 308 KIKRDERTLINPDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEH 387
Cdd:cd14213 161 KMKRDERTLKNPDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFQTHDSKEH 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 388 LAMMERILGPLPKHMIQKTRKRKYFHHDRLDWDEHSSAGRYVSRRCKPLKEFMLSQDVEHERLFDLIQKMLEYDPAKRIT 467
Cdd:cd14213 241 LAMMERILGPLPKHMIQKTRKRKYFHHDQLDWDEHSSAGRYVRRRCKPLKEFMLSQDVDHEQLFDLIQKMLEYDPAKRIT 320
                       330
                ....*....|
gi 67551261 468 LREALKHPFF 477
Cdd:cd14213 321 LDEALKHPFF 330
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
148-477 0e+00

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: 574.51  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 148 HLICQSGDVLSARYEIVDTLGEGAFGKVVECIDHKAGgRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTDPNSTFRCVQM 227
Cdd:cd14134   1 HLIYKPGDLLTNRYKILRLLGEGTFGKVLECWDRKRK-RYVAVKIIRNVEKYREAAKIEIDVLETLAEKDPNGKSHCVQL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 228 LEWFEHHGHICIVFELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYTEAYNP 307
Cdd:cd14134  80 RDWFDYRGHMCIVFELLGPSLYDFLKKNNYGPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLVDSDYVKVYNP 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 308 KIKRDERTLINPDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEH 387
Cdd:cd14134 160 KKKRQIRVPKSTDIKLIDFGSATFDDEYHSSIVSTRHYRAPEVILGLGWSYPCDVWSIGCILVELYTGELLFQTHDNLEH 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 388 LAMMERILGPLPKHMIQKTR---KRKYFHHDRLDWDEHSSAGRYVSRRCKPLKEFMLSQDVEHERLFDLIQKMLEYDPAK 464
Cdd:cd14134 240 LAMMERILGPLPKRMIRRAKkgaKYFYFYHGRLDWPEGSSSGRSIKRVCKPLKRLMLLVDPEHRLLFDLIRKMLEYDPSK 319
                       330
                ....*....|...
gi 67551261 465 RITLREALKHPFF 477
Cdd:cd14134 320 RITAKEALKHPFF 332
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
148-477 1.74e-179

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: 505.71  E-value: 1.74e-179
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 148 HLICQSGDVLSARYEIVDTLGEGAFGKVVECIDHKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTDPNSTFRCVQM 227
Cdd:cd14215   1 HLIYRSGDWLQERYEIVSTLGEGTFGRVVQCIDHRRGGARVALKIIKNVEKYKEAARLEINVLEKINEKDPENKNLCVQM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 228 LEWFEHHGHICIVFELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYTEAYNP 307
Cdd:cd14215  81 FDWFDYHGHMCISFELLGLSTFDFLKENNYLPYPIHQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFVNSDYELTYNL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 308 KIKRDERTLINPDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEH 387
Cdd:cd14215 161 EKKRDERSVKSTAIRVVDFGSATFDHEHHSTIVSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNREH 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 388 LAMMERILGPLPKHMIQKTRKRKYFHHDRLDWDEHSSAGRYVSRRCKPLKEFMLSQDVEHERLFDLIQKMLEYDPAKRIT 467
Cdd:cd14215 241 LAMMERILGPIPSRMIRKTRKQKYFYHGRLDWDENTSAGRYVRENCKPLRRYLTSEAEEHHQLFDLIESMLEYEPSKRLT 320
                       330
                ....*....|
gi 67551261 468 LREALKHPFF 477
Cdd:cd14215 321 LAAALKHPFF 330
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
147-477 3.88e-173

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: 489.91  E-value: 3.88e-173
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 147 GHLICQSGDVLSARYEIVDTLGEGAFGKVVECIDHKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTDPNSTFRCVQ 226
Cdd:cd14214   1 GHLVCRIGDWLQERYEIVGDLGEGTFGKVVECLDHARGKSQVALKIIRNVGKYREAARLEINVLKKIKEKDKENKFLCVL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 227 MLEWFEHHGHICIVFELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYTEAYN 306
Cdd:cd14214  81 MSDWFNFHGHMCIAFELLGKNTFEFLKENNFQPYPLPHIRHMAYQLCHALKFLHENQLTHTDLKPENILFVNSEFDTLYN 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 307 PKIKRDERTLINPDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKE 386
Cdd:cd14214 161 ESKSCEEKSVKNTSIRVADFGSATFDHEHHTTIVATRHYRPPEVILELGWAQPCDVWSLGCILFEYYRGFTLFQTHENRE 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 387 HLAMMERILGPLPKHMIQKTRKRKYFHHDRLDWDEHSSAGRYVSRRCKPLKEFMLSQDVEHERLFDLIQKMLEYDPAKRI 466
Cdd:cd14214 241 HLVMMEKILGPIPSHMIHRTRKQKYFYKGSLVWDENSSDGRYVSENCKPLMSYMLGDSLEHTQLFDLLRRMLEFDPALRI 320
                       330
                ....*....|.
gi 67551261 467 TLREALKHPFF 477
Cdd:cd14214 321 TLKEALLHPFF 331
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
147-477 2.84e-102

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: 308.32  E-value: 2.84e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 147 GHLICQSGDVLSARYEIVDTLGEGAFGKVVECIDHKAGgRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTDPNSTFRCVQ 226
Cdd:cd14210   1 GDYKVVLGDHIAYRYEVLSVLGKGSFGQVVKCLDHKTG-QLVAIKIIRNKKRFHQQALVEVKILKHLNDNDPDDKHNIVR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 227 MLEWFEHHGHICIVFELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYTeayn 306
Cdd:cd14210  80 YKDSFIFRGHLCIVFELLSINLYELLKSNNFQGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSKS---- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 307 pkikrdertlinpDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKE 386
Cdd:cd14210 156 -------------SIKVIDFGSSCFEGEKVYTYIQSRFYRAPEVILGLPYDTAIDMWSLGCILAELYTGYPLFPGENEEE 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 387 HLAMMERILGPLPKHMIQK-TRKRKYFHHDRLDWDEHSSAGRYVSRRCKPLKEFMLSQDvehERLFDLIQKMLEYDPAKR 465
Cdd:cd14210 223 QLACIMEVLGVPPKSLIDKaSRRKKFFDSNGKPRPTTNSKGKKRRPGSKSLAQVLKCDD---PSFLDFLKKCLRWDPSER 299
                       330
                ....*....|..
gi 67551261 466 ITLREALKHPFF 477
Cdd:cd14210 300 MTPEEALQHPWI 311
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
161-477 4.15e-97

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: 292.99  E-value: 4.15e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIDHKAGgRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTDPnsTFRCVQMLEWFEHHG--HIC 238
Cdd:cd05118   1 YEVLRKIGEGAFGTVWLARDKVTG-EKVAIKKIKNDFRHPKAALREIKLLKHLNDVEG--HPNIVKLLDVFEHRGgnHLC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 239 IVFELLGLSTYDFIKENGfLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSdyteaynpkikrdertliN 318
Cdd:cd05118  78 LVFELMGMNLYELIKDYP-RGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLE------------------L 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 319 PDIKVVDFGSATYDDEH-HSTLVSTRHYRAPEVIL-ALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMMERILG 396
Cdd:cd05118 139 GQLKLADFGLARSFTSPpYTPYVATRWYRAPEVLLgAKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIVRLLG 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 397 PlpkhmiqktrkrkyfhhdrldwdehssagryvsrrckplkefmlsqdvehERLFDLIQKMLEYDPAKRITLREALKHPF 476
Cdd:cd05118 219 T--------------------------------------------------PEALDLLSKMLKYDPAKRITASQALAHPY 248

                .
gi 67551261 477 F 477
Cdd:cd05118 249 F 249
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
147-477 3.45e-84

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: 263.03  E-value: 3.45e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 147 GHLICQSGDVLSARYEIVDTLGEGAFGKVVECIDHKAGgRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTDPNSTFRCVQ 226
Cdd:cd14226   1 YDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDHVEQ-EWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTENKYYIVR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 227 MLEWFEHHGHICIVFELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLT--HTDLKPENILFVqsdytea 304
Cdd:cd14226  80 LKRHFMFRNHLCLVFELLSYNLYDLLRNTNFRGVSLNLTRKFAQQLCTALLFLSTPELSiiHCDLKPENILLC------- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 305 yNPKikrdeRTlinpDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDS 384
Cdd:cd14226 153 -NPK-----RS----AIKIIDFGSSCQLGQRIYQYIQSRFYRSPEVLLGLPYDLAIDMWSLGCILVEMHTGEPLFSGANE 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 385 KEHLAMMERILGPLPKHMIQKTRK-RKYF-HHDRLDW--DEHSSAGRYVSRRCKPLKEfMLSQD---------------- 444
Cdd:cd14226 223 VDQMNKIVEVLGMPPVHMLDQAPKaRKFFeKLPDGTYylKKTKDGKKYKPPGSRKLHE-ILGVEtggpggrragepghtv 301
                       330       340       350
                ....*....|....*....|....*....|...
gi 67551261 445 VEHERLFDLIQKMLEYDPAKRITLREALKHPFF 477
Cdd:cd14226 302 EDYLKFKDLILRMLDYDPKTRITPAEALQHSFF 334
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
161-477 4.90e-83

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: 257.20  E-value: 4.90e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIDHKAGgRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTDPNSTFRCVQMLEWFEHHGHICIV 240
Cdd:cd14133   1 YEVLEVLGKGTFGQVVKCYDLLTG-EEVALKIIKNNKDYLDQSLDEIRLLELLNKKDKADKYHIVRLKDVFYFKNHLCIV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 241 FELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVqsDYTEaynpkikrdertlinPD 320
Cdd:cd14133  80 FELLSQNLYEFLKQNKFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLA--SYSR---------------CQ 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 321 IKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMMERILGPLPK 400
Cdd:cd14133 143 IKIIDFGSSCFLTQRLYSYIQSRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGTIGIPPA 222
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 67551261 401 HMIqktrkrkyfhhdrldwdEHSSAGRyvsrrckplkefmlsqdvehERLFDLIQKMLEYDPAKRITLREALKHPFF 477
Cdd:cd14133 223 HML-----------------DQGKADD--------------------ELFVDFLKKLLEIDPKERPTASQALSHPWL 262
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
143-477 1.05e-79

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: 251.55  E-value: 1.05e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 143 DDEEGHLICQSGDVLSARYEIVDTLGEGAFGKVVECIDHKAGgRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTDPNSTF 222
Cdd:cd14225  27 DDENGSYLKVLHDHIAYRYEILEVIGKGSFGQVVKALDHKTN-EHVAIKIIRNKKRFHHQALVEVKILDALRRKDRDNSH 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 223 RCVQMLEWFEHHGHICIVFELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYT 302
Cdd:cd14225 106 NVIHMKEYFYFRNHLCITFELLGMNLYELIKKNNFQGFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQRGQS 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 303 eaynpkikrdertlinpDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTH 382
Cdd:cd14225 186 -----------------SIKVIDFGSSCYEHQRVYTYIQSRFYRSPEVILGLPYSMAIDMWSLGCILAELYTGYPLFPGE 248
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 383 DSKEHLAMMERILGPLPKHMIQKTRKRKYFhhdrldWDEH-------SSAGRYVSRRCKPLKEFMLSQDveheRLF-DLI 454
Cdd:cd14225 249 NEVEQLACIMEVLGLPPPELIENAQRRRLF------FDSKgnprcitNSKGKKRRPNSKDLASALKTSD----PLFlDFI 318
                       330       340
                ....*....|....*....|...
gi 67551261 455 QKMLEYDPAKRITLREALKHPFF 477
Cdd:cd14225 319 RRCLEWDPSKRMTPDEALQHEWI 341
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
161-477 8.44e-79

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 246.29  E-value: 8.44e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261    161 YEIVDTLGEGAFGKVVECIdHKAGGRHVAVKIVK--NVDRYCEAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHGHIC 238
Cdd:smart00220   1 YEILEKLGEGSFGKVYLAR-DKKTGKLVAIKVIKkkKIKKDRERILREIKILKKLK--HPN----IVRLYDVFEDEDKLY 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261    239 IVFELL-GLSTYDFIKENGFLPfrLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQsdyteaynpkikrdertli 317
Cdd:smart00220  74 LVMEYCeGGDLFDLLKKRGRLS--EDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDE------------------- 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261    318 NPDIKVVDFGSATY--DDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPthDSKEHLAMMERIL 395
Cdd:smart00220 133 DGHVKLADFGLARQldPGEKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFP--GDDQLLELFKKIG 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261    396 GPLPKhmiqktrkrkyfhhdrldwdehssagryvsrrcKPLKEFMLSQDveherLFDLIQKMLEYDPAKRITLREALKHP 475
Cdd:smart00220 211 KPKPP---------------------------------FPPPEWDISPE-----AKDLIRKLLVKDPEKRLTAEEALQHP 252

                   ..
gi 67551261    476 FF 477
Cdd:smart00220 253 FF 254
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
161-477 1.43e-74

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: 237.92  E-value: 1.43e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIDHKAGgRHVAVKIVKNVDRYCEAARSEIQVLEHLNTT-DPNSTFRCVQMLEWFEHHGHICI 239
Cdd:cd14212   1 YLVLDLLGQGTFGQVVKCQDLKTN-KLVAVKVLKNKPAYFRQAMLEIAILTLLNTKyDPEDKHHIVRLLDHFMHHGHLCI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 240 VFELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDyteaynpkikrdertliNP 319
Cdd:cd14212  80 VFELLGVNLYELLKQNQFRGLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNLD-----------------SP 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 320 DIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMMERILGPLP 399
Cdd:cd14212 143 EIKLIDFGSACFENYTLYTYIQSRFYRSPEVLLGLPYSTAIDMWSLGCIAAELFLGLPLFPGNSEYNQLSRIIEMLGMPP 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 400 KHMIQKTRK-RKYFHHDR---------------LDWDEHSSAG---RYVS-----------RRCKPLKEFMLSQDVEHER 449
Cdd:cd14212 223 DWMLEKGKNtNKFFKKVAksggrstyrlktpeeFEAENNCKLEpgkRYFKyktlediimnyPMKKSKKEQIDKEMETRLA 302
                       330       340
                ....*....|....*....|....*...
gi 67551261 450 LFDLIQKMLEYDPAKRITLREALKHPFF 477
Cdd:cd14212 303 FIDFLKGLLEYDPKKRWTPDQALNHPFI 330
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
143-476 4.64e-73

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: 235.80  E-value: 4.64e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 143 DDEEGHLICQSGDVLSARYEIVDTLGEGAFGKVVECIDHKAGgRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTDPNSTF 222
Cdd:cd14224  49 DDEQGSYIHVPHDHIAYRYEVLKVIGKGSFGQVVKAYDHKTH-QHVALKMVRNEKRFHRQAAEEIRILEHLKKQDKDNTM 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 223 RCVQMLEWFEHHGHICIVFELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqsdyt 302
Cdd:cd14224 128 NVIHMLESFTFRNHICMTFELLSMNLYELIKKNKFQGFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENIL------- 200
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 303 eaynpkIKRDERTlinpDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTH 382
Cdd:cd14224 201 ------LKQQGRS----GIKVIDFGSSCYEHQRIYTYIQSRFYRAPEVILGARYGMPIDMWSFGCILAELLTGYPLFPGE 270
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 383 DSKEHLAMMERILGPLPKHMIQKTRKRKYF----HHDRLDWDEHSSAGRYV-----SRRCK-----PLKEFMLSQDVEHE 448
Cdd:cd14224 271 DEGDQLACMIELLGMPPQKLLETSKRAKNFisskGYPRYCTVTTLPDGSVVlnggrSRRGKmrgppGSKDWVTALKGCDD 350
                       330       340
                ....*....|....*....|....*....
gi 67551261 449 RLF-DLIQKMLEYDPAKRITLREALKHPF 476
Cdd:cd14224 351 PLFlDFLKRCLEWDPAARMTPSQALRHPW 379
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
154-477 9.03e-67

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: 217.44  E-value: 9.03e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 154 GDVLSARYEIVDTLGEGAFGKVVECIDhKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTDPNSTFR--CVQMLEWF 231
Cdd:cd14136   5 GEVYNGRYHVVRKLGWGHFSTVWLCWD-LQNKRFVALKVVKSAQHYTEAALDEIKLLKCVREADPKDPGRehVVQLLDDF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 232 EHHG----HICIVFELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSN-KLTHTDLKPENILFVQSdyteayn 306
Cdd:cd14136  84 KHTGpngtHVCMVFEVLGPNLLKLIKRYNYRGIPLPLVKKIARQVLQGLDYLHTKcGIIHTDIKPENVLLCIS------- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 307 pkikrdertliNPDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSK- 385
Cdd:cd14136 157 -----------KIEVKIADLGNACWTDKHFTEDIQTRQYRSPEVILGAGYGTPADIWSTACMAFELATGDYLFDPHSGEd 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 386 -----EHLAMMERILGPLPKHMIQKTRK-RKYFHHdrldwdehssagRYVSRRCKPLKEFMLsQDV----------EHER 449
Cdd:cd14136 226 ysrdeDHLALIIELLGRIPRSIILSGKYsREFFNR------------KGELRHISKLKPWPL-EDVlvekykwskeEAKE 292
                       330       340
                ....*....|....*....|....*...
gi 67551261 450 LFDLIQKMLEYDPAKRITLREALKHPFF 477
Cdd:cd14136 293 FASFLLPMLEYDPEKRATAAQCLQHPWL 320
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
160-477 1.68e-62

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: 205.92  E-value: 1.68e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDHKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTDPNSTFRCVQMLEWFEHHGHICI 239
Cdd:cd14135   1 RYRVYGYLGKGVFSNVVRARDLARGNQEVAIKIIRNNELMHKAGLKELEILKKLNDADPDDKKHCIRLLRHFEHKNHLCL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 240 VFELLGLSTYDFIKENGF-LPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteaynpkikrDERTLIn 318
Cdd:cd14135  81 VFESLSMNLREVLKKYGKnVGLNIKAVRSYAQQLFLALKHLKKCNILHADIKPDNILV---------------NEKKNT- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 319 pdIKVVDFGSATYDDEHHST--LVStRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMMERILG 396
Cdd:cd14135 145 --LKLCDFGSASDIGENEITpyLVS-RFYRAPEIILGLPYDYPIDMWSVGCTLYELYTGKILFPGKTNNHMLKLMMDLKG 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 397 PLPKHMIQKTR-KRKYFHHDrLDW-----DEHS-----------SAGRYVSRRCKPLKEFMLSQDVEHERLFDLIQKMLE 459
Cdd:cd14135 222 KFPKKMLRKGQfKDQHFDEN-LNFiyrevDKVTkkevrrvmsdiKPTKDLKTLLIGKQRLPDEDRKKLLQLKDLLDKCLM 300
                       330
                ....*....|....*...
gi 67551261 460 YDPAKRITLREALKHPFF 477
Cdd:cd14135 301 LDPEKRITPNEALQHPFI 318
PTZ00284 PTZ00284
protein kinase; Provisional
145-476 1.22e-61

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 208.28  E-value: 1.22e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  145 EEGHLICQSG---DVLSARYEIVDTLGEGAFGKVVECIDHKAGgRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTDPNST 221
Cdd:PTZ00284 112 EEGHFYVVLGediDVSTQRFKILSLLGEGTFGKVVEAWDRKRK-EYCAVKIVRNVPKYTRDAKIEIQFMEKVRQADPADR 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  222 FRCVQMLEWFEHH-GHICIVFELLGLSTYDFIKENGflPFRLDHIRKMAYQICKSVNFLHSN-KLTHTDLKPENILFVQS 299
Cdd:PTZ00284 191 FPLMKIQRYFQNEtGHMCIVMPKYGPCLLDWIMKHG--PFSHRHLAQIIFQTGVALDYFHTElHLMHTDLKPENILMETS 268
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  300 DYTeaYNPKIKRDertlINPD---IKVVDFGSATydDEHHS--TLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYL 374
Cdd:PTZ00284 269 DTV--VDPVTNRA----LPPDpcrVRICDLGGCC--DERHSrtAIVSTRHYRSPEVVLGLGWMYSTDMWSMGCIIYELYT 340
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  375 GFTVFPTHDSKEHLAMMERILGPLPKHMIQK--TRKRKyfhhdrldwDEHSSAG--------RYVSR--RCKPLKEfMLS 442
Cdd:PTZ00284 341 GKLLYDTHDNLEHLHLMEKTLGRLPSEWAGRcgTEEAR---------LLYNSAGqlrpctdpKHLARiaRARPVRE-VIR 410
                        330       340       350
                 ....*....|....*....|....*....|....
gi 67551261  443 QDVeherLFDLIQKMLEYDPAKRITLREALKHPF 476
Cdd:PTZ00284 411 DDL----LCDLIYGLLHYDRQKRLNARQMTTHPY 440
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
160-476 1.45e-58

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: 193.85  E-value: 1.45e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIdHKAGGRHVAVKIV---KNVDRYCEAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHGH 236
Cdd:cd05117   1 KYELGKVLGRGSFGVVRLAV-HKKTGEEYAVKIIdkkKLKSEDEEMLRREIEILKRLD--HPN----IVKLYEVFEDDKN 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELL-GLSTYDFIKENGFlpFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDyteaynpkikrdert 315
Cdd:cd05117  74 LYLVMELCtGGELFDRIVKKGS--FSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKD--------------- 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 316 lINPDIKVVDFGSATY--DDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILieYYL--GFTVFPTHDSKEhlaMM 391
Cdd:cd05117 137 -PDSPIKIIDFGLAKIfeEGEKLKTVCGTPYYVAPEVLKGKGYGKKCDIWSLGVIL--YILlcGYPPFYGETEQE---LF 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 392 ERIlgplpkhmiqktrKRKYFHHDRLDWDEhssagryVSRRCKplkefmlsqdveherlfDLIQKMLEYDPAKRITLREA 471
Cdd:cd05117 211 EKI-------------LKGKYSFDSPEWKN-------VSEEAK-----------------DLIKRLLVVDPKKRLTAAEA 253

                ....*
gi 67551261 472 LKHPF 476
Cdd:cd05117 254 LNHPW 258
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
161-476 3.57e-54

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: 184.57  E-value: 3.57e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIdHKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTDPNStFRCVQMLEWFEHHGHICIV 240
Cdd:cd14211   1 YEVLEFLGRGTFGQVVKCW-KRGTNEIVAIKILKNHPSYARQGQIEVSILSRLSQENADE-FNFVRAYECFQHKNHTCLV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 241 FELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVqsdyteayNPkIKRDERtlinpd 320
Cdd:cd14211  79 FEMLEQNLYDFLKQNKFSPLPLKYIRPILQQVLTALLKLKSLGLIHADLKPENIMLV--------DP-VRQPYR------ 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 321 IKVVDFGSATYDDEH-HSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMMERILGPLP 399
Cdd:cd14211 144 VKVIDFGSASHVSKAvCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGSSEYDQIRYISQTQGLPA 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 400 KHMIQKTRKRKYF-----HHDRLDW-----DEHSS--------AGRYVSRRCKPLKEF----------MLSQDVEHERLF 451
Cdd:cd14211 224 EHLLNAATKTSRFfnrdpDSPYPLWrlktpEEHEAetgikskeARKYIFNCLDDMAQVngpsdlegseLLAEKADRREFI 303
                       330       340
                ....*....|....*....|....*
gi 67551261 452 DLIQKMLEYDPAKRITLREALKHPF 476
Cdd:cd14211 304 DLLKRMLTIDQERRITPGEALNHPF 328
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
161-476 3.47e-53

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: 182.15  E-value: 3.47e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECidHKAGGRH-VAVKIVKNVDRYCEAARSEIQVLEHLNTTDPNStFRCVQMLEWFEHHGHICI 239
Cdd:cd14229   2 YEVLDFLGRGTFGQVVKC--WKRGTNEiVAVKILKNHPSYARQGQIEVGILARLSNENADE-FNFVRAYECFQHRNHTCL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 240 VFELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVqsdyteayNPkIKRDERtlinp 319
Cdd:cd14229  79 VFEMLEQNLYDFLKQNKFSPLPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMLV--------DP-VRQPYR----- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 320 dIKVVDFGSATYDDEH-HSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMMERILGPL 398
Cdd:cd14229 145 -VKVIDFGSASHVSKTvCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGALEYDQIRYISQTQGLP 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 399 PKHMIQKTRKRKYFHHDRLD-----W-----DEHSSAGRYVSRRCKP-----LKEF-------------MLSQDVEHERL 450
Cdd:cd14229 224 GEQLLNVGTKTSRFFCRETDapyssWrlktlEEHEAETGMKSKEARKyifnsLDDIahvnmvmdlegsdLLAEKADRREF 303
                       330       340
                ....*....|....*....|....*.
gi 67551261 451 FDLIQKMLEYDPAKRITLREALKHPF 476
Cdd:cd14229 304 VALLKKMLLIDADLRITPADTLSHPF 329
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
160-480 5.68e-49

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: 169.61  E-value: 5.68e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDHKAGGRhVAVKIVKNVDRYCEaaRsEIQVLEHLNttDPNstfrCVQMLEWFEHHG---- 235
Cdd:cd14137   5 SYTIEKVIGSGSFGVVYQAKLLETGEV-VAIKKVLQDKRYKN--R-ELQIMRRLK--HPN----IVKLKYFFYSSGekkd 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 236 --HICIVFELLGLSTYDFIKE--NGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteaynpkikr 311
Cdd:cd14137  75 evYLNLVMEYMPETLYRVIRHysKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLV--------------- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 312 DERTLInpdIKVVDFGSATY--DDEHHSTLVSTRHYRAPEVIL-ALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHL 388
Cdd:cd14137 140 DPETGV---LKLCDFGSAKRlvPGEPNVSYICSRYYRAPELIFgATDYTTAIDIWSAGCVLAELLLGQPLFPGESSVDQL 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 389 AMMERILGPLPKHMIqktrkrKYFHHDRLDWdehssagRYVSRRCKPLKEFmLSQDVEHErLFDLIQKMLEYDPAKRITL 468
Cdd:cd14137 217 VEIIKVLGTPTREQI------KAMNPNYTEF-------KFPQIKPHPWEKV-FPKRTPPD-AIDLLSKILVYNPSKRLTA 281
                       330
                ....*....|..
gi 67551261 469 REALKHPFFDLL 480
Cdd:cd14137 282 LEALAHPFFDEL 293
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
157-479 5.93e-49

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: 171.81  E-value: 5.93e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 157 LSARYEIVDTLGEGAFGKVVECIDhKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTDPNStFRCVQMLEWFEHHGH 236
Cdd:cd14227  13 MTNTYEVLEFLGRGTFGQVVKCWK-RGTNEIVAIKILKNHPSYARQGQIEVSILARLSTESADD-YNFVRAYECFQHKNH 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDyTEAYNpkikrdertl 316
Cdd:cd14227  91 TCLVFEMLEQNLYDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPS-RQPYR---------- 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 317 inpdIKVVDFGSATYDDEH-HSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMMERIL 395
Cdd:cd14227 160 ----VKVIDFGSASHVSKAvCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQ 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 396 GPLPKHMIQK-TRKRKYFHHD--------RLDW-DEHSS--------AGRYVSRRCKPLKEFMLSQDVE----------H 447
Cdd:cd14227 236 GLPAEYLLSAgTKTTRFFNRDtdspyplwRLKTpEDHEAetgikskeARKYIFNCLDDMAQVNMTTDLEgsdmlvekadR 315
                       330       340       350
                ....*....|....*....|....*....|..
gi 67551261 448 ERLFDLIQKMLEYDPAKRITLREALKHPFFDL 479
Cdd:cd14227 316 REFIDLLKKMLTIDADKRITPIETLNHPFVTM 347
STKc_SRPK1 cd14216
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs ...
154-477 1.23e-48

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK1 binds with high affinity the alternative splicing factor, SRSF1 (serine/arginine-rich splicing factor 1), and regiospecifically phosphorylates 10-12 serines in its RS domain. It plays a role in the regulation of pre-mRNA splicing, chromatin structure, and germ cell development. 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. 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: 271118 [Multi-domain]  Cd Length: 349  Bit Score: 170.60  E-value: 1.23e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 154 GDVLSARYEIVDTLGEGAFGKVVECIDHKaGGRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTDPNSTFR--CVQMLEWF 231
Cdd:cd14216   5 GDLFNGRYHVIRKLGWGHFSTVWLSWDIQ-GKRFVAMKVVKSAEHYTETALDEIKLLKSVRNSDPNDPNRemVVQLLDDF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 232 EHHG----HICIVFELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSN-KLTHTDLKPENILF-VQSDYTEAY 305
Cdd:cd14216  84 KISGvngtHICMVFEVLGHHLLKWIIKSNYQGLPLPCVKKIIRQVLQGLDYLHTKcRIIHTDIKPENILLsVNEQYIRRL 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 306 NPKIKRDERT-LINP---------DIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLG 375
Cdd:cd14216 164 AAEATEWQRNfLVNPlepknaeklKVKIADLGNACWVHKHFTEDIQTRQYRSLEVLIGSGYNTPADIWSTACMAFELATG 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 376 FTVFPTHDSKE------HLAMMERILGPLPKHMIQKTRKRKYFHHDRLDWdehssagRYVSrRCKP-------LKEFMLS 442
Cdd:cd14216 244 DYLFEPHSGEDysrdedHIALIIELLGKVPRKLIVAGKYSKEFFTKKGDL-------KHIT-KLKPwglfevlVEKYEWS 315
                       330       340       350
                ....*....|....*....|....*....|....*
gi 67551261 443 QDvEHERLFDLIQKMLEYDPAKRITLREALKHPFF 477
Cdd:cd14216 316 QE-EAAGFTDFLLPMLELIPEKRATAAECLRHPWL 349
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
160-477 2.23e-48

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: 167.88  E-value: 2.23e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECiDHKAGGRHVAVKIVKNVDRYCEAARS---EIQVLEHLNttDPNstfrCVQMLEWFEHHGH 236
Cdd:cd07833   2 KYEVLGVVGEGAYGVVLKC-RNKATGEIVAIKKFKESEDDEDVKKTalrEVKVLRQLR--HEN----IVNLKEAFRRKGR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELLGLSTYDFIKE--NGFLPfrlDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrder 314
Cdd:cd07833  75 LYLVFEYVERTLLELLEAspGGLPP---DAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGV------------- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 315 tlinpdIKVVDFGSATY----DDEHHSTLVSTRHYRAPEVIL-ALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLA 389
Cdd:cd07833 139 ------LKLCDFGFARAltarPASPLTDYVATRWYRAPELLVgDTNYGKPVDVWAIGCIMAELLDGEPLFPGDSDIDQLY 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 390 MMERILGPLPKHMIQKTRKRKYFHHDRLDWDEH--SSAGRYvsrRCKPlkefmlsqdveHERLFDLIQKMLEYDPAKRIT 467
Cdd:cd07833 213 LIQKCLGPLPPSHQELFSSNPRFAGVAFPEPSQpeSLERRY---PGKV-----------SSPALDFLKACLRMDPKERLT 278
                       330
                ....*....|
gi 67551261 468 LREALKHPFF 477
Cdd:cd07833 279 CDELLQHPYF 288
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
157-479 6.09e-46

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: 163.72  E-value: 6.09e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 157 LSARYEIVDTLGEGAFGKVVECIDhKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTDPNStFRCVQMLEWFEHHGH 236
Cdd:cd14228  13 MTNSYEVLEFLGRGTFGQVAKCWK-RSTKEIVAIKILKNHPSYARQGQIEVSILSRLSSENADE-YNFVRSYECFQHKNH 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSdyteaynpkIKRDERtl 316
Cdd:cd14228  91 TCLVFEMLEQNLYDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDP---------VRQPYR-- 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 317 inpdIKVVDFGSATYDDEH-HSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMMERIL 395
Cdd:cd14228 160 ----VKVIDFGSASHVSKAvCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQ 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 396 GPLPKHMIQK-TRKRKYFHHD--------RLDW-DEHS--------SAGRYVSRRCKPLKEFMLSQDVE----------H 447
Cdd:cd14228 236 GLPAEYLLSAgTKTSRFFNRDpnlgyplwRLKTpEEHEletgikskEARKYIFNCLDDMAQVNMSTDLEgtdmlaekadR 315
                       330       340       350
                ....*....|....*....|....*....|..
gi 67551261 448 ERLFDLIQKMLEYDPAKRITLREALKHPFFDL 479
Cdd:cd14228 316 REYIDLLKKMLTIDADKRITPLKTLNHPFVTM 347
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
161-477 4.90e-45

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: 158.85  E-value: 4.90e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIDHKAGGRhVAVKIVKNvdRY-----CEAARsEIQVLEHLNTtDPNstfrCVQMLEWFEHHG 235
Cdd:cd07830   1 YKVIKQLGDGTFGSVYLARNKETGEL-VAIKKMKK--KFysweeCMNLR-EVKSLRKLNE-HPN----IVKLKEVFREND 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 236 HICIVFELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfVQSDYTeaynpkikrdert 315
Cdd:cd07830  72 ELYFVFEYMEGNLYQLMKDRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLL-VSGPEV------------- 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 316 linpdIKVVDFGSA-------TYDDehhstLVSTRHYRAPEVILALGW-SQPCDVWSIGCILIEYYLGFTVFPTHDSKEH 387
Cdd:cd07830 138 -----VKIADFGLAreirsrpPYTD-----YVSTRWYRAPEILLRSTSySSPVDIWALGCIMAELYTLRPLFPGSSEIDQ 207
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 388 LAMMERILGPlPKHMiqktrkrkyfhhdrlDWDEH---SSAGRYVSRRCKPLKEFMLSQDVEHErLFDLIQKMLEYDPAK 464
Cdd:cd07830 208 LYKICSVLGT-PTKQ---------------DWPEGyklASKLGFRFPQFAPTSLHQLIPNASPE-AIDLIKDMLRWDPKK 270
                       330
                ....*....|...
gi 67551261 465 RITLREALKHPFF 477
Cdd:cd07830 271 RPTASQALQHPYF 283
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
161-477 5.60e-45

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: 158.98  E-value: 5.60e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIDhKAGGRHVAVKIVK---NVDRYCEAARSEIQVLEHLNTTD-PNstfrCVQMLEWF----- 231
Cdd:cd07838   1 YEEVAEIGEGAYGTVYKARD-LQDGRFVALKKVRvplSEEGIPLSTIREIALLKQLESFEhPN----VVRLLDVChgprt 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 232 EHHGHICIVFELL--GLSTY-DFIKENGFLPfrlDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqsdyteaynpk 308
Cdd:cd07838  76 DRELKLTLVFEHVdqDLATYlDKCPKPGLPP---ETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNIL------------- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 309 IKRDERtlinpdIKVVDFGSA-TYDDEHHSTL-VSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKE 386
Cdd:cd07838 140 VTSDGQ------VKLADFGLArIYSFEMALTSvVVTLWYRAPEVLLQSSYATPVDMWSVGCIFAELFNRRPLFRGSSEAD 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 387 HLAMMERILGPLPKHmiqktrkrkyfhhdrlDWDEHSSAGR--YVSRRCKPLKEFMLSQDVEHErlfDLIQKMLEYDPAK 464
Cdd:cd07838 214 QLGKIFDVIGLPSEE----------------EWPRNSALPRssFPSYTPRPFKSFVPEIDEEGL---DLLKKMLTFNPHK 274
                       330
                ....*....|...
gi 67551261 465 RITLREALKHPFF 477
Cdd:cd07838 275 RISAFEALQHPYF 287
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
160-478 1.73e-44

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: 158.84  E-value: 1.73e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDhKAGGRHVAVKIVKNVDR---YCEAARSEIQVLEHLN-----------TTDPNSTFRcv 225
Cdd:cd07834   1 RYELLKPIGSGAYGVVCSAYD-KRTGRKVAIKKISNVFDdliDAKRILREIKILRHLKheniiglldilRPPSPEEFN-- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 226 qmlewfehhgHICIVFELLGLSTYDFIKENGFLpfRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqsdyteay 305
Cdd:cd07834  78 ----------DVYIVTELMETDLHKVIKSPQPL--TDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNIL---------- 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 306 npkIKRDErtlinpDIKVVDFGSATYDDEHHSTL-----VSTRHYRAPEVIL-ALGWSQPCDVWSIGCILIEYYLGFTVF 379
Cdd:cd07834 136 ---VNSNC------DLKICDFGLARGVDPDEDKGflteyVVTRWYRAPELLLsSKKYTKAIDIWSVGCIFAELLTRKPLF 206
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 380 PTHDskeHLAMMERILGPLPKhmiqktrkrkyFHHDRLDWDEHSSAGRYV----SRRCKPLKEFMlsqDVEHERLFDLIQ 455
Cdd:cd07834 207 PGRD---YIDQLNLIVEVLGT-----------PSEEDLKFISSEKARNYLkslpKKPKKPLSEVF---PGASPEAIDLLE 269
                       330       340
                ....*....|....*....|...
gi 67551261 456 KMLEYDPAKRITLREALKHPFFD 478
Cdd:cd07834 270 KMLVFNPKKRITADEALAHPYLA 292
STKc_SRPK3 cd14218
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs ...
152-477 5.73e-44

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK3 is highly expressed in the heart and skeletal muscles, and is controlled by a muscle-specific enhancer that is regulated by MEF2. It may play an important role in muscle development. 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. 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: 271120 [Multi-domain]  Cd Length: 365  Bit Score: 158.64  E-value: 5.73e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 152 QSGDVLSARYEIVDTLGEGAFGKVVECIDHKAGgRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTDPNSTFR--CVQMLE 229
Cdd:cd14218   3 KIGDLFNGRYHVVRKLGWGHFSTVWLCWDIQRK-RFVALKVVKSAVHYTETAVDEIKLLKCVRDSDPSDPKRetIVQLID 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 230 WFEHHG----HICIVFELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSN-KLTHTDLKPENILFVQSD---- 300
Cdd:cd14218  82 DFKISGvngvHVCMVLEVLGHQLLKWIIKSNYQGLPLPCVKSILRQVLQGLDYLHTKcKIIHTDIKPENILMCVDEgyvr 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 301 --------YTEAYNPKIKRDERT------LINP---------DIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWS 357
Cdd:cd14218 162 rlaaeatiWQQAGAPPPSGSSVSfgasdfLVNPlepqnadkiRVKIADLGNACWVHKHFTEDIQTRQYRALEVLIGAEYG 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 358 QPCDVWSIGCILIEYYLGFTVFPTHD------SKEHLAMMERILGPLPKHMIQKTR-KRKYFHHdrldwdehssagRYVS 430
Cdd:cd14218 242 TPADIWSTACMAFELATGDYLFEPHSgedytrDEDHIAHIVELLGDIPPHFALSGRySREYFNR------------RGEL 309
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 67551261 431 RRCKPLKEFMLSQDV---------EHERLFDLIQKMLEYDPAKRITLREALKHPFF 477
Cdd:cd14218 310 RHIKNLKHWGLYEVLvekyewpleQAAQFTDFLLPMMEFLPEKRATAAQCLQHPWL 365
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
161-477 3.85e-43

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: 153.79  E-value: 3.85e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIDhKAGGRHVAVKIVKNVDRY----CEAARsEIQVLEHLNttDPNstfrCVQMLEWFEHHGH 236
Cdd:cd07829   1 YEKLEKLGEGTYGVVYKAKD-KKTGEIVALKKIRLDNEEegipSTALR-EISLLKELK--HPN----IVKLLDVIHTENK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELLGLSTYDFIKENGfLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENIlfvqsdyteaynpkikrdertL 316
Cdd:cd07829  73 LYLVFEYCDQDLKKYLDKRP-GPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNL---------------------L 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 317 INPD--IKVVDFGSA--------TYDDEhhstlVSTRHYRAPEVIL-ALGWSQPCDVWSIGCILIEYYLGFTVFPThDSK 385
Cdd:cd07829 131 INRDgvLKLADFGLArafgiplrTYTHE-----VVTLWYRAPEILLgSKHYSTAVDIWSVGCIFAELITGKPLFPG-DSE 204
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 386 EH-LAMMERILG-PLPKhmiqktrkrkyfhhdrlDWDEHSSAGRYVSR----RCKPLKEFMLSQDvehERLFDLIQKMLE 459
Cdd:cd07829 205 IDqLFKIFQILGtPTEE-----------------SWPGVTKLPDYKPTfpkwPKNDLEKVLPRLD---PEGIDLLSKMLQ 264
                       330
                ....*....|....*...
gi 67551261 460 YDPAKRITLREALKHPFF 477
Cdd:cd07829 265 YNPAKRISAKEALKHPYF 282
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
160-476 8.50e-43

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: 152.63  E-value: 8.50e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDhKAGGRHVAVKI-----VKNVDRYCEAARSEIQVLEHLNTTdpnstfRCVQMLEWFEHH 234
Cdd:cd14098   1 KYQIIDRLGSGTFAEVKKAVE-VETGKMRAIKQivkrkVAGNDKNLQLFQREINILKSLEHP------GIVRLIDWYEDD 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 235 GHICIVFELL-GLSTYDFIKENGFLPfrLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDyteaynPKIkrde 313
Cdd:cd14098  74 QHIYLVMEYVeGGDLMDFIMAWGAIP--EQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDD------PVI---- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 314 rtlinpdIKVVDFGSA--TYDDEHHSTLVSTRHYRAPEVILAL------GWSQPCDVWSIGCILieyYLGFTVFPTHDSK 385
Cdd:cd14098 142 -------VKISDFGLAkvIHTGTFLVTFCGTMAYLAPEILMSKeqnlqgGYSNLVDMWSVGCLV---YVMLTGALPFDGS 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 386 EHLAMMERIlgplpkhmiqktrkrkyfhhdrldwdehsSAGRYVSrrcKPLKEFMLSQDVeherlFDLIQKMLEYDPAKR 465
Cdd:cd14098 212 SQLPVEKRI-----------------------------RKGRYTQ---PPLVDFNISEEA-----IDFILRLLDVDPEKR 254
                       330
                ....*....|.
gi 67551261 466 ITLREALKHPF 476
Cdd:cd14098 255 MTAAQALDHPW 265
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
161-477 2.01e-42

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: 152.04  E-value: 2.01e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIDHKAGgRHVAVKIVKNVDRYCEAARS--EIQVLEHLnTTDPNstfrCVQMLEWF--EHHGH 236
Cdd:cd07831   1 YKILGKIGEGTFSEVLKAQSRKTG-KYYAIKCMKKHFKSLEQVNNlrEIQALRRL-SPHPN----ILRLIEVLfdRKTGR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELLGLSTYDFIKeNGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqsdyteaynpkIKRDErtl 316
Cdd:cd07831  75 LALVFELMDMNLYELIK-GRKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENIL-------------IKDDI--- 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 317 inpdIKVVDFGSA--TYDDEHHSTLVSTRHYRAPEVILALGWSQP-CDVWSIGCILIEYYLGFTVFPTHDSKEHLAMMER 393
Cdd:cd07831 138 ----LKLADFGSCrgIYSKPPYTEYISTRWYRAPECLLTDGYYGPkMDIWAVGCVFFEILSLFPLFPGTNELDQIAKIHD 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 394 ILGpLPKHMIQKtRKRKYFHhdrLDWDEHSSAGRYVSRrckplkefmLSQDVEHERLfDLIQKMLEYDPAKRITLREALK 473
Cdd:cd07831 214 VLG-TPDAEVLK-KFRKSRH---MNYNFPSKKGTGLRK---------LLPNASAEGL-DLLKKLLAYDPDERITAKQALR 278

                ....
gi 67551261 474 HPFF 477
Cdd:cd07831 279 HPYF 282
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
157-477 3.03e-41

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: 150.21  E-value: 3.03e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 157 LSARYEIVDTLGEGAFGKVVECIDHKAGgRHVAVK-IVKNVDRYCEAARS--EIQVLEHLNttDPN-----STFRCVQML 228
Cdd:cd07855   3 VGDRYEPIETIGSGAYGVVCSAIDTKSG-QKVAIKkIPNAFDVVTTAKRTlrELKILRHFK--HDNiiairDILRPKVPY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 229 EWFEHhghICIVFELLGLSTYDFIKENGflPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqsdyteaynpk 308
Cdd:cd07855  80 ADFKD---VYVVLDLMESDLHHIIHSDQ--PLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLL------------- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 309 ikrdertlINPD--IKVVDFGSA----TYDDEHHSTL---VSTRHYRAPEVILALG-WSQPCDVWSIGCILIEYYLGFTV 378
Cdd:cd07855 142 --------VNENceLKIGDFGMArglcTSPEEHKYFMteyVATRWYRAPELMLSLPeYTQAIDMWSVGCIFAEMLGRRQL 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 379 FPTHDSKEHLAMMERILGPLPKHMIQKT---RKRKYF----HHDRLDWDEhssagRYVSRRCKPLkefmlsqdveherlf 451
Cdd:cd07855 214 FPGKNYVHQLQLILTVLGTPSQAVINAIgadRVRRYIqnlpNKQPVPWET-----LYPKADQQAL--------------- 273
                       330       340
                ....*....|....*....|....*.
gi 67551261 452 DLIQKMLEYDPAKRITLREALKHPFF 477
Cdd:cd07855 274 DLLSQMLRFDPSERITVAEALQHPFL 299
Pkinase pfam00069
Protein kinase domain;
161-477 9.45e-41

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 145.46  E-value: 9.45e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261   161 YEIVDTLGEGAFGKVVECIdHKAGGRHVAVKIVKNVDR---YCEAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHGHI 237
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAK-HRDTGKIVAIKKIKKEKIkkkKDKNILREIKILKKLN--HPN----IVRLYDAFEDKDNL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261   238 CIVFELL-GLSTYDFIKENGFLPfrLDHIRKMAYQICKSVNflHSNKLThtdlkpenilfvqsdyteaynpkikrdertl 316
Cdd:pfam00069  74 YLVLEYVeGGSLFDLLSEKGAFS--EREAKFIMKQILEGLE--SGSSLT------------------------------- 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261   317 inpdikvvdfgsatyddehhsTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMMERILG 396
Cdd:pfam00069 119 ---------------------TFVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPY 177
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261   397 PLPKHmiqktrkrkyfhhdrldWDEHSSAGRyvsrrckplkefmlsqdveherlfDLIQKMLEYDPAKRITLREALKHPF 476
Cdd:pfam00069 178 AFPEL-----------------PSNLSEEAK------------------------DLLKKLLKKDPSKRLTATQALQHPW 216

                  .
gi 67551261   477 F 477
Cdd:pfam00069 217 F 217
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
160-477 1.14e-40

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: 147.72  E-value: 1.14e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDHKAGgRHVAVKIVKNVDRYCEA------ARSEIQVLEHLNttDPNstfrCVQMLEWFEH 233
Cdd:cd07841   1 RYEKGKKLGEGTYAVVYKARDKETG-RIVAIKKIKLGERKEAKdginftALREIKLLQELK--HPN----IIGLLDVFGH 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 234 HGHICIVFELLGlstYDF--IKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqsdyteaynpkikr 311
Cdd:cd07841  74 KSNINLVFEFME---TDLekVIKDKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLL---------------- 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 312 dertlINPD--IKVVDFGSAT---YDDEHHSTLVSTRHYRAPEviLALGWSQ---PCDVWSIGCILIEYYLGFTVFPTHD 383
Cdd:cd07841 135 -----IASDgvLKLADFGLARsfgSPNRKMTHQVVTRWYRAPE--LLFGARHygvGVDMWSVGCIFAELLLRVPFLPGDS 207
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 384 SKEHLAMMERILG-PLPKhmiqktrkrkyfhhdrlDWDEHSSAGRYV---SRRCKPLKEF--MLSQDveherLFDLIQKM 457
Cdd:cd07841 208 DIDQLGKIFEALGtPTEE-----------------NWPGVTSLPDYVefkPFPPTPLKQIfpAASDD-----ALDLLQRL 265
                       330       340
                ....*....|....*....|
gi 67551261 458 LEYDPAKRITLREALKHPFF 477
Cdd:cd07841 266 LTLNPNKRITARQALEHPYF 285
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
160-477 3.96e-40

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: 145.93  E-value: 3.96e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIdHKAGGRHVAVKIVKNV---DRYCEAARSEIQVLEHLNTTdPNstfrCVQMLEWFEHHGH 236
Cdd:cd07832   1 RYKILGRIGEGAHGIVFKAK-DRETGETVALKKVALRkleGGIPNQALREIKALQACQGH-PY----VVKLRDVFPHGTG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELLGLSTYDFIKeNGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDyteaynpkikrdertl 316
Cdd:cd07832  75 FVLVFEYMLSSLSEVLR-DEERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTG---------------- 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 317 inpDIKVVDFGSATY----DDEHHSTLVSTRHYRAPEVIL-ALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMM 391
Cdd:cd07832 138 ---VLKIADFGLARLfseeDPRLYSHQVATRWYRAPELLYgSRKYDEGVDLWAVGCIFAELLNGSPLFPGENDIEQLAIV 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 392 ERILG-PLPKhmiqktrkrkyfhhdrlDWDEHSSAGRYVSRRCKPLKEFMLSQDV--EHERLFDLIQKMLEYDPAKRITL 468
Cdd:cd07832 215 LRTLGtPNEK-----------------TWPELTSLPDYNKITFPESKGIRLEEIFpdCSPEAIDLLKGLLVYNPKKRLSA 277

                ....*....
gi 67551261 469 REALKHPFF 477
Cdd:cd07832 278 EEALRHPYF 286
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
160-476 5.70e-40

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: 144.58  E-value: 5.70e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIdHKAGGRHVAVKIV---KNVDRYCEAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHGH 236
Cdd:cd14003   1 NYELGKTLGEGSFGKVKLAR-HKLTGEKVAIKIIdksKLKEEIEEKIKREIEIMKLLN--HPN----IIKLYEVIETENK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELL-GLSTYDFIKENGflPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteaynpkikrDErt 315
Cdd:cd14003  74 IYLVMEYAsGGELFDYIVNNG--RLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILL---------------DK-- 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 316 liNPDIKVVDFGSAT--YDDEHHSTLVSTRHYRAPEVILALGW-SQPCDVWSIGCILieYYLGFTVFPTHDSKEhlamme 392
Cdd:cd14003 135 --NGNLKIIDFGLSNefRGGSLLKTFCGTPAYAAPEVLLGRKYdGPKADVWSLGVIL--YAMLTGYLPFDDDND------ 204
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 393 rilgplpKHMIQKTRKRKYFHHdrldwdehssagRYVSRRCKplkefmlsqdveherlfDLIQKMLEYDPAKRITLREAL 472
Cdd:cd14003 205 -------SKLFRKILKGKYPIP------------SHLSPDAR-----------------DLIRRMLVVDPSKRITIEEIL 248

                ....
gi 67551261 473 KHPF 476
Cdd:cd14003 249 NHPW 252
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
160-477 1.26e-39

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: 144.75  E-value: 1.26e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECiDHKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTDPNSTfrcVQMLEWFEHHGHICI 239
Cdd:cd07848   2 KFEVLGVVGEGAYGVVLKC-RHKETKEIVAIKKFKDSEENEEVKETTLRELKMLRTLKQENI---VELKEAFRRRGKLYL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 240 VFELLGLSTYDFIKE--NGFLPfrlDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrdertli 317
Cdd:cd07848  78 VFEYVEKNMLELLEEmpNGVPP---EKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDV---------------- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 318 npdIKVVDFGSATY----DDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMMER 393
Cdd:cd07848 139 ---LKLCDFGFARNlsegSNANYTEYVATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQPLFPGESEIDQLFTIQK 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 394 ILGPLPKHMIQKTRKRKYFHHDRLDWDEHSSAgryVSRRckplkefmlSQDVEHERLFDLIQKMLEYDPAKRITLREALK 473
Cdd:cd07848 216 VLGPLPAEQMKLFYSNPRFHGLRFPAVNHPQS---LERR---------YLGILSGVLLDLMKNLLKLNPTDRYLTEQCLN 283

                ....
gi 67551261 474 HPFF 477
Cdd:cd07848 284 HPAF 287
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
160-477 1.06e-37

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: 140.95  E-value: 1.06e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDHKAGGRHVAVKIVKNVDRYCEAARS--EIQVLEHLNTTDPNSTFRCVQMLEWFEHHGHI 237
Cdd:cd07877  18 RYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSIIHAKRTyrELRLLKHMKHENVIGLLDVFTPARSLEEFNDV 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 238 CIVFELLGLSTYDFIKENGFLPfrlDHIRKMAYQICKSVNFLHSNKLTHTDLKPENiLFVQSDYteaynpkikrdertli 317
Cdd:cd07877  98 YLVTHLMGADLNNIVKCQKLTD---DHVQFLIYQILRGLKYIHSADIIHRDLKPSN-LAVNEDC---------------- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 318 npDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILA-LGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMMERILG 396
Cdd:cd07877 158 --ELKILDFGLARHTDDEMTGYVATRWYRAPEIMLNwMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVG 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 397 PLPKHMIQKTRKRkyfhhdrldwdehsSAGRYVSRRCK-PLKEFmlsQDV---EHERLFDLIQKMLEYDPAKRITLREAL 472
Cdd:cd07877 236 TPGAELLKKISSE--------------SARNYIQSLTQmPKMNF---ANVfigANPLAVDLLEKMLVLDSDKRITAAQAL 298

                ....*
gi 67551261 473 KHPFF 477
Cdd:cd07877 299 AHAYF 303
STKc_SRPK2 cd14217
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 2; STKs ...
154-477 2.75e-37

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK2 mediates neuronal cell cycle and cell death through regulation of nuclear cyclin D1. It has also been found to promote leukemia cell proliferation by regulating cyclin A1. SRPK2 also plays a role in regulating pre-mRNA splicing and is required for spliceosomal B complex formation. 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. 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: 271119 [Multi-domain]  Cd Length: 366  Bit Score: 140.55  E-value: 2.75e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 154 GDVLSARYEIVDTLGEGAFGKVVECIDHKaGGRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTDPNSTFR--CVQMLEWF 231
Cdd:cd14217   7 GDLFNGRYHVIRKLGWGHFSTVWLCWDMQ-GKRFVAMKVVKSAQHYTETALDEIKLLRCVRESDPEDPNKdmVVQLIDDF 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 232 EHHG----HICIVFELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSN-KLTHTDLKPENILFVQSD------ 300
Cdd:cd14217  86 KISGmngiHVCMVFEVLGHHLLKWIIKSNYQGLPIRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMCVDDayvrrm 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 301 ------YTEAYNP-----KIKRDERTLINP---------DIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPC 360
Cdd:cd14217 166 aaeateWQKAGAPppsgsAVSTAPDLLVNPldprnadkiRVKIADLGNACWVHKHFTEDIQTRQYRSIEVLIGAGYSTPA 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 361 DVWSIGCILIEYYLGFTVFPTHD------SKEHLAMMERILGPLPKHMIQKTRKRKYFHHDRLDWdehssagRYVSrRCK 434
Cdd:cd14217 246 DIWSTACMAFELATGDYLFEPHSgedysrDEDHIAHIIELLGCIPRHFALSGKYSREFFNRRGEL-------RHIT-KLK 317
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 67551261 435 PLKEFML--------SQDVEHerLFDLIQKMLEYDPAKRITLREALKHPFF 477
Cdd:cd14217 318 PWSLFDVlvekygwpHEDAAQ--FTDFLIPMLEMVPEKRASAGECLRHPWL 366
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
157-476 4.03e-37

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: 139.36  E-value: 4.03e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 157 LSARYEIVDTLGEGAFGKVVECIDHKAGGRhVAVKIVKNVDR--YCEAARSEIQVLEHLNTTDPNStFRCVQMLEWFEHH 234
Cdd:cd07849   3 VGPRYQNLSYIGEGAYGMVCSAVHKPTGQK-VAIKKISPFEHqtYCLRTLREIKILLRFKHENIIG-ILDIQRPPTFESF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 235 GHICIVFELLGLSTYDFIKENgflPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteayNPkikrder 314
Cdd:cd07849  81 KDVYIVQELMETDLYKLIKTQ---HLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLL---------NT------- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 315 tliNPDIKVVDFG---SATYDDEHHSTL---VSTRHYRAPEVILAL-GWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEH 387
Cdd:cd07849 142 ---NCDLKICDFGlarIADPEHDHTGFLteyVATRWYRAPEIMLNSkGYTKAIDIWSVGCILAEMLSNRPLFPGKDYLHQ 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 388 LAMMERILGplPKHM-----IQKTRKRKYF----HHDRLDWDE----HSSAGryvsrrckplkefmlsqdveherlFDLI 454
Cdd:cd07849 219 LNLILGILG--TPSQedlncIISLKARNYIkslpFKPKVPWNKlfpnADPKA------------------------LDLL 272
                       330       340
                ....*....|....*....|..
gi 67551261 455 QKMLEYDPAKRITLREALKHPF 476
Cdd:cd07849 273 DKMLTFNPHKRITVEEALAHPY 294
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
167-475 5.39e-37

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: 135.48  E-value: 5.39e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIDhKAGGRHVAVKIVK--NVDRYCEAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHGHICIVFELL 244
Cdd:cd00180   1 LGKGSFGKVYKARD-KETGKKVAVKVIPkeKLKKLLEELLREIEILKKLN--HPN----IVKLYDVFETENFLYLVMEYC 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 245 GLST-YDFIKENGFlPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqsdyteaynpkIKRDERtlinpdIKV 323
Cdd:cd00180  74 EGGSlKDLLKENKG-PLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENIL-------------LDSDGT------VKL 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 324 VDFGSATYDDEHHSTLV-----STRHYRAPEVILALGWSQPCDVWSIGCILIEyylgftvfpthdskehlamMERILgpl 398
Cdd:cd00180 134 ADFGLAKDLDSDDSLLKttggtTPPYYAPPELLGGRYYGPKVDIWSLGVILYE-------------------LEELK--- 191
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 67551261 399 pkhmiqktrkrkyfhhdrldwdehssagryvsrrckplkefmlsqdveherlfDLIQKMLEYDPAKRITLREALKHP 475
Cdd:cd00180 192 -----------------------------------------------------DLIRRMLQYDPKKRPSAKELLEHL 215
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
160-477 5.04e-36

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: 136.15  E-value: 5.04e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDHKAGgRHVAVKivKNVDryceAARseiqvlehlNTTDPNSTFRCVQMLEWFEHHGHIC- 238
Cdd:cd07852   8 RYEILKKLGKGAYGIVWKAIDKKTG-EVVALK--KIFD----AFR---------NATDAQRTFREIMFLQELNDHPNIIk 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 239 --------------IVFELLGLSTYDFIKENGFLPfrlDHIRKMAYQICKSVNFLHSNKLTHTDLKPENIlfvqsdytea 304
Cdd:cd07852  72 llnviraendkdiyLVFEYMETDLHAVIRANILED---IHKQYIMYQLLKALKYLHSGGVIHRDLKPSNI---------- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 305 ynpkikrdertLINPD--IKVVDFG-----SATYDDEHHSTL---VSTRHYRAPEVILA-LGWSQPCDVWSIGCILIEYY 373
Cdd:cd07852 139 -----------LLNSDcrVKLADFGlarslSQLEEDDENPVLtdyVATRWYRAPEILLGsTRYTKGVDMWSVGCILGEML 207
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 374 LGFTVFPTHDSkehLAMMERILGPLPKHMIQktrkrkyfhhDRLDWDEHSSAG---RYVSRRCKPLKEFMLSQDVEherL 450
Cdd:cd07852 208 LGKPLFPGTST---LNQLEKIIEVIGRPSAE----------DIESIQSPFAATmleSLPPSRPKSLDELFPKASPD---A 271
                       330       340
                ....*....|....*....|....*..
gi 67551261 451 FDLIQKMLEYDPAKRITLREALKHPFF 477
Cdd:cd07852 272 LDLLKKLLVFNPNKRLTAEEALRHPYV 298
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
161-477 8.15e-36

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: 134.23  E-value: 8.15e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIDHKAGgRHVAVKIVKNVDRYCE----AARsEIQVLEHLNttDPNstfrCVQMLE------W 230
Cdd:cd07840   1 YEKIAQIGEGTYGQVYKARNKKTG-ELVALKKIRMENEKEGfpitAIR-EIKLLQKLD--HPN----VVRLKEivtskgS 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 231 FEHHGHICIVFE-----LLGLStydfikENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqsdyteay 305
Cdd:cd07840  73 AKYKGSIYMVFEymdhdLTGLL------DNPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNIL---------- 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 306 npkikrdertlINPD--IKVVDFGSA-TYDDEHHSTL---VSTRHYRAPEviLALGWSQ---PCDVWSIGCILIEYYLGF 376
Cdd:cd07840 137 -----------INNDgvLKLADFGLArPYTKENNADYtnrVITLWYRPPE--LLLGATRygpEVDMWSVGCILAELFTGK 203
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 377 TVFPTHDSKEHLAMMERILGPLPKHMIQKTRKRKYFHHDRLDwdehssaGRYVSRrckpLKEFM---LSQDVeherlFDL 453
Cdd:cd07840 204 PIFQGKTELEQLEKIFELCGSPTEENWPGVSDLPWFENLKPK-------KPYKRR----LREVFknvIDPSA-----LDL 267
                       330       340
                ....*....|....*....|....
gi 67551261 454 IQKMLEYDPAKRITLREALKHPFF 477
Cdd:cd07840 268 LDKLLTLDPKKRISADQALQHEYF 291
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
161-477 2.28e-34

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


Pssm-ID: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 130.10  E-value: 2.28e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIDhKAGGRHVAVKIVKnVDRYCEAARS----EIQVLEHLNttDPNstfrCVQMLEwFEHHGH 236
Cdd:cd07835   1 YQKLEKIGEGTYGVVYKARD-KLTGEIVALKKIR-LETEDEGVPStairEISLLKELN--HPN----IVRLLD-VVHSEN 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 -ICIVFELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqsdyteaynpkIKRDErt 315
Cdd:cd07835  72 kLYLVFEFLDLDLKKYMDSSPLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLL-------------IDTEG-- 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 316 linpDIKVVDFGSA--------TYDDEhhstlVSTRHYRAPEVIL-ALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKE 386
Cdd:cd07835 137 ----ALKLADFGLArafgvpvrTYTHE-----VVTLWYRAPEILLgSKHYSTPVDIWSVGCIFAEMVTRRPLFPGDSEID 207
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 387 HLAMMERILG-PlpkhmiqktrkrkyfhhDRLDWDEHSSAGRYVSR----RCKPLKEFMLSQDvehERLFDLIQKMLEYD 461
Cdd:cd07835 208 QLFRIFRTLGtP-----------------DEDVWPGVTSLPDYKPTfpkwARQDLSKVVPSLD---EDGLDLLSQMLVYD 267
                       330
                ....*....|....*.
gi 67551261 462 PAKRITLREALKHPFF 477
Cdd:cd07835 268 PAKRISAKAALQHPYF 283
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
155-474 8.52e-34

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 133.21  E-value: 8.52e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 155 DVLSARYEIVDTLGEGAFGKVVECIDHKAGgRHVAVKIVK----NVDRYCEAARSEIQVLEHLNttDPNstfrCVQMLEW 230
Cdd:COG0515   3 ALLLGRYRILRLLGRGGMGVVYLARDLRLG-RPVALKVLRpelaADPEARERFRREARALARLN--HPN----IVRVYDV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 231 FEHHGHICIVFELL-GLSTYDFIKENGflPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENIlfvqsdyteaynpki 309
Cdd:COG0515  76 GEEDGRPYLVMEYVeGESLADLLRRRG--PLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANI--------------- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 310 krdertLINPD--IKVVDFGSATYDDEHHST----LVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFpthD 383
Cdd:COG0515 139 ------LLTPDgrVKLIDFGIARALGGATLTqtgtVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPF---D 209
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 384 SKEHLAMMERILgplpkhmiqktrkrkyfHHDRLDWDEHSSAgryvsrrckplkefmLSQDVEherlfDLIQKMLEYDPA 463
Cdd:COG0515 210 GDSPAELLRAHL-----------------REPPPPPSELRPD---------------LPPALD-----AIVLRALAKDPE 252
                       330
                ....*....|....*
gi 67551261 464 KRIT----LREALKH 474
Cdd:COG0515 253 ERYQsaaeLAAALRA 267
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
159-477 1.78e-33

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: 129.34  E-value: 1.78e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 159 ARYEIVDTLGEGAFGKVVECIDhKAGGRHVAVKivkNVDRYCE----AARS--EIQVLEHLN------------TTDPNS 220
Cdd:cd07851  15 DRYQNLSPVGSGAYGQVCSAFD-TKTGRKVAIK---KLSRPFQsaihAKRTyrELRLLKHMKhenviglldvftPASSLE 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 221 TFRCVQMlewfehhghiciVFELLGLSTYDFIKENgflpfRL--DHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfVQ 298
Cdd:cd07851  91 DFQDVYL------------VTHLMGADLNNIVKCQ-----KLsdDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLA-VN 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 299 SDYteaynpkikrdertlinpDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILA-LGWSQPCDVWSIGCILIEYYLGFT 377
Cdd:cd07851 153 EDC------------------ELKILDFGLARHTDDEMTGYVATRWYRAPEIMLNwMHYNQTVDIWSVGCIMAELLTGKT 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 378 VFPTHDSKEHLAMMERILGPLPKHMIQKTrkrkyfhhdrldwdEHSSAGRYVS----RRCKPLKEFMLSQDVEherLFDL 453
Cdd:cd07851 215 LFPGSDHIDQLKRIMNLVGTPDEELLKKI--------------SSESARNYIQslpqMPKKDFKEVFSGANPL---AIDL 277
                       330       340
                ....*....|....*....|....
gi 67551261 454 IQKMLEYDPAKRITLREALKHPFF 477
Cdd:cd07851 278 LEKMLVLDPDKRITAAEALAHPYL 301
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
160-477 2.70e-33

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: 127.46  E-value: 2.70e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDHKAGGRHVAVKIVKnVDRYCE----AARSEIQVLEHLNTTDPNSTFRC--VQMLEWFEH 233
Cdd:cd07862   2 QYECVAEIGEGAYGKVFKARDLKNGGRFVALKRVR-VQTGEEgmplSTIREVAVLRHLETFEHPNVVRLfdVCTVSRTDR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 234 HGHICIVFELLG--LSTY-DFIKENGFLPfrlDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDyteaynpkik 310
Cdd:cd07862  81 ETKLTLVFEHVDqdLTTYlDKVPEPGVPT---ETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSG---------- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 311 rdertlinpDIKVVDFGSA-TYDDEHH-STLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHL 388
Cdd:cd07862 148 ---------QIKLADFGLArIYSFQMAlTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFRGSSDVDQL 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 389 AMMERILG-PLPKhmiqktrkrkyfhhdrlDWDEHSSAGR--YVSRRCKPLKEFMLSQDvehERLFDLIQKMLEYDPAKR 465
Cdd:cd07862 219 GKILDVIGlPGEE-----------------DWPRDVALPRqaFHSKSAQPIEKFVTDID---ELGKDLLLKCLTFNPAKR 278
                       330
                ....*....|..
gi 67551261 466 ITLREALKHPFF 477
Cdd:cd07862 279 ISAYSALSHPYF 290
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
160-476 2.90e-33

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: 127.55  E-value: 2.90e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDHKAGGRHVAVKIVK----NVDRYCEAARSEI--QVLEHLNTTDPNstfrCVQMLEWFEH 233
Cdd:cd14096   2 NYRLINKIGEGAFSNVYKAVPLRNTGKPVAIKVVRkadlSSDNLKGSSRANIlkEVQIMKRLSHPN----IVKLLDFQES 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 234 HGHICIVFELL-GLSTYDFIKENGFlpFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYTEAYNPKIKR- 311
Cdd:cd14096  78 DEYYYIVLELAdGGEIFHQIVRLTY--FSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEPIPFIPSIVKLRKAd 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 312 ------DERTLIN-------PDIKVVDFG-SATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFT 377
Cdd:cd14096 156 ddetkvDEGEFIPgvggggiGIVKLADFGlSKQVWDSNTKTPCGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFP 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 378 vfPTHDSKEHLaMMERILgplpkhmiqktrkRKYFHHDRLDWDEHSSAGRyvsrrckplkefmlsqdveherlfDLIQKM 457
Cdd:cd14096 236 --PFYDESIET-LTEKIS-------------RGDYTFLSPWWDEISKSAK------------------------DLISHL 275
                       330
                ....*....|....*....
gi 67551261 458 LEYDPAKRITLREALKHPF 476
Cdd:cd14096 276 LTVDPAKRYDIDEFLAHPW 294
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
160-473 2.97e-33

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: 126.55  E-value: 2.97e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDHKaGGRHVAVKIVK----NVDRYCEAARSEIQVLEHLNttDPNStfrcVQMLEWFEHHG 235
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTL-LGRPVAIKVLRpelaEDEEFRERFLREARALARLS--HPNI----VRVYDVGEDDG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 236 HICIVFELL-GLSTYDFIKENGFLPfrLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENIlfvqsdyteaynpkikrder 314
Cdd:cd14014  74 RPYIVMEYVeGGSLADLLRERGPLP--PREALRILAQIADALAAAHRAGIVHRDIKPANI-------------------- 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 315 tLINPD--IKVVDFGSATYDDEHHSTLVS----TRHYRAPEVILALGWSQPCDVWSIGCILieYYLgFTVFPTHDSKEHL 388
Cdd:cd14014 132 -LLTEDgrVKLTDFGIARALGDSGLTQTGsvlgTPAYMAPEQARGGPVDPRSDIYSLGVVL--YEL-LTGRPPFDGDSPA 207
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 389 AMMERILGPLPKHMIQktrkrkyfhhdrldwdehssagrYVSRRCKPLKEfmlsqdveherlfdLIQKMLEYDPAKRITL 468
Cdd:cd14014 208 AVLAKHLQEAPPPPSP-----------------------LNPDVPPALDA--------------IILRALAKDPEERPQS 250

                ....*
gi 67551261 469 REALK 473
Cdd:cd14014 251 AAELL 255
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
161-477 4.26e-33

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: 125.78  E-value: 4.26e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIdHKAGGRHVAVKIVK-NVDRYCEAARSEIQVLEHLNTtdPNstfrCVQMLEWFEHHGHICI 239
Cdd:cd05122   2 FEILEKIGKGGFGVVYKAR-HKKTGQIVAIKKINlESKEKKESILNEIAILKKCKH--PN----IVKYYGSYLKKDELWI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 240 VFELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDyteaynpkikrdertlinp 319
Cdd:cd05122  75 VMEFCSGGSLKDLLKNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDG------------------- 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 320 DIKVVDFGSATY--DDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTvfPTHDSKEHLAMMERILGP 397
Cdd:cd05122 136 EVKLIDFGLSAQlsDGKTRNTFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKP--PYSELPPMKALFLIATNG 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 398 LPKhmiqktrkrkyfhhdrLDWDEHSSagryvsrrckplKEFMlsqdveherlfDLIQKMLEYDPAKRITLREALKHPFF 477
Cdd:cd05122 214 PPG----------------LRNPKKWS------------KEFK-----------DFLKKCLQKDPEKRPTAEQLLKHPFI 254
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
157-476 1.31e-32

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: 126.53  E-value: 1.31e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 157 LSARYEIVDTLGEGAFGKVVECIDhKAGGRHVAVK-IVKNVDRYCEAARS--EIQVLEHL---NTTDPNSTFrcVQMLEw 230
Cdd:cd07856   8 ITTRYSDLQPVGMGAFGLVCSARD-QLTGQNVAVKkIMKPFSTPVLAKRTyrELKLLKHLrheNIISLSDIF--ISPLE- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 231 fehhgHICIVFELLGLSTYDFIKENgflPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQsdyteaynpkik 310
Cdd:cd07856  84 -----DIYFVTELLGTDLHRLLTSR---PLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNE------------ 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 311 rdertliNPDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILAlgWSQ---PCDVWSIGCILIEYYLGFTVFPTHDSKEH 387
Cdd:cd07856 144 -------NCDLKICDFGLARIQDPQMTGYVSTRYYRAPEIMLT--WQKydvEVDIWSAGCIFAEMLEGKPLFPGKDHVNQ 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 388 LAMMERILGPLPKHMIQKTRKRKYFhhdrldwdehssagRYVS----RRCKPLKEFMLSQDVEHerlFDLIQKMLEYDPA 463
Cdd:cd07856 215 FSIITELLGTPPDDVINTICSENTL--------------RFVQslpkRERVPFSEKFKNADPDA---IDLLEKMLVFDPK 277
                       330
                ....*....|...
gi 67551261 464 KRITLREALKHPF 476
Cdd:cd07856 278 KRISAAEALAHPY 290
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
160-477 2.08e-32

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: 125.18  E-value: 2.08e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECiDHKAGGRHVAVKivknvdRYCEA---------ARSEIQVLEHLNttDPNstfrCVQMLEW 230
Cdd:cd07847   2 KYEKLSKIGEGSYGVVFKC-RNRETGQIVAIK------KFVESeddpvikkiALREIRMLKQLK--HPN----LVNLIEV 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 231 FEHHGHICIVFELLGLSTYDFIKENgflPFRLD--HIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDyteaynpk 308
Cdd:cd07847  69 FRRKRKLHLVFEYCDHTVLNELEKN---PRGVPehLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQG-------- 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 309 ikrdertlinpDIKVVDFGSA---TYDDEHHSTLVSTRHYRAPEVILA-LGWSQPCDVWSIGCILIEYYLGFTVFPTHDS 384
Cdd:cd07847 138 -----------QIKLCDFGFArilTGPGDDYTDYVATRWYRAPELLVGdTQYGPPVDVWAIGCVFAELLTGQPLWPGKSD 206
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 385 KEHLAMMERILGPL-PKHmIQKTRKRKYFHHDRLDwdehssagryVSRRCKPLKEFMLSQdveHERLFDLIQKMLEYDPA 463
Cdd:cd07847 207 VDQLYLIRKTLGDLiPRH-QQIFSTNQFFKGLSIP----------EPETREPLESKFPNI---SSPALSFLKGCLQMDPT 272
                       330
                ....*....|....
gi 67551261 464 KRITLREALKHPFF 477
Cdd:cd07847 273 ERLSCEELLEHPYF 286
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
160-477 6.98e-32

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: 125.16  E-value: 6.98e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDHKAGGRHVAVKIVKNVDRYCEAARS--EIQVLEHLNTTDpnstfrCVQMLEWF------ 231
Cdd:cd07878  16 RYQNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLSRPFQSLIHARRTyrELRLLKHMKHEN------VIGLLDVFtpatsi 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 232 EHHGHICIVFELLGLSTYDFIKengFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENIlfvqsdyteaynpkikr 311
Cdd:cd07878  90 ENFNEVYLVTNLMGADLNNIVK---CQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNV----------------- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 312 dertLINPD--IKVVDFGSATYDDEHHSTLVSTRHYRAPEVILA-LGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHL 388
Cdd:cd07878 150 ----AVNEDceLRILDFGLARQADDEMTGYVATRWYRAPEIMLNwMHYNQTVDIWSVGCIMAELLKGKALFPGNDYIDQL 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 389 A-MMERILGPLPKHM--IQKTRKRKYFhhDRLDWDEHSSAGRyVSRRCKPLKefmlsqdveherlFDLIQKMLEYDPAKR 465
Cdd:cd07878 226 KrIMEVVGTPSPEVLkkISSEHARKYI--QSLPHMPQQDLKK-IFRGANPLA-------------IDLLEKMLVLDSDKR 289
                       330
                ....*....|..
gi 67551261 466 ITLREALKHPFF 477
Cdd:cd07878 290 ISASEALAHPYF 301
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
157-480 7.65e-32

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: 124.79  E-value: 7.65e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 157 LSARYEIVDTLGEGAFGkVVECIDHKAGGRHVAVKIVKNV-DRYCEAARS--EIQVLEHL---NTTDPNSTFRCVQMlEW 230
Cdd:cd07858   3 VDTKYVPIKPIGRGAYG-IVCSAKNSETNEKVAIKKIANAfDNRIDAKRTlrEIKLLRHLdheNVIAIKDIMPPPHR-EA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 231 FEHhghICIVFELLGLSTYDFIKENGflPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteayNPkik 310
Cdd:cd07858  81 FND---VYIVYELMDTDLHQIIRSSQ--TLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLL---------NA--- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 311 rdertliNPDIKVVDFGSATYDDEHH---STLVSTRHYRAPEVILAL-GWSQPCDVWSIGCILIEYYLGFTVFPTHDSKE 386
Cdd:cd07858 144 -------NCDLKICDFGLARTTSEKGdfmTEYVVTRWYRAPELLLNCsEYTTAIDVWSVGCIFAELLGRKPLFPGKDYVH 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 387 HLAMMERILGPlPKhmiqktrkrkyfhHDRLDWDEHSSAGRYVsrrckplKEFMLSQDVEHERLF--------DLIQKML 458
Cdd:cd07858 217 QLKLITELLGS-PS-------------EEDLGFIRNEKARRYI-------RSLPYTPRQSFARLFphanplaiDLLEKML 275
                       330       340
                ....*....|....*....|..
gi 67551261 459 EYDPAKRITLREALKHPFFDLL 480
Cdd:cd07858 276 VFDPSKRITVEEALAHPYLASL 297
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
160-482 8.52e-32

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: 124.51  E-value: 8.52e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDHKAGGRhVAVKIVKNV-DRYCEAAR--SEIQVLEHLNTTD---------PNS--TFRcv 225
Cdd:cd07859   1 RYKIQEVIGKGSYGVVCSAIDTHTGEK-VAIKKINDVfEHVSDATRilREIKLLRLLRHPDiveikhimlPPSrrEFK-- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 226 qmlewfehhgHICIVFELLGLSTYDFIKENGFLPfrLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqsdyteaY 305
Cdd:cd07859  78 ----------DIYVVFELMESDLHQVIKANDDLT--PEHHQFFLYQLLRALKYIHTANVFHRDLKPKNIL---------A 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 306 NPKIKrdertlinpdIKVVDFGSA--TYDDEHHSTL----VSTRHYRAPEVILAL--GWSQPCDVWSIGCILIEYYLGFT 377
Cdd:cd07859 137 NADCK----------LKICDFGLArvAFNDTPTAIFwtdyVATRWYRAPELCGSFfsKYTPAIDIWSIGCIFAEVLTGKP 206
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 378 VFPTHDSKEHLAMMERILGPLPKHMIQKTRKRKyfhhdrldwdehssAGRYVS--RRCKPLKefmLSQDVEH--ERLFDL 453
Cdd:cd07859 207 LFPGKNVVHQLDLITDLLGTPSPETISRVRNEK--------------ARRYLSsmRKKQPVP---FSQKFPNadPLALRL 269
                       330       340
                ....*....|....*....|....*....
gi 67551261 454 IQKMLEYDPAKRITLREALKHPFFDLLKK 482
Cdd:cd07859 270 LERLLAFDPKDRPTAEEALADPYFKGLAK 298
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
160-477 2.86e-31

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: 121.09  E-value: 2.86e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDHKAGGRhVAVK---IVKNVDRYCEAARSEIQVLEHLNTtdPNstfrCVQMLEWFEHHGH 236
Cdd:cd06606   1 RWKKGELLGKGSFGSVYLALNLDTGEL-MAVKeveLSGDSEEELEALEREIRILSSLKH--PN----IVRYLGTERTENT 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELL-GLSTYDFIKENGflPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqsdyteaynpkikrdert 315
Cdd:cd06606  74 LNIFLEYVpGGSLASLLKKFG--KLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANIL-------------------- 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 316 lINPD--IKVVDFGSA-----TYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPthDSKEHL 388
Cdd:cd06606 132 -VDSDgvVKLADFGCAkrlaeIATGEGTKSLRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWS--ELGNPV 208
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 389 AMMERILG-----PLPKHmiqktrkrkyfhhdrldwdehssagryvsrrckplkefmLSQDveherLFDLIQKMLEYDPA 463
Cdd:cd06606 209 AALFKIGSsgeppPIPEH---------------------------------------LSEE-----AKDFLRKCLQRDPK 244
                       330
                ....*....|....
gi 67551261 464 KRITLREALKHPFF 477
Cdd:cd06606 245 KRPTADELLQHPFL 258
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
159-478 2.95e-31

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: 123.14  E-value: 2.95e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 159 ARYEIVDTLGEGAFGKVVECIDHKAGGRhVAVKIVK---NVDRYCEAARSEIQVLEHL---NTTDPNSTFRCVQMLEWFE 232
Cdd:cd07880  15 DRYRDLKQVGSGAYGTVCSALDRRTGAK-VAIKKLYrpfQSELFAKRAYRELRLLKHMkheNVIGLLDVFTPDLSLDRFH 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 233 HhghICIVFELLGLSTYDFIKENgflpfRL--DHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqsdyteaynpkik 310
Cdd:cd07880  94 D---FYLVMPFMGTDLGKLMKHE-----KLseDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLA--------------- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 311 rdertlINPD--IKVVDFGSATYDDEHHSTLVSTRHYRAPEVILA-LGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEH 387
Cdd:cd07880 151 ------VNEDceLKILDFGLARQTDSEMTGYVVTRWYRAPEVILNwMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHLDQ 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 388 LAMMERILGPLPKHMIQK---TRKRKYFHH-DRLDWDEHSSAGRYVSrrckPLKefmlsqdveherlFDLIQKMLEYDPA 463
Cdd:cd07880 225 LMEIMKVTGTPSKEFVQKlqsEDAKNYVKKlPRFRKKDFRSLLPNAN----PLA-------------VNVLEKMLVLDAE 287
                       330
                ....*....|....*
gi 67551261 464 KRITLREALKHPFFD 478
Cdd:cd07880 288 SRITAAEALAHPYFE 302
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
161-476 2.22e-30

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: 118.35  E-value: 2.22e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVeCIDHKAGGRHVAVKIV--KNVDRYCEAA--RSEIQVLEHLNttDPNstfrCVQMLEWFEHHGH 236
Cdd:cd14007   2 FEIGKPLGKGKFGNVY-LAREKKSGFIVALKVIskSQLQKSGLEHqlRREIEIQSHLR--HPN----ILRLYGYFEDKKR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELLGL-STYDFIKENGflpfRLDHIR--KMAYQICKSVNFLHSNKLTHTDLKPENILFvqsDYTEaynpkikrde 313
Cdd:cd14007  75 IYLILEYAPNgELYKELKKQK----RFDEKEaaKYIYQLALALDYLHSKNIIHRDIKPENILL---GSNG---------- 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 314 rtlinpDIKVVDFGSATYDDEH-HSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFpthDSKEHLAMME 392
Cdd:cd14007 138 ------ELKLADFGWSVHAPSNrRKTFCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPF---ESKSHQETYK 208
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 393 RILGPlpkhmiqktrkrkyfhhdRLDWDEHSSAGryvsrrckplkefmlsqdveherLFDLIQKMLEYDPAKRITLREAL 472
Cdd:cd14007 209 RIQNV------------------DIKFPSSVSPE-----------------------AKDLISKLLQKDPSKRLSLEQVL 247

                ....
gi 67551261 473 KHPF 476
Cdd:cd14007 248 NHPW 251
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
160-476 3.45e-30

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: 120.21  E-value: 3.45e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDHKAGgRHVAVKIV----KNVDRYCEAARSEI--QVLEHLNTTDPNSTFRCVQMLEWFEH 233
Cdd:cd07850   1 RYQNLKPIGSGAQGIVCAAYDTVTG-QNVAIKKLsrpfQNVTHAKRAYRELVlmKLVNHKNIIGLLNVFTPQKSLEEFQD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 234 hghICIVFELLGLSTYDFIKengflpFRLDHIRK--MAYQICKSVNFLHSNKLTHTDLKPENILfVQSDYTeaynpkikr 311
Cdd:cd07850  80 ---VYLVMELMDANLCQVIQ------MDLDHERMsyLLYQMLCGIKHLHSAGIIHRDLKPSNIV-VKSDCT--------- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 312 dertlinpdIKVVDFGSA--TYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDskeHLA 389
Cdd:cd07850 141 ---------LKILDFGLArtAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIRGTVLFPGTD---HID 208
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 390 MMERI---LGPLPKHMIQKTRkrkyfhhdrldwdehSSAGRYVSRR--CKPLKEFMLSQDV-------EHERLF-----D 452
Cdd:cd07850 209 QWNKIieqLGTPSDEFMSRLQ---------------PTVRNYVENRpkYAGYSFEELFPDVlfppdseEHNKLKasqarD 273
                       330       340
                ....*....|....*....|....
gi 67551261 453 LIQKMLEYDPAKRITLREALKHPF 476
Cdd:cd07850 274 LLSKMLVIDPEKRISVDDALQHPY 297
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
157-475 3.90e-30

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: 118.26  E-value: 3.90e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 157 LSARYEIVDTLGEGAFGKVVECIDhKAGGRHVAVKIVKNVD------RYCEAARS---EIQVLEHLNttDPNstfrCVQM 227
Cdd:cd14084   4 LRKKYIMSRTLGSGACGEVKLAYD-KSTCKKVAIKIINKRKftigsrREINKPRNietEIEILKKLS--HPC----IIKI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 228 LEWFEHHGHICIVFELL-GLSTYDFIKenGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSdyteayn 306
Cdd:cd14084  77 EDFFDAEDDYYIVLELMeGGELFDRVV--SNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQ------- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 307 pkikrDERTLinpdIKVVDFGSATY--DDEHHSTLVSTRHYRAPEVILALG---WSQPCDVWSIGCILIEYYLGFTVFPT 381
Cdd:cd14084 148 -----EEECL----IKITDFGLSKIlgETSLMKTLCGTPTYLAPEVLRSFGtegYTRAVDCWSLGVILFICLSGYPPFSE 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 382 HDSKEHLAMmerilgplpkhmiQKTRKRKYFHHdrldwdehsSAGRYVSRRCKplkefmlsqdveherlfDLIQKMLEYD 461
Cdd:cd14084 219 EYTQMSLKE-------------QILSGKYTFIP---------KAWKNVSEEAK-----------------DLVKKMLVVD 259
                       330
                ....*....|....
gi 67551261 462 PAKRITLREALKHP 475
Cdd:cd14084 260 PSRRPSIEEALEHP 273
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
167-477 1.36e-29

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: 117.79  E-value: 1.36e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIdHKAGGRHVAVKIVKnvdRYCEAARsEIQVLEHLNTtDPNstfrCVQMLEWFEHHGHICIVFELLgl 246
Cdd:cd14092  14 LGDGSFSVCRKCV-HKKTGQEFAVKIVS---RRLDTSR-EVQLLRLCQG-HPN----IVKLHEVFQDELHTYLVMELL-- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 247 stydfikENGFLpfrLDHIRKMAY-----------QICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrdert 315
Cdd:cd14092  82 -------RGGEL---LERIRKKKRfteseasrimrQLVSAVSFMHSKGVVHRDLKPENLLFTDEDD-------------- 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 316 liNPDIKVVDFGSATY--DDEHHSTLVSTRHYRAPEVIL----ALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLA 389
Cdd:cd14092 138 --DAEIKIVDFGFARLkpENQPLKTPCFTLPYAAPEVLKqalsTQGYDESCDLWSLGVILYTMLSGQVPFQSPSRNESAA 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 390 -MMERIlgplpkhmiqktrKRKYFHHDRLDWDEhssagryVSRRCKplkefmlsqdveherlfDLIQKMLEYDPAKRITL 468
Cdd:cd14092 216 eIMKRI-------------KSGDFSFDGEEWKN-------VSSEAK-----------------SLIQGLLTVDPSKRLTM 258

                ....*....
gi 67551261 469 REALKHPFF 477
Cdd:cd14092 259 SELRNHPWL 267
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
167-477 1.50e-29

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: 116.50  E-value: 1.50e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIDhKAGGRHVAVKIV-----------KNVDRYCEAA----RSEIQVLEHLNttDPNstfrCVQMLEWF 231
Cdd:cd14008   1 LGRGSFGKVKLALD-TETGQLYAIKIFnksrlrkrregKNDRGKIKNAlddvRREIAIMKKLD--HPN----IVRLYEVI 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 232 E--HHGHICIVFELL-GLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDyteaynpk 308
Cdd:cd14008  74 DdpESDKLYLVLEYCeGGPVMELDSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADG-------- 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 309 ikrdertlinpDIKVVDFGSA---TYDDEHHSTLVSTRHYRAPEVILALGWSQ---PCDVWSIGCILieYYLGFTVFPtH 382
Cdd:cd14008 146 -----------TVKISDFGVSemfEDGNDTLQKTAGTPAFLAPELCDGDSKTYsgkAADIWALGVTL--YCLVFGRLP-F 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 383 DSKEHLAMMERILgplpkhmiqktrkrkyfhhdrldwdehssagryvsrrcKPLKEFMLSQDVEHErLFDLIQKMLEYDP 462
Cdd:cd14008 212 NGDNILELYEAIQ--------------------------------------NQNDEFPIPPELSPE-LKDLLRRMLEKDP 252
                       330
                ....*....|....*
gi 67551261 463 AKRITLREALKHPFF 477
Cdd:cd14008 253 EKRITLKEIKEHPWV 267
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
160-476 2.85e-29

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: 117.51  E-value: 2.85e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECID-HKAGGRHVAVKIVKNV---DRYCEAARSEIQVLEHLNTtDPNSTfrCVQMLE--WFEH 233
Cdd:cd07857   1 RYELIKELGQGAYGIVCSARNaETSEEETVAIKKITNVfskKILAKRALRELKLLRHFRG-HKNIT--CLYDMDivFPGN 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 234 HGHICIVFELLGLSTYDFIKENgfLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqsdyteaynpkikrde 313
Cdd:cd07857  78 FNELYLYEELMEADLHQIIRSG--QPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLL------------------ 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 314 rtlINPD--IKVVDFGSA-------TYDDEHHSTLVSTRHYRAPEVILAL-GWSQPCDVWSIGCILIEYYLGFTVFPTHD 383
Cdd:cd07857 138 ---VNADceLKICDFGLArgfsenpGENAGFMTEYVATRWYRAPEIMLSFqSYTKAIDVWSVGCILAELLGRKPVFKGKD 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 384 SKEHLAMMERILGPLPKHMIQKTRKRKYfhhdrldWDEHSSAGRYvsrrckPLKEF-MLSQDVEHERLfDLIQKMLEYDP 462
Cdd:cd07857 215 YVDQLNQILQVLGTPDEETLSRIGSPKA-------QNYIRSLPNI------PKKPFeSIFPNANPLAL-DLLEKLLAFDP 280
                       330
                ....*....|....
gi 67551261 463 AKRITLREALKHPF 476
Cdd:cd07857 281 TKRISVEEALEHPY 294
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
157-475 2.96e-29

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: 115.55  E-value: 2.96e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 157 LSARYEIVDTLGEGAFGKVVECIDhKAGGRHVAVKIV--KNVDRYCEAARSEIQVLEHLNttDPNstfrCVQMLEWFEHH 234
Cdd:cd14083   1 IRDKYEFKEVLGTGAFSEVVLAED-KATGKLVAIKCIdkKALKGKEDSLENEIAVLRKIK--HPN----IVQLLDIYESK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 235 GHICIVFELL-GLSTYDFIKENGFLPFR--LDHIRkmayQICKSVNFLHSNKLTHTDLKPENILFvqsdYTEAYNPKikr 311
Cdd:cd14083  74 SHLYLVMELVtGGELFDRIVEKGSYTEKdaSHLIR----QVLEAVDYLHSLGIVHRDLKPENLLY----YSPDEDSK--- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 312 dertlinpdIKVVDFG-SATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGciLIEYYLGFTVFPTHDSKEHlAM 390
Cdd:cd14083 143 ---------IMISDFGlSKMEDSGVMSTACGTPGYVAPEVLAQKPYGKAVDCWSIG--VISYILLCGYPPFYDENDS-KL 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 391 MERILgplpkhmiqktrkRKYFHHDRLDWDEHSSAGRyvsrrckplkefmlsqdveherlfDLIQKMLEYDPAKRITLRE 470
Cdd:cd14083 211 FAQIL-------------KAEYEFDSPYWDDISDSAK------------------------DFIRHLMEKDPNKRYTCEQ 253

                ....*
gi 67551261 471 ALKHP 475
Cdd:cd14083 254 ALEHP 258
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
157-481 3.15e-29

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: 117.70  E-value: 3.15e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 157 LSARYEIVDTLGEGAFGKVVECIDHKAGGRhVAVKivknvdRYCEAARSEIQVlehlnttdpNSTFRCVQMLEWFEHHGH 236
Cdd:cd07879  13 LPERYTSLKQVGSGAYGSVCSAIDKRTGEK-VAIK------KLSRPFQSEIFA---------KRAYRELTLLKHMQHENV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELLGLSTY---------------DFIKENGfLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENiLFVQSDY 301
Cdd:cd07879  77 IGLLDVFTSAVSGdefqdfylvmpymqtDLQKIMG-HPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGN-LAVNEDC 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 302 teaynpkikrdertlinpDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILA-LGWSQPCDVWSIGCILIEYYLGFTVFP 380
Cdd:cd07879 155 ------------------ELKILDFGLARHADAEMTGYVVTRWYRAPEVILNwMHYNQTVDIWSVGCIMAEMLTGKTLFK 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 381 THDSKEHLAMMERILGPLPKHMIQKTrkrkyfhhdrldwdEHSSAGRYVSRRCK-PLKEFMLSQDVEHERLFDLIQKMLE 459
Cdd:cd07879 217 GKDYLDQLTQILKVTGVPGPEFVQKL--------------EDKAAKSYIKSLPKyPRKDFSTLFPKASPQAVDLLEKMLE 282
                       330       340
                ....*....|....*....|..
gi 67551261 460 YDPAKRITLREALKHPFFDLLK 481
Cdd:cd07879 283 LDVDKRLTATEALEHPYFDSFR 304
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
160-478 5.42e-29

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: 116.10  E-value: 5.42e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIdHKAGGRHVAVKIVKNVDRYceAARSEIQVLEHLNTTdPNstfrCVQMLEWF--EHHGHI 237
Cdd:cd14132  19 DYEIIRKIGRGKYSEVFEGI-NIGNNEKVVIKVLKPVKKK--KIKREIKILQNLRGG-PN----IVKLLDVVkdPQSKTP 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 238 CIVFELLglSTYDFIKEngFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqsdyteaynpkIKRDERTLi 317
Cdd:cd14132  91 SLIFEYV--NNTDFKTL--YPTLTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIM-------------IDHEKRKL- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 318 npdiKVVDFGSATY--DDEHHSTLVSTRHYRAPEVILALgwsqPC-----DVWSIGCILIE-YYLGFTVFPTHDSKEHLA 389
Cdd:cd14132 153 ----RLIDWGLAEFyhPGQEYNVRVASRYYKGPELLVDY----QYydyslDMWSLGCMLASmIFRKEPFFHGHDNYDQLV 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 390 MMERILG--PLPKHMiqktrkRKYfhHDRLDWDEHSSAGRYvSRrcKPLKEFmLSQDVEH---ERLFDLIQKMLEYDPAK 464
Cdd:cd14132 225 KIAKVLGtdDLYAYL------DKY--GIELPPRLNDILGRH-SK--KPWERF-VNSENQHlvtPEALDLLDKLLRYDHQE 292
                       330
                ....*....|....
gi 67551261 465 RITLREALKHPFFD 478
Cdd:cd14132 293 RITAKEAMQHPYFD 306
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
161-478 1.07e-28

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: 114.93  E-value: 1.07e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIDhKAGGRHVAVKIVKnvdryceaarseiqvLEHLNTTDPNSTFRCVQMLEWFEHHGHIC-- 238
Cdd:cd07837   3 YEKLEKIGEGTYGKVYKARD-KNTGKLVALKKTR---------------LEMEEEGVPSTALREVSLLQMLSQSIYIVrl 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 239 ---------------IVFELLGLSTYDFIKENG---FLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsd 300
Cdd:cd07837  67 ldvehveengkpllyLVFEYLDTDLKKFIDSYGrgpHNPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLV---- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 301 yteaynpkikRDERTLInpdiKVVDFG---SATYDDEHHSTLVSTRHYRAPEVIL-ALGWSQPCDVWSIGCILIEYYLGF 376
Cdd:cd07837 143 ----------DKQKGLL----KIADLGlgrAFTIPIKSYTHEIVTLWYRAPEVLLgSTHYSTPVDMWSVGCIFAEMSRKQ 208
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 377 TVFPTHDSKEHLAMMERILGPLPKHMIQKTRKRKyfhhdrlDWDEHSsagryvsrRCKPLKEFMLSQDVEHERLfDLIQK 456
Cdd:cd07837 209 PLFPGDSELQQLLHIFRLLGTPNEEVWPGVSKLR-------DWHEYP--------QWKPQDLSRAVPDLEPEGV-DLLTK 272
                       330       340
                ....*....|....*....|..
gi 67551261 457 MLEYDPAKRITLREALKHPFFD 478
Cdd:cd07837 273 MLAYDPAKRISAKAALQHPYFD 294
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
160-477 1.40e-28

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: 114.44  E-value: 1.40e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECiDHKAGGRHVAVKIV---KNVDRYCEAARSEIQVLEHLNTTDpnstfrCVQMLEWFEHHGH 236
Cdd:cd07846   2 KYENLGLVGEGSYGMVMKC-RHKETGQIVAIKKFlesEDDKMVKKIAMREIKMLKQLRHEN------LVNLIEVFRRKKR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELLGLSTYDFIK--ENGFlpfRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrder 314
Cdd:cd07846  75 WYLVFEFVDHTVLDDLEkyPNGL---DESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGV------------- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 315 tlinpdIKVVDFGSATY---DDEHHSTLVSTRHYRAPEVILA-LGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAM 390
Cdd:cd07846 139 ------VKLCDFGFARTlaaPGEVYTDYVATRWYRAPELLVGdTKYGKAVDVWAVGCLVTEMLTGEPLFPGDSDIDQLYH 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 391 MERILGPLPKHMIQKTRKRKYFHHDRL-DWDEHSSAgryvSRRCKPLKEFMLsqdveherlfDLIQKMLEYDPAKRITLR 469
Cdd:cd07846 213 IIKCLGNLIPRHQELFQKNPLFAGVRLpEVKEVEPL----ERRYPKLSGVVI----------DLAKKCLHIDPDKRPSCS 278

                ....*...
gi 67551261 470 EALKHPFF 477
Cdd:cd07846 279 ELLHHEFF 286
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
123-481 2.07e-28

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 117.06  E-value: 2.07e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  123 TSHRRSHGKShrrkrtRSVEDDEEGHLICQSGDVLSARYEIVDTLGEGAFGKVVE--CIDHKaggRHVAVKIVKNVDRYC 200
Cdd:PTZ00036  36 DEEERSHNNN------AGEDEDEEKMIDNDINRSPNKSYKLGNIIGNGSFGVVYEaiCIDTS---EKVAIKKVLQDPQYK 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  201 EAARSEIQVLEHLNTTDPNSTF--RCVQMlewFEHHGHICIVFELLGLSTYDFIK----ENGFLPFRLdhIRKMAYQICK 274
Cdd:PTZ00036 107 NRELLIMKNLNHINIIFLKDYYytECFKK---NEKNIFLNVVMEFIPQTVHKYMKhyarNNHALPLFL--VKLYSYQLCR 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  275 SVNFLHSNKLTHTDLKPENILFVQSDYTeaynpkikrdertlinpdIKVVDFGSAT--YDDEHHSTLVSTRHYRAPEVIL 352
Cdd:PTZ00036 182 ALAYIHSKFICHRDLKPQNLLIDPNTHT------------------LKLCDFGSAKnlLAGQRSVSYICSRFYRAPELML 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  353 -ALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMMERILG-PLPKHMiqKTRKRKYfhHDRLDWDEHSSAGRYVS 430
Cdd:PTZ00036 244 gATNYTTHIDLWSLGCIIAEMILGYPIFSGQSSVDQLVRIIQVLGtPTEDQL--KEMNPNY--ADIKFPDVKPKDLKKVF 319
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 67551261  431 RRCKPlkefmlsqdvehERLFDLIQKMLEYDPAKRITLREALKHPFFDLLK 481
Cdd:PTZ00036 320 PKGTP------------DDAINFISQFLKYEPLKRLNPIEALADPFFDDLR 358
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
160-477 2.08e-28

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: 113.90  E-value: 2.08e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDHKAGgRHVAVKIVKnvdryceaarseIQVLEHlntTDPNSTFRCVQMLEWFEHHGH--- 236
Cdd:cd07863   1 QYEPVAEIGVGAYGTVYKARDPHSG-HFVALKSVR------------VQTNED---GLPLSTVREVALLKRLEAFDHpni 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 -----IC------------IVFELLG--LSTY-DFIKENGfLPfrLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILf 296
Cdd:cd07863  65 vrlmdVCatsrtdretkvtLVFEHVDqdLRTYlDKVPPPG-LP--AETIKDLMRQFLRGLDFLHANCIVHRDLKPENIL- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 297 VQSDYTeaynpkikrdertlinpdIKVVDFGSATYDDEHHS--TLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYL 374
Cdd:cd07863 141 VTSGGQ------------------VKLADFGLARIYSCQMAltPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFR 202
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 375 GFTVFPTHDSKEHLAMMERILGpLPKhmiqktrkrkyfhHDRLDWDEHSSAGRYVSRRCKPLKEFMLSQDvehERLFDLI 454
Cdd:cd07863 203 RKPLFCGNSEADQLGKIFDLIG-LPP-------------EDDWPRDVTLPRGAFSPRGPRPVQSVVPEIE---ESGAQLL 265
                       330       340
                ....*....|....*....|...
gi 67551261 455 QKMLEYDPAKRITLREALKHPFF 477
Cdd:cd07863 266 LEMLTFNPHKRISAFRALQHPFF 288
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
161-477 2.27e-28

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: 113.75  E-value: 2.27e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGkVVECIDHKAGGRHVAVKIVKnVDRYCEAARS----EIQVLEHLNttDPNstfrCVQMLEWFEHHGH 236
Cdd:cd07860   2 FQKVEKIGEGTYG-VVYKARNKLTGEVVALKKIR-LDTETEGVPStairEISLLKELN--HPN----IVKLLDVIHTENK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELLG--LSTYDFIKENGFLPFRLdhIRKMAYQICKSVNFLHSNKLTHTDLKPENIlfvqsdyteaynpkikrder 314
Cdd:cd07860  74 LYLVFEFLHqdLKKFMDASALTGIPLPL--IKSYLFQLLQGLAFCHSHRVLHRDLKPQNL-------------------- 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 315 tLINPD--IKVVDFGSA--------TYDDEhhstlVSTRHYRAPEVILALG-WSQPCDVWSIGCILIEYYLGFTVFPTHD 383
Cdd:cd07860 132 -LINTEgaIKLADFGLArafgvpvrTYTHE-----VVTLWYRAPEILLGCKyYSTAVDIWSLGCIFAEMVTRRALFPGDS 205
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 384 SKEHLAMMERILGPlPkhmiqktrkrkyfhhDRLDWDEHSSAGRYVSR----RCKPLKEF--MLSQDVEherlfDLIQKM 457
Cdd:cd07860 206 EIDQLFRIFRTLGT-P---------------DEVVWPGVTSMPDYKPSfpkwARQDFSKVvpPLDEDGR-----DLLSQM 264
                       330       340
                ....*....|....*....|
gi 67551261 458 LEYDPAKRITLREALKHPFF 477
Cdd:cd07860 265 LHYDPNKRISAKAALAHPFF 284
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
160-476 2.82e-28

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: 112.73  E-value: 2.82e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECiDHKAGGRHVAVKIVKNV---DRYCEAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHGH 236
Cdd:cd14002   2 NYHVLELIGEGSFGKVYKG-RRKYTGQVVALKFIPKRgksEKELRNLRQEIEILRKLN--HPN----IIEMLDSFETKKE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELLGLSTYDFIKENGFLPfrLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQsdyteaynpkikrdertl 316
Cdd:cd14002  75 FVVVTEYAQGELFQILEDDGTLP--EEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGK------------------ 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 317 iNPDIKVVDFGSATYDDEHHSTLVS---TRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPThDSKEHLAmmer 393
Cdd:cd14002 135 -GGVVKLCDFGFARAMSCNTLVLTSikgTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYT-NSIYQLV---- 208
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 394 ilgplpkHMIQKtrkrkyfhhDRLDWDEhssagrYVSRRCKplkefmlsqdveherlfDLIQKMLEYDPAKRITLREALK 473
Cdd:cd14002 209 -------QMIVK---------DPVKWPS------NMSPEFK-----------------SFLQGLLNKDPSKRLSWPDLLE 249

                ...
gi 67551261 474 HPF 476
Cdd:cd14002 250 HPF 252
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
161-475 4.46e-28

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: 112.38  E-value: 4.46e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDT-LGEGAFGKVVECIdHKAGGRHVAVKIVKNVDRyceaARSEIQvLEHLNTTDPNstfrCVQMLEWFE--HHGHI 237
Cdd:cd14089   2 YTISKQvLGLGINGKVLECF-HKKTGEKFALKVLRDNPK----ARREVE-LHWRASGCPH----IVRIIDVYEntYQGRK 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 238 C--IVFELL-GLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqsdYTEaynpkiKRDER 314
Cdd:cd14089  72 CllVVMECMeGGELFSRIQERADSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLL-----YSS------KGPNA 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 315 TLinpdiKVVDFGSATYDDEHHS--TLVSTRHYRAPEVILALGWSQPCDVWSIGCILieyYLGFTVFPTHDSKEHLAMme 392
Cdd:cd14089 141 IL-----KLTDFGFAKETTTKKSlqTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIM---YILLCGYPPFYSNHGLAI-- 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 393 rilgplPKHMIQKTRKRKY-FHHDrlDWDEhssagryVSRRCKplkefmlsqdveherlfDLIQKMLEYDPAKRITLREA 471
Cdd:cd14089 211 ------SPGMKKRIRNGQYeFPNP--EWSN-------VSEEAK-----------------DLIRGLLKTDPSERLTIEEV 258

                ....
gi 67551261 472 LKHP 475
Cdd:cd14089 259 MNHP 262
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
159-477 8.21e-28

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: 112.79  E-value: 8.21e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 159 ARYEIVDTLGEGAFGKVVECIdHKAGGRHVAVK--IVKNV-DRYCEAARSEIQVLEHLNttDPNstfrCVQMLEWF---- 231
Cdd:cd07866   8 RDYEILGKLGEGTFGEVYKAR-QIKTGRVVALKkiLMHNEkDGFPITALREIKILKKLK--HPN----VVPLIDMAverp 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 232 -EHHGHICIVFELLGLSTYDF--IKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqsdyteaynpk 308
Cdd:cd07866  81 dKSKRKRGSVYMVTPYMDHDLsgLLENPSVKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANIL------------- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 309 IKRdertliNPDIKVVDFGSA-TYDD-------------EHHSTLVSTRHYRAPEviLALGWSQ---PCDVWSIGCILIE 371
Cdd:cd07866 148 IDN------QGILKIADFGLArPYDGpppnpkggggggtRKYTNLVVTRWYRPPE--LLLGERRyttAVDIWGIGCVFAE 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 372 YYLGFTVFPTHDSKEHLAMMERILGPLPKHMIQKTRKRKYFHhdrlDWDEHSSAGRYVSRRCKPLKEFMLsqdveherlf 451
Cdd:cd07866 220 MFTRRPILQGKSDIDQLHLIFKLCGTPTEETWPGWRSLPGCE----GVHSFTNYPRTLEERFGKLGPEGL---------- 285
                       330       340
                ....*....|....*....|....*.
gi 67551261 452 DLIQKMLEYDPAKRITLREALKHPFF 477
Cdd:cd07866 286 DLLSKLLSLDPYKRLTASDALEHPYF 311
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
167-477 8.73e-28

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: 111.07  E-value: 8.73e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIdHKAGGRHVAVKIVK----NVDRYCEAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHGHICIVFE 242
Cdd:cd05123   1 LGKGSFGKVLLVR-KKDTGKLYAMKVLRkkeiIKRKEVEHTLNERNILERVN--HPF----IVKLHYAFQTEEKLYLVLD 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 243 LLG---LSTYdfIKENGFLPfrLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrdertlinp 319
Cdd:cd05123  74 YVPggeLFSH--LSKEGRFP--EERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGH------------------ 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 320 dIKVVDFGSATY---DDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEhlaMMERILg 396
Cdd:cd05123 132 -IKLTDFGLAKElssDGDRTYTFCGTPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKE---IYEKIL- 206
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 397 plpkhmiqktrkrkyfhHDRLDWDEhssagrYVSRRCKplkefmlsqdveherlfDLIQKMLEYDPAKRIT--LREALK- 473
Cdd:cd05123 207 -----------------KSPLKFPE------YVSPEAK-----------------SLISGLLQKDPTKRLGsgGAEEIKa 246

                ....
gi 67551261 474 HPFF 477
Cdd:cd05123 247 HPFF 250
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
161-475 5.05e-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: 110.03  E-value: 5.05e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIdHKAGGRHVAVKIVKNVDRYCeaaRSEIQVL----EHlnttdPN-STFRCVqmlewFEHHG 235
Cdd:cd14091   2 YEIKEEIGKGSYSVCKRCI-HKATGKEYAVKIIDKSKRDP---SEEIEILlrygQH-----PNiITLRDV-----YDDGN 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 236 HICIVFELL-GLSTYDFIKENGFLPFRldHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVqsdyTEAYNPkikrder 314
Cdd:cd14091  68 SVYLVTELLrGGELLDRILRQKFFSER--EASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYA----DESGDP------- 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 315 tlinPDIKVVDFGSATYDDEHHSTLVS---TRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPT--HDSKEhlA 389
Cdd:cd14091 135 ----ESLRICDFGFAKQLRAENGLLMTpcyTANFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPFASgpNDTPE--V 208
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 390 MMERI-LGPLPkhmiqktrkrkyFHHDRldWDEHSSAGRyvsrrckplkefmlsqdveherlfDLIQKMLEYDPAKRITL 468
Cdd:cd14091 209 ILARIgSGKID------------LSGGN--WDHVSDSAK------------------------DLVRKMLHVDPSQRPTA 250

                ....*..
gi 67551261 469 REALKHP 475
Cdd:cd14091 251 AQVLQHP 257
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
167-478 6.02e-27

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: 111.76  E-value: 6.02e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIDHKAGGRhVAVKIVKNV-DRY--CEAARSEIQVLEHLNTTDPNSTFRCVQ--MLEWFEHhghICIVF 241
Cdd:cd07853   8 IGYGAFGVVWSVTDPRDGKR-VALKKMPNVfQNLvsCKRVFRELKMLCFFKHDNVLSALDILQppHIDPFEE---IYVVT 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 242 ELLGLSTYDFIKENGflPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfVQSdyteaynpkikrdertliNPDI 321
Cdd:cd07853  84 ELMQSDLHKIIVSPQ--PLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLL-VNS------------------NCVL 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 322 KVVDFGSA---TYDDEHHSTL-VSTRHYRAPEVIL-ALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMMERILG 396
Cdd:cd07853 143 KICDFGLArveEPDESKHMTQeVVTQYYRAPEILMgSRHYTSAVDIWSVGCIFAELLGRRILFQAQSPIQQLDLITDLLG 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 397 PLPKHMIQKTRkrkyfhhdrldwdehSSAGRYVSRRCKPLKE----FMLSQDVEHERlFDLIQKMLEYDPAKRITLREAL 472
Cdd:cd07853 223 TPSLEAMRSAC---------------EGARAHILRGPHKPPSlpvlYTLSSQATHEA-VHLLCRMLVFDPDKRISAADAL 286

                ....*.
gi 67551261 473 KHPFFD 478
Cdd:cd07853 287 AHPYLD 292
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
160-477 8.56e-27

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: 108.70  E-value: 8.56e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIdHKAGGRHVAVKIV--KNVDRYC-EAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHGH 236
Cdd:cd08215   1 KYEKIRVIGKGSFGSAYLVR-RKSDGKLYVLKEIdlSNMSEKErEEALNEVKLLSKLK--HPN----IVKYYESFEENGK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFE------LlglstYDFIKE--NGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENIlFVQSDYTeaynpk 308
Cdd:cd08215  74 LCIVMEyadggdL-----AQKIKKqkKKGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNI-FLTKDGV------ 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 309 ikrdertlinpdIKVVDFGSA---TYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEyylgftvfpthdsk 385
Cdd:cd08215 142 ------------VKLGDFGISkvlESTTDLAKTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYE-------------- 195
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 386 ehLAMMerilgplpkhmiqktrkRKYFHHDRLdwdeHSSAGRYVSRRCKPLKEfMLSQDveherLFDLIQKMLEYDPAKR 465
Cdd:cd08215 196 --LCTL-----------------KHPFEANNL----PALVYKIVKGQYPPIPS-QYSSE-----LRDLVNSMLQKDPEKR 246
                       330
                ....*....|..
gi 67551261 466 ITLREALKHPFF 477
Cdd:cd08215 247 PSANEILSSPFI 258
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
167-402 8.69e-27

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: 108.39  E-value: 8.69e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVvecidHKA--GGRHVAVKIVKNVD---RYCEAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHGHICIVF 241
Cdd:cd13999   1 IGSGSFGEV-----YKGkwRGTDVAIKKLKVEDdndELLKEFRREVSILSKLR--HPN----IVQFIGACLSPPPLCIVT 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 242 ELL-GLSTYDFIKENGFlPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfVQSDYTeaynpkikrdertlinpd 320
Cdd:cd13999  70 EYMpGGSLYDLLHKKKI-PLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNIL-LDENFT------------------ 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 321 IKVVDFGSAT---YDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMM--ERIL 395
Cdd:cd13999 130 VKIADFGLSRiknSTTEKMTGVVGTPRWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAVvqKGLR 209

                ....*..
gi 67551261 396 GPLPKHM 402
Cdd:cd13999 210 PPIPPDC 216
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
159-477 1.11e-26

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: 108.60  E-value: 1.11e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 159 ARYEIVDTLGEGAFGKVVECIdHKAGGRHVAVKIV---------KNVDRYCEAARSEIQVLEHLNTtDPNstfrCVQMLE 229
Cdd:cd14093   3 AKYEPKEILGRGVSSTVRRCI-EKETGQEFAVKIIditgeksseNEAEELREATRREIEILRQVSG-HPN----IIELHD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 230 WFEHHGHICIVFELL-GLSTYDFIKENGFLPFRldHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteaynpk 308
Cdd:cd14093  77 VFESPTFIFLVFELCrKGELFDYLTEVVTLSEK--KTRRIMRQLFEAVEFLHSLNIVHRDLKPENILL------------ 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 309 ikrDErtliNPDIKVVDFGSATY--DDEHHSTLVSTRHYRAPEVIL------ALGWSQPCDVWSIGCILIEYYLGFTVFp 380
Cdd:cd14093 143 ---DD----NLNVKISDFGFATRldEGEKLRELCGTPGYLAPEVLKcsmydnAPGYGKEVDMWACGVIMYTLLAGCPPF- 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 381 THDSKehlAMMERilgplpkhMIQKTRkrkyFHHDRLDWDEHSSAGRyvsrrckplkefmlsqdveherlfDLIQKMLEY 460
Cdd:cd14093 215 WHRKQ---MVMLR--------NIMEGK----YEFGSPEWDDISDTAK------------------------DLISKLLVV 255
                       330
                ....*....|....*..
gi 67551261 461 DPAKRITLREALKHPFF 477
Cdd:cd14093 256 DPKKRLTAEEALEHPFF 272
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
160-477 1.40e-26

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: 108.02  E-value: 1.40e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDhKAGGRHVAVKIVKN----VDRYCEAARSEIQVleHLNTTDPNstfrCVQMLEWFEHHG 235
Cdd:cd14099   2 RYRRGKFLGKGGFAKCYEVTD-MSTGKVYAGKVVPKssltKPKQREKLKSEIKI--HRSLKHPN----IVKFHDCFEDEE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 236 HICIVFELL-GLSTYDFIKENGflPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteaynpkikrDEr 314
Cdd:cd14099  75 NVYILLELCsNGSLMELLKRRK--ALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFL---------------DE- 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 315 tliNPDIKVVDFGSAT---YDDEHHSTLVSTRHYRAPEVIL-ALGWSQPCDVWSIGCILieYYL--GFTVFPTHDSKEhl 388
Cdd:cd14099 137 ---NMNVKIGDFGLAArleYDGERKKTLCGTPNYIAPEVLEkKKGHSFEVDIWSLGVIL--YTLlvGKPPFETSDVKE-- 209
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 389 aMMERIlgplpkhmiqktRKRKYfhhdrlDWDEHSSagryVSRRCKplkefmlsqdveherlfDLIQKMLEYDPAKRITL 468
Cdd:cd14099 210 -TYKRI------------KKNEY------SFPSHLS----ISDEAK-----------------DLIRSMLQPDPTKRPSL 249

                ....*....
gi 67551261 469 REALKHPFF 477
Cdd:cd14099 250 DEILSHPFF 258
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
167-371 1.83e-26

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: 107.83  E-value: 1.83e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIDhKAGGRHVAVKIVkNVDRYCEAARSEIQVLE---HLNTTDPNStfRCVQMLEWFEHHGHICIVFEL 243
Cdd:cd06625   8 LGQGAFGQVYLCYD-ADTGRELAVKQV-EIDPINTEASKEVKALEceiQLLKNLQHE--RIVQYYGCLQDEKSLSIFMEY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 244 L-GLSTYDFIKENGFLPFRLdhIRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqsdyteaynpkikRDErtliNPDIK 322
Cdd:cd06625  84 MpGGSVKDEIKAYGALTENV--TRKYTRQILEGLAYLHSNMIVHRDIKGANIL---------------RDS----NGNVK 142
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 67551261 323 VVDFGSATYDDEHHS-----TLVSTRHYRAPEVILALGWSQPCDVWSIGCILIE 371
Cdd:cd06625 143 LGDFGASKRLQTICSstgmkSVTGTPYWMSPEVINGEGYGRKADIWSVGCTVVE 196
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
161-477 4.79e-26

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: 107.31  E-value: 4.79e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGkVVECIDHKAGGRHVAVKIVKNvdrycEAARS--------EIQVLehLNTTDPN----------STF 222
Cdd:cd07843   7 YEKLNRIEEGTYG-VVYRARDKKTGEIVALKKLKM-----EKEKEgfpitslrEINIL--LKLQHPNivtvkevvvgSNL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 223 RCVQM-LEWFEHhghicivfELLGLstydfiKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqsdy 301
Cdd:cd07843  79 DKIYMvMEYVEH--------DLKSL------METMKQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLL------ 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 302 teaYNPKIkrdertlinpDIKVVDFGSA-TYDD--EHHSTLVSTRHYRAPEVIL-ALGWSQPCDVWSIGCILIEYYLGFT 377
Cdd:cd07843 139 ---LNNRG----------ILKICDFGLArEYGSplKPYTQLVVTLWYRAPELLLgAKEYSTAIDMWSVGCIFAELLTKKP 205
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 378 VFPTHDSKEHLAMMERILGpLPkhmiqkTRKRkyfhhdrldWDEHSSagrYVSRRCKPLKEFMLSQDVEHERL------- 450
Cdd:cd07843 206 LFPGKSEIDQLNKIFKLLG-TP------TEKI---------WPGFSE---LPGAKKKTFTKYPYNQLRKKFPAlslsdng 266
                       330       340
                ....*....|....*....|....*..
gi 67551261 451 FDLIQKMLEYDPAKRITLREALKHPFF 477
Cdd:cd07843 267 FDLLNRLLTYDPAKRISAEDALKHPYF 293
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
160-475 5.11e-26

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: 106.64  E-value: 5.11e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIdHKAGGRHVAVKIVKNvdRYCEAA----RSEIQVLEHLNttDPNstfrCVQMLEWFEHHG 235
Cdd:cd14095   1 KYDIGRVIGDGNFAVVKECR-DKATDKEYALKIIDK--AKCKGKehmiENEVAILRRVK--HPN----IVQLIEEYDTDT 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 236 HICIVFELL-GLSTYDFIKENGFLPFRlDHIRkMAYQICKSVNFLHSNKLTHTDLKPENILFVqsdyteaynpKIKRDER 314
Cdd:cd14095  72 ELYLVMELVkGGDLFDAITSSTKFTER-DASR-MVTDLAQALKYLHSLSIVHRDIKPENLLVV----------EHEDGSK 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 315 TLinpdiKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHD-SKEHLamMER 393
Cdd:cd14095 140 SL-----KLADFGLATEVKEPLFTVCGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRSPDrDQEEL--FDL 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 394 ILgplpkhmiqktrkRKYFHHDRLDWDEHSSAGRyvsrrckplkefmlsqdveherlfDLIQKMLEYDPAKRITLREALK 473
Cdd:cd14095 213 IL-------------AGEFEFLSPYWDNISDSAK------------------------DLISRMLVVDPEKRYSAGQVLD 255

                ..
gi 67551261 474 HP 475
Cdd:cd14095 256 HP 257
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
161-476 5.44e-26

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: 107.42  E-value: 5.44e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIdHKAGGRHVAVKIVknvDRYCEAARSEIQVLEHLNTtDPNstfrCVQMLEWFEHHGHICIV 240
Cdd:cd14175   3 YVVKETIGVGSYSVCKRCV-HKATNMEYAVKVI---DKSKRDPSEEIEILLRYGQ-HPN----IITLKDVYDDGKHVYLV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 241 FELL-GLSTYDFIKENGFLPFRldHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQsdytEAYNPKikrdertlinp 319
Cdd:cd14175  74 TELMrGGELLDKILRQKFFSER--EASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVD----ESGNPE----------- 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 320 DIKVVDFGSATYDDEHHSTLVS---TRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHdskehlammeriLG 396
Cdd:cd14175 137 SLRICDFGFAKQLRAENGLLMTpcyTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFANG------------PS 204
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 397 PLPKHMIQKTRKRKyFHHDRLDWDEHSSAGRyvsrrckplkefmlsqdveherlfDLIQKMLEYDPAKRITLREALKHPF 476
Cdd:cd14175 205 DTPEEILTRIGSGK-FTLSGGNWNTVSDAAK------------------------DLVSKMLHVDPHQRLTAKQVLQHPW 259
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
157-477 5.55e-26

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: 108.33  E-value: 5.55e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 157 LSARYEIVDTLGEGAFGKVVECIDHKAGgRHVAVK-IVKNVDRYCEAARSEIQVLEHLNTTDpnstfrCVQMLEWFEHHG 235
Cdd:cd07854   3 LGSRYMDLRPLGCGSNGLVFSAVDSDCD-KRVAVKkIVLTDPQSVKHALREIKIIRRLDHDN------IVKVYEVLGPSG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 236 H--------------ICIVFELLGLSTYDFIKENgflPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDY 301
Cdd:cd07854  76 SdltedvgsltelnsVYIVQEYMETDLANVLEQG---PLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTEDL 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 302 TeaynpkikrdertlinpdIKVVDFGSATYDDEHH------STLVSTRHYRAPEVILA-LGWSQPCDVWSIGCILIEYYL 374
Cdd:cd07854 153 V------------------LKIGDFGLARIVDPHYshkgylSEGLVTKWYRSPRLLLSpNNYTKAIDMWAAGCIFAEMLT 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 375 GFTVFP-THDskehLAMMERILGPLPkhMIQKTRKRKYFHHDRLDWDEHSSAGRyvsrrcKPLKEFMlsQDVEHERLfDL 453
Cdd:cd07854 215 GKPLFAgAHE----LEQMQLILESVP--VVREEDRNELLNVIPSFVRNDGGEPR------RPLRDLL--PGVNPEAL-DF 279
                       330       340
                ....*....|....*....|....
gi 67551261 454 IQKMLEYDPAKRITLREALKHPFF 477
Cdd:cd07854 280 LEQILTFNPMDRLTAEEALMHPYM 303
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
161-477 5.67e-26

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: 106.50  E-value: 5.67e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIDHKAG-GRHVAVKIVknvDRYcEAARS--------EIQVLEHLNttDPNstfrCVQMLEWF 231
Cdd:cd14080   2 YRLGKTIGEGSYSKVKLAEYTKSGlKEKVACKII---DKK-KAPKDflekflprELEILRKLR--HPN----IIQVYSIF 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 232 EHHGHICIVFE------LLglstyDFIKENGFLPFRLdhIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteay 305
Cdd:cd14080  72 ERGSKVFIFMEyaehgdLL-----EYIQKRGALSESQ--ARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNN---- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 306 npkikrdertlinpdIKVVDFGSA-TYDDEHHSTLVST----RHYRAPEVILALGWS-QPCDVWSIGCILieYYLGFTVF 379
Cdd:cd14080 141 ---------------VKLSDFGFArLCPDDDGDVLSKTfcgsAAYAAPEILQGIPYDpKKYDIWSLGVIL--YIMLCGSM 203
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 380 PTHDSKehlammerilgplPKHMIQKTRKRKYfhhdrldwdEHSSAGRYVSRRCKplkefmlsqdveherlfDLIQKMLE 459
Cdd:cd14080 204 PFDDSN-------------IKKMLKDQQNRKV---------RFPSSVKKLSPECK-----------------DLIDQLLE 244
                       330
                ....*....|....*...
gi 67551261 460 YDPAKRITLREALKHPFF 477
Cdd:cd14080 245 PDPTKRATIEEILNHPWL 262
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
161-477 9.10e-26

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: 106.35  E-value: 9.10e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGkVVECIDHKAGGRHVAVKIVK---NVDRYCEAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHGHI 237
Cdd:cd07861   2 YTKIEKIGEGTYG-VVYKGRNKKTGQIVAMKKIRlesEEEGVPSTAIREISLLKELQ--HPN----IVCLEDVLMQENRL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 238 CIVFELLG--LSTY-DFIKENGFLPFRLdhIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQsdyteaynpkikrder 314
Cdd:cd07861  75 YLVFEFLSmdLKKYlDSLPKGKYMDAEL--VKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDN---------------- 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 315 tliNPDIKVVDFGSA--------TYDDEhhstlVSTRHYRAPEVIL-ALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSK 385
Cdd:cd07861 137 ---KGVIKLADFGLArafgipvrVYTHE-----VVTLWYRAPEVLLgSPRYSTPVDIWSIGTIFAEMATKKPLFHGDSEI 208
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 386 EHLAMMERILGPlpkhmiqktrkrkyfhHDRLDWDEHSSAGRYVSRRCKpLKEFMLSQDVEH--ERLFDLIQKMLEYDPA 463
Cdd:cd07861 209 DQLFRIFRILGT----------------PTEDIWPGVTSLPDYKNTFPK-WKKGSLRTAVKNldEDGLDLLEKMLIYDPA 271
                       330
                ....*....|....
gi 67551261 464 KRITLREALKHPFF 477
Cdd:cd07861 272 KRISAKKALVHPYF 285
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
160-479 1.40e-25

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: 107.48  E-value: 1.40e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDhKAGGRHVAVK-IVKNVDRYCEAARSE-----IQVLEHLNTTDPNSTFRCVQMLEWFEH 233
Cdd:cd07874  18 RYQNLKPIGSGAQGIVCAAYD-AVLDRNVAIKkLSRPFQNQTHAKRAYrelvlMKCVNHKNIISLLNVFTPQKSLEEFQD 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 234 hghICIVFELLGLSTYDFIKengflpFRLDHIRK--MAYQICKSVNFLHSNKLTHTDLKPENILfVQSDYTeaynpkikr 311
Cdd:cd07874  97 ---VYLVMELMDANLCQVIQ------MELDHERMsyLLYQMLCGIKHLHSAGIIHRDLKPSNIV-VKSDCT--------- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 312 dertlinpdIKVVDFGSATYDDEHH--STLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHL- 388
Cdd:cd07874 158 ---------LKILDFGLARTAGTSFmmTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKILFPGRDYIDQWn 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 389 AMMERILGPLPKHMIQKTRKRKYFHHDRLDWdehssAGRYVSrrcKPLKEFMLSQDVEHERL-----FDLIQKMLEYDPA 463
Cdd:cd07874 229 KVIEQLGTPCPEFMKKLQPTVRNYVENRPKY-----AGLTFP---KLFPDSLFPADSEHNKLkasqaRDLLSKMLVIDPA 300
                       330
                ....*....|....*.
gi 67551261 464 KRITLREALKHPFFDL 479
Cdd:cd07874 301 KRISVDEALQHPYINV 316
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
161-478 1.74e-25

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: 105.84  E-value: 1.74e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVeCIDHKAGGRHVAVKIVKNVDRYCEAA-RSEIQVLEHLNTTDpnstfrCVQMLEWFEHHGHICI 239
Cdd:cd14166   5 FIFMEVLGSGAFSEVY-LVKQRSTGKLYALKCIKKSPLSRDSSlENEIAVLKRIKHEN------IVTLEDIYESTTHYYL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 240 VFELL-GLSTYDFIKENGFlpFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteaYNPkikrDErtliN 318
Cdd:cd14166  78 VMQLVsGGELFDRILERGV--YTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLY--------LTP----DE----N 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 319 PDIKVVDFG-SATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILieyYLGFTVFPTHDSKEHLAMMERIlgp 397
Cdd:cd14166 140 SKIMITDFGlSKMEQNGIMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIT---YILLCGYPPFYEETESRLFEKI--- 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 398 lpkhmiqktrKRKYFHHDRLDWDEHSSAGRyvsrrckplkefmlsqdveherlfDLIQKMLEYDPAKRITLREALKHPFF 477
Cdd:cd14166 214 ----------KEGYYEFESPFWDDISESAK------------------------DFIRHLLEKNPSKRYTCEKALSHPWI 259

                .
gi 67551261 478 D 478
Cdd:cd14166 260 I 260
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
161-476 1.78e-25

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: 105.11  E-value: 1.78e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVeCIDHKAGGRHVAVKIV--KNVDRYCEAARSEIQVLEHLNTTDpnstfrCVQMLEWFEHHGHIC 238
Cdd:cd14167   5 YDFREVLGTGAFSEVV-LAEEKRTQKLVAIKCIakKALEGKETSIENEIAVLHKIKHPN------IVALDDIYESGGHLY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 239 IVFELL-GLSTYDFIKENGFLPFRldHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDyteaynpkikRDERTLI 317
Cdd:cd14167  78 LIMQLVsGGELFDRIVEKGFYTER--DASKLIFQILDAVKYLHDMGIVHRDLKPENLLYYSLD----------EDSKIMI 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 318 NpdikvvDFGSATYDDEHH--STLVSTRHYRAPEVILALGWSQPCDVWSIGCILieyYLGFTVFPTHDSKEHLAMMERIL 395
Cdd:cd14167 146 S------DFGLSKIEGSGSvmSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIA---YILLCGYPPFYDENDAKLFEQIL 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 396 gplpkhmiqktrkRKYFHHDRLDWDEHSSAGRyvsrrckplkefmlsqdveherlfDLIQKMLEYDPAKRITLREALKHP 475
Cdd:cd14167 217 -------------KAEYEFDSPYWDDISDSAK------------------------DFIQHLMEKDPEKRFTCEQALQHP 259

                .
gi 67551261 476 F 476
Cdd:cd14167 260 W 260
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
160-479 2.72e-25

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: 106.67  E-value: 2.72e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDhKAGGRHVAVK-IVKNVDRYCEAARSE-----IQVLEHLNTTDPNSTFRCVQMLEWFEH 233
Cdd:cd07875  25 RYQNLKPIGSGAQGIVCAAYD-AILERNVAIKkLSRPFQNQTHAKRAYrelvlMKCVNHKNIIGLLNVFTPQKSLEEFQD 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 234 hghICIVFELLGLSTYDFIKengflpFRLDHIRK--MAYQICKSVNFLHSNKLTHTDLKPENILfVQSDYTeaynpkikr 311
Cdd:cd07875 104 ---VYIVMELMDANLCQVIQ------MELDHERMsyLLYQMLCGIKHLHSAGIIHRDLKPSNIV-VKSDCT--------- 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 312 dertlinpdIKVVDFGSATYDDEHH--STLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHL- 388
Cdd:cd07875 165 ---------LKILDFGLARTAGTSFmmTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGVLFPGTDHIDQWn 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 389 AMMERILGPLPKHMIQKTRKRKYFHHDRLDWDEHSSAgryvsrrcKPLKEFMLSQDVEHERL-----FDLIQKMLEYDPA 463
Cdd:cd07875 236 KVIEQLGTPCPEFMKKLQPTVRTYVENRPKYAGYSFE--------KLFPDVLFPADSEHNKLkasqaRDLLSKMLVIDAS 307
                       330
                ....*....|....*.
gi 67551261 464 KRITLREALKHPFFDL 479
Cdd:cd07875 308 KRISVDEALQHPYINV 323
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
157-476 1.03e-24

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: 103.75  E-value: 1.03e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 157 LSARYEIVDTLGEGAFGKVVECiDHKAGGRHVAVKIVK-NVDRycEAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHG 235
Cdd:cd14085   1 LEDFFEIESELGRGATSVVYRC-RQKGTQKPYAVKKLKkTVDK--KIVRTEIGVLLRLS--HPN----IIKLKEIFETPT 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 236 HICIVFELL-GLSTYDFIKENGFLPFR--LDHIRkmayQICKSVNFLHSNKLTHTDLKPENILFVQSdyteaynpkikRD 312
Cdd:cd14085  72 EISLVLELVtGGELFDRIVEKGYYSERdaADAVK----QILEAVAYLHENGIVHRDLKPENLLYATP-----------AP 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 313 ERTLinpdiKVVDFG-SATYDDE-HHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTvfPTHDSKEHLAM 390
Cdd:cd14085 137 DAPL-----KIADFGlSKIVDQQvTMKTVCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFE--PFYDERGDQYM 209
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 391 MERILgplpkhmiqktrkrkyfhhdRLDWDEHSSAGRYVSRRCKplkefmlsqdveherlfDLIQKMLEYDPAKRITLRE 470
Cdd:cd14085 210 FKRIL--------------------NCDYDFVSPWWDDVSLNAK-----------------DLVKKLIVLDPKKRLTTQQ 252

                ....*.
gi 67551261 471 ALKHPF 476
Cdd:cd14085 253 ALQHPW 258
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
161-477 2.84e-24

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: 101.91  E-value: 2.84e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIDhKAGGRHVAVKI-----------VKNVDRyceaarsEIQVLEHLNTtdPN-----STFRC 224
Cdd:cd05581   3 FKFGKPLGEGSYSTVVLAKE-KETGKEYAIKVldkrhiikekkVKYVTI-------EKEVLSRLAH--PGivklyYTFQD 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 225 VQ----MLEWFEHhGhicivfELLglstyDFIKENGFLPFrlDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsd 300
Cdd:cd05581  73 ESklyfVLEYAPN-G------DLL-----EYIRKYGSLDE--KCTRFYTAEIVLALEYLHSKGIIHRDLKPENILL---- 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 301 yTEAYNPKI------KRDERTLINPDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYL 374
Cdd:cd05581 135 -DEDMHIKItdfgtaKVLGPDSSPESTKGDADSQIAYNQARAASFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLT 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 375 GFTVFptHDSKEHLAMmerilgplpkhmiQKTRKRKYfhhdrlDWDEHssagryvsrrckplkefmLSQDVEherlfDLI 454
Cdd:cd05581 214 GKPPF--RGSNEYLTF-------------QKIVKLEY------EFPEN------------------FPPDAK-----DLI 249
                       330       340
                ....*....|....*....|....*....
gi 67551261 455 QKMLEYDPAKRITLRE-----ALK-HPFF 477
Cdd:cd05581 250 QKLLVLDPSKRLGVNEnggydELKaHPFF 278
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
160-477 3.10e-24

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: 101.53  E-value: 3.10e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDHKAGgRHVAVKIVKNVDRYCE---AARSEIQVLEHLNttDPNstfrCVQMLEWFEHHGH 236
Cdd:cd06627   1 NYQLGDLIGRGAFGSVYKGLNLNTG-EFVAIKQISLEKIPKSdlkSVMGEIDLLKKLN--HPN----IVKYIGSVKTKDS 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELL-GLSTYDFIKENGFLPFRLdhIRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqsdyteaynpkikrderT 315
Cdd:cd06627  74 LYIILEYVeNGSLASIIKKFGKFPESL--VAVYIYQVLEGLAYLHEQGVIHRDIKGANIL-------------------T 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 316 LINPDIKVVDFGSATYDDEHHS---TLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYylgFTVFPTHDSKEHLAMME 392
Cdd:cd06627 133 TKDGLVKLADFGVATKLNEVEKdenSVVGTPYWMAPEVIEMSGVTTASDIWSVGCTVIEL---LTGNPPYYDLQPMAALF 209
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 393 RIlgplpkhmiqktrkrkyfhhdrldwdehssagryVSRRCKPLKEfMLSQDVEherlfDLIQKMLEYDPAKRITLREAL 472
Cdd:cd06627 210 RI----------------------------------VQDDHPPLPE-NISPELR-----DFLLQCFQKDPTLRPSAKELL 249

                ....*
gi 67551261 473 KHPFF 477
Cdd:cd06627 250 KHPWL 254
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
160-477 3.35e-24

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: 102.45  E-value: 3.35e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECiDHKAGGRHVAVKIVKnVDRYCEA----ARSEIQVLEHLN-----------TTDPNSTFRC 224
Cdd:cd07865  13 KYEKLAKIGQGTFGEVFKA-RHRKTGQIVALKKVL-MENEKEGfpitALREIKILQLLKhenvvnlieicRTKATPYNRY 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 225 vqmlewfehHGHICIVFE-----LLGLSTYDFIKengflpFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqs 299
Cdd:cd07865  91 ---------KGSIYLVFEfcehdLAGLLSNKNVK------FTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANIL---- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 300 dyteaynpkIKRDERtlinpdIKVVDFGSA------TYDDEH-HSTLVSTRHYRAPEviLALG---WSQPCDVWSIGCIL 369
Cdd:cd07865 152 ---------ITKDGV------LKLADFGLArafslaKNSQPNrYTNRVVTLWYRPPE--LLLGerdYGPPIDMWGAGCIM 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 370 IEYYLGFTVFPTHDSKEHLAMMERILGPLPKHMIQKTRKRKYFHHDRLDWDEHssagRYVSRRCKPLkefmlsqdVEHER 449
Cdd:cd07865 215 AEMWTRSPIMQGNTEQHQLTLISQLCGSITPEVWPGVDKLELFKKMELPQGQK----RKVKERLKPY--------VKDPY 282
                       330       340
                ....*....|....*....|....*...
gi 67551261 450 LFDLIQKMLEYDPAKRITLREALKHPFF 477
Cdd:cd07865 283 ALDLIDKLLVLDPAKRIDADTALNHDFF 310
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
161-477 3.60e-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: 101.19  E-value: 3.60e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIdHKAGGRHVAVKIV-----KNVDRYcEAARSEIQVLEHLnttdpnstfrcvqmlewfeHHG 235
Cdd:cd14079   4 YILGKTLGVGSFGKVKLAE-HELTGHKVAVKILnrqkiKSLDME-EKIRREIQILKLF-------------------RHP 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 236 HICIVFELLGLST--------------YDFIKENGFLPfrLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdy 301
Cdd:cd14079  63 HIIRLYEVIETPTdifmvmeyvsggelFDYIVQKGRLS--EDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLL----- 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 302 teaynpkikrDErtliNPDIKVVDFG--SATYDDEHHSTLVSTRHYRAPEVILALGWSQP-CDVWSIGCILieYYLGFTV 378
Cdd:cd14079 136 ----------DS----NMNVKIADFGlsNIMRDGEFLKTSCGSPNYAAPEVISGKLYAGPeVDVWSCGVIL--YALLCGS 199
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 379 FPTHDskEHLAMM-ERILG---PLPKHmiqktrkrkyfhhdrldwdehssagryvsrrckplkefmLSQDVEherlfDLI 454
Cdd:cd14079 200 LPFDD--EHIPNLfKKIKSgiyTIPSH---------------------------------------LSPGAR-----DLI 233
                       330       340
                ....*....|....*....|...
gi 67551261 455 QKMLEYDPAKRITLREALKHPFF 477
Cdd:cd14079 234 KRMLVVDPLKRITIPEIRQHPWF 256
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
167-475 4.68e-24

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: 100.81  E-value: 4.68e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIdHKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTdpnstfRCVQMLEWFEHHGHICIVFELL-G 245
Cdd:cd14006   1 LGRGRFGVVKRCI-EKATGREFAAKFIPKRDKKKEAVLREISILNQLQHP------RIIQLHEAYESPTELVLILELCsG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 246 LSTYDFIKENGFLpfRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrdertlinPDIKVVD 325
Cdd:cd14006  74 GELLDRLAERGSL--SEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPS-----------------PQIKIID 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 326 FGSATY--DDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGciLIEYYL--GFTVFPTHDSKEHLAmmeRILGPlpkh 401
Cdd:cd14006 135 FGLARKlnPGEELKEIFGTPEFVAPEIVNGEPVSLATDMWSIG--VLTYVLlsGLSPFLGEDDQETLA---NISAC---- 205
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 67551261 402 miqktrkrkyfhhdRLDWDEHSSAGryVSRRCKplkefmlsqdveherlfDLIQKMLEYDPAKRITLREALKHP 475
Cdd:cd14006 206 --------------RVDFSEEYFSS--VSQEAK-----------------DFIRKLLVKEPRKRPTAQEALQHP 246
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
160-477 7.08e-24

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: 100.39  E-value: 7.08e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIdHKAGGRHVAVKIV--KNVDRYCEAARS-----EIQVLEHLNTTD-PNstfrCVQMLEWF 231
Cdd:cd14005   1 QYEVGDLLGKGGFGTVYSGV-RIRDGLPVAVKFVpkSRVTEWAMINGPvpvplEIALLLKASKPGvPG----VIRLLDWY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 232 EHHGHICIVFE-------LlglstYDFIKENGFLPFRLdhIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdytea 304
Cdd:cd14005  76 ERPDGFLLIMErpepcqdL-----FDFITERGALSENL--ARIIFRQVVEAVRHCHQRGVLHRDIKDENLLI-------- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 305 ynpkikrDERTLinpDIKVVDFGSATY-DDEHHSTLVSTRHYRAPEVIL-ALGWSQPCDVWSIGCILieYYLGFTVFPTH 382
Cdd:cd14005 141 -------NLRTG---EVKLIDFGCGALlKDSVYTDFDGTRVYSPPEWIRhGRYHGRPATVWSLGILL--YDMLCGDIPFE 208
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 383 dskehlammerilgplpkHMIQKTRKRKYFHHDrldwdehssagryVSRRCKplkefmlsqdveherlfDLIQKMLEYDP 462
Cdd:cd14005 209 ------------------NDEQILRGNVLFRPR-------------LSKECC-----------------DLISRCLQFDP 240
                       330
                ....*....|....*
gi 67551261 463 AKRITLREALKHPFF 477
Cdd:cd14005 241 SKRPSLEQILSHPWF 255
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
160-477 7.88e-24

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: 101.59  E-value: 7.88e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDHK-AGGRHVAVK-IVKNVDRY---CEAARSEIQVLEHLNttDPNstfrCVQMLEWFEHH 234
Cdd:cd07842   1 KYEIEGCIGRGTYGRVYKAKRKNgKDGKEYAIKkFKGDKEQYtgiSQSACREIALLRELK--HEN----VVSLVEVFLEH 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 235 GHICI--VFE-----LLGLSTYDFIKENGFLPFRLdhIRKMAYQICKSVNFLHSNKLTHTDLKPENILfVQSDyteaynp 307
Cdd:cd07842  75 ADKSVylLFDyaehdLWQIIKFHRQAKRVSIPPSM--VKSLLWQILNGIHYLHSNWVLHRDLKPANIL-VMGE------- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 308 kikRDERTLInpdiKVVDFGSATYDDE------HHSTLVSTRHYRAPEVIL-ALGWSQPCDVWSIGCILIEYylgFTVFP 380
Cdd:cd07842 145 ---GPERGVV----KIGDLGLARLFNAplkplaDLDPVVVTIWYRAPELLLgARHYTKAIDIWAIGCIFAEL---LTLEP 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 381 THDSKE---------HLAMMERILgplpKHMIQKTRKR-----KYFHHDRLDwdEHSSAGRYVSRRCKPLKEFMLSQDve 446
Cdd:cd07842 215 IFKGREakikksnpfQRDQLERIF----EVLGTPTEKDwpdikKMPEYDTLK--SDTKASTYPNSLLAKWMHKHKKPD-- 286
                       330       340       350
                ....*....|....*....|....*....|.
gi 67551261 447 hERLFDLIQKMLEYDPAKRITLREALKHPFF 477
Cdd:cd07842 287 -SQGFDLLRKLLEYDPTKRITAEEALEHPYF 316
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
161-477 1.03e-23

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: 100.02  E-value: 1.03e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIdHKAGGRHVAVKIVKNVDRYCEAARSEIQ-------VLEHlnttdPNstfrCVQMLEWFEH 233
Cdd:cd14081   3 YRLGKTLGKGQTGLVKLAK-HCVTGQKVAIKIVNKEKLSKESVLMKVEreiaimkLIEH-----PN----VLKLYDVYEN 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 234 HGHICIVFELL-GLSTYDFIKENGFLPFRldHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteaynpkikrD 312
Cdd:cd14081  73 KKYLYLVLEYVsGGELFDYLVKKGRLTEK--EARKFFRQIISALDYCHSHSICHRDLKPENLLL---------------D 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 313 ERTlinpDIKVVDFGSATYDDEHH--STLVSTRHYRAPEVILALGW-SQPCDVWSIGCILieYYLgftvfpthdskehla 389
Cdd:cd14081 136 EKN----NIKIADFGMASLQPEGSllETSCGSPHYACPEVIKGEKYdGRKADIWSCGVIL--YAL--------------- 194
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 390 mmerILGPLP------KHMIQKTRKRKYFHHDrldwdehssagrYVSRRCKplkefmlsqdveherlfDLIQKMLEYDPA 463
Cdd:cd14081 195 ----LVGALPfdddnlRQLLEKVKRGVFHIPH------------FISPDAQ-----------------DLLRRMLEVNPE 241
                       330
                ....*....|....
gi 67551261 464 KRITLREALKHPFF 477
Cdd:cd14081 242 KRITIEEIKKHPWF 255
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
160-476 3.17e-23

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: 100.87  E-value: 3.17e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDHKAGGRHVAVKIVKNVDRYCEAARSE-----IQVLEHLNTTDPNSTFRCVQMLEWFEHh 234
Cdd:cd07876  22 RYQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRPFQNQTHAKRAYrelvlLKCVNHKNIISLLNVFTPQKSLEEFQD- 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 235 ghICIVFELLGLSTYDFIKengflpFRLDHIRK--MAYQICKSVNFLHSNKLTHTDLKPENILfVQSDYTeaynpkikrd 312
Cdd:cd07876 101 --VYLVMELMDANLCQVIH------MELDHERMsyLLYQMLCGIKHLHSAGIIHRDLKPSNIV-VKSDCT---------- 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 313 ertlinpdIKVVDFGSATYDDEHH--STLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAM 390
Cdd:cd07876 162 --------LKILDFGLARTACTNFmmTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGSVIFQGTDHIDQWNK 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 391 MERILG-PLPKHMIQKTRKRKYFHHDRLDWDEHSSAGRYvsrrckplKEFMLSQDVEHERL-----FDLIQKMLEYDPAK 464
Cdd:cd07876 234 VIEQLGtPSAEFMNRLQPTVRNYVENRPQYPGISFEELF--------PDWIFPSESERDKLktsqaRDLLSKMLVIDPDK 305
                       330
                ....*....|..
gi 67551261 465 RITLREALKHPF 476
Cdd:cd07876 306 RISVDEALRHPY 317
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
161-477 3.44e-23

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: 99.05  E-value: 3.44e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVvECIDHKAGGRHVAVKIVKnvdryceaARSEIQVLEHLNTTDPNSTFR---CVQMLEWFEHHGHI 237
Cdd:cd06611   7 WEIIGELGDGAFGKV-YKAQHKETGLFAAAKIIQ--------IESEEELEDFMVEIDILSECKhpnIVGLYEAYFYENKL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 238 CIVFELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDyteaynpkikrdertli 317
Cdd:cd06611  78 WILIEFCDGGALDSIMLELERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDG----------------- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 318 npDIKVVDFG-SA--TYDDEHHSTLVSTRHYRAPEVILALGW-SQP----CDVWSIGCILIEYYLGftvFPTHDSKEHLA 389
Cdd:cd06611 141 --DVKLADFGvSAknKSTLQKRDTFIGTPYWMAPEVVACETFkDNPydykADIWSLGITLIELAQM---EPPHHELNPMR 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 390 MMERILGPLPKHMIQKTRKRKYFHhdrldwdehssagryvsrrckplkefmlsqdveherlfDLIQKMLEYDPAKRITLR 469
Cdd:cd06611 216 VLLKILKSEPPTLDQPSKWSSSFN--------------------------------------DFLKSCLVKDPDDRPTAA 257

                ....*...
gi 67551261 470 EALKHPFF 477
Cdd:cd06611 258 ELLKHPFV 265
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
161-477 4.29e-23

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


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 98.93  E-value: 4.29e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVEcidhkagGRHvavKIVKNVdryceAARSEIQvLEHlNTTDPNSTFRCVQMLEWFEH------- 233
Cdd:cd07871   7 YVKLDKLGEGTYATVFK-------GRS---KLTENL-----VALKEIR-LEH-EEGAPCTAIREVSLLKNLKHanivtlh 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 234 ---HGHICI--VFELLGLSTYDFIKENGFLpFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteaynpk 308
Cdd:cd07871  70 diiHTERCLtlVFEYLDSDLKQYLDNCGNL-MSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLI------------ 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 309 ikrDERTlinpDIKVVDFGSA--------TYDDEhhstlVSTRHYRAPEVIL-ALGWSQPCDVWSIGCILIEYYLGFTVF 379
Cdd:cd07871 137 ---NEKG----ELKLADFGLAraksvptkTYSNE-----VVTLWYRPPDVLLgSTEYSTPIDMWGVGCILYEMATGRPMF 204
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 380 PTHDSKEHLAMMERILGPLPKHMIQKTRKRKYFHhdrldwdehssAGRYVSRRCKPLKEFMLSQDVEHerlFDLIQKMLE 459
Cdd:cd07871 205 PGSTVKEELHLIFRLLGTPTEETWPGVTSNEEFR-----------SYLFPQYRAQPLINHAPRLDTDG---IDLLSSLLL 270
                       330
                ....*....|....*...
gi 67551261 460 YDPAKRITLREALKHPFF 477
Cdd:cd07871 271 YETKSRISAEAALRHSYF 288
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
167-477 4.34e-23

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: 98.66  E-value: 4.34e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIDHKAGGRhVAVKIVKNV-------DRYCEAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHGHICI 239
Cdd:cd06630   8 LGTGAFSSCYQARDVKTGTL-MAVKQVSFCrnssseqEEVVEAIREEIRMMARLN--HPN----IVRMLGATQHKSHFNI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 240 VFELL-GLSTYDFIKENGflPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsDYTeaynpkikrdertliN 318
Cdd:cd06630  81 FVEWMaGGSVASLLSKYG--AFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLV---DST---------------G 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 319 PDIKVVDFGSA-------TYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMM 391
Cdd:cd06630 141 QRLRIADFGAAarlaskgTGAGEFQGQLLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEKISNHLALI 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 392 ERILG-----PLPKHMIQKTRkrkyfhhdrldwdehssagryvsrrckplkefmlsqdveherlfDLIQKMLEYDPAKRI 466
Cdd:cd06630 221 FKIASattppPIPEHLSPGLR--------------------------------------------DVTLRCLELQPEDRP 256
                       330
                ....*....|.
gi 67551261 467 TLREALKHPFF 477
Cdd:cd06630 257 PARELLKHPVF 267
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
157-477 6.21e-23

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 99.45  E-value: 6.21e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  157 LSARYEIVDT-LGEGAFGKVVECIDHKAGgRHVAVKIVKNVDRYCEAARS---------------EIQV---LEHLNTTD 217
Cdd:PTZ00024   6 ISERYIQKGAhLGEGTYGKVEKAYDTLTG-KIVAIKKVKIIEISNDVTKDrqlvgmcgihfttlrELKImneIKHENIMG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  218 pnstfrcvqMLEWFEHHGHICIVFELLglsTYDFIKE-NGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILf 296
Cdd:PTZ00024  85 ---------LVDVYVEGDFINLVMDIM---ASDLKKVvDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIF- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  297 vqsdyteaynpkikrdertlINPD--IKVVDFG----------SATYDDEHHSTL-------VSTRHYRAPEVIL-ALGW 356
Cdd:PTZ00024 152 --------------------INSKgiCKIADFGlarrygyppySDTLSKDETMQRreemtskVVTLWYRAPELLMgAEKY 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  357 SQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMMERILG-PLPKHMIQKTRKRKYFhhdrldwdehssagRYVSRRCKP 435
Cdd:PTZ00024 212 HFAVDMWSVGCIFAELLTGKPLFPGENEIDQLGRIFELLGtPNEDNWPQAKKLPLYT--------------EFTPRKPKD 277
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 67551261  436 LKE-FMLSQDVEherlFDLIQKMLEYDPAKRITLREALKHPFF 477
Cdd:PTZ00024 278 LKTiFPNASDDA----IDLLQSLLKLNPLERISAKEALKHEYF 316
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
168-476 6.54e-23

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: 97.76  E-value: 6.54e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 168 GEGAFGKVVECIDHKAGGRhVAVKIVKNVD---RYCEAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHGHICIVFELL 244
Cdd:cd06626   9 GEGTFGKVYTAVNLDTGEL-MAMKEIRFQDndpKTIKEIADEMKVLEGLD--HPN----LVRYYGVEVHREEVYIFMEYC 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 245 -GLSTYDFIKENGFLPFRLdhIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrdertlinpdIKV 323
Cdd:cd06626  82 qEGTLEELLRHGRILDEAV--IRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGL-------------------IKL 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 324 VDFGSATY--------DDEHHSTLVSTRHYRAPEVIL---ALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSK----EHL 388
Cdd:cd06626 141 GDFGSAVKlknntttmAPGEVNSLVGTPAYMAPEVITgnkGEGHGRAADIWSLGCVVLEMATGKRPWSELDNEwaimYHV 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 389 AMMERilGPLPKHmiqktrkrkyfhhdrldwDEHSSAGRYVSRRCkplkefmlsqdveherlfdliqkmLEYDPAKRITL 468
Cdd:cd06626 221 GMGHK--PPIPDS------------------LQLSPEGKDFLSRC------------------------LESDPKKRPTA 256

                ....*...
gi 67551261 469 REALKHPF 476
Cdd:cd06626 257 SELLDHPF 264
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
161-476 9.90e-23

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: 97.56  E-value: 9.90e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIDhKAGGRHVAVKIVKNvdRYCEAAR---------SEIQVLEHLNttDPNstfrCVQMLEWF 231
Cdd:cd14105   7 YDIGEELGSGQFAVVKKCRE-KSTGLEYAAKFIKK--RRSKASRrgvsredieREVSILRQVL--HPN----IITLHDVF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 232 EHHGHICIVFELL-GLSTYDFIKENGFLpfRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVqsdyteaynpkik 310
Cdd:cd14105  78 ENKTDVVLILELVaGGELFDFLAEKESL--SEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLL------------- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 311 rdERTLINPDIKVVDFGSA--TYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHL 388
Cdd:cd14105 143 --DKNVPIPRIKLIDFGLAhkIEDGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETL 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 389 AMMERIlgplpkhmiqktrkrkyfhhdRLDWDEhssagRYVSRRCKPLKEFmlsqdveherlfdlIQKMLEYDPAKRITL 468
Cdd:cd14105 221 ANITAV---------------------NYDFDD-----EYFSNTSELAKDF--------------IRQLLVKDPRKRMTI 260

                ....*...
gi 67551261 469 REALKHPF 476
Cdd:cd14105 261 QESLRHPW 268
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
160-476 1.06e-22

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: 97.28  E-value: 1.06e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDHKagGRHVAVKIV--KNVDRYC-EAARSEIQVLEHLNTTDpnstfRCVQMLEW--FEHH 234
Cdd:cd14131   2 PYEILKQLGKGGSSKVYKVLNPK--KKIYALKRVdlEGADEQTlQSYKNEIELLKKLKGSD-----RIIQLYDYevTDED 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 235 GHICIVFELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSdyteaynpkikrder 314
Cdd:cd14131  75 DYLYMVMECGEIDLATILKKKRPKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLVKG--------------- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 315 tlinpDIKVVDFG--SATYDDE---HHSTLVSTRHYRAPEVILALGWSQ----------PCDVWSIGCILieYYLGFTVF 379
Cdd:cd14131 140 -----RLKLIDFGiaKAIQNDTtsiVRDSQVGTLNYMSPEAIKDTSASGegkpkskigrPSDVWSLGCIL--YQMVYGKT 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 380 PTHDSKEHLAMMERILGplPKHMIqktrkrkyfhhdrlDWDEHSSAGryvsrrckplkefmlsqdveherLFDLIQKMLE 459
Cdd:cd14131 213 PFQHITNPIAKLQAIID--PNHEI--------------EFPDIPNPD-----------------------LIDVMKRCLQ 253
                       330
                ....*....|....*..
gi 67551261 460 YDPAKRITLREALKHPF 476
Cdd:cd14131 254 RDPKKRPSIPELLNHPF 270
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
161-476 1.12e-22

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: 97.13  E-value: 1.12e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVeCIDHKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTDpnSTFR---CVQMLewfeHHGHI 237
Cdd:cd14077   3 WEFVKTIGAGSMGKVK-LAKHIRTGEKCAIKIIPRASNAGLKKEREKRLEKEISRDI--RTIReaaLSSLL----NHPHI 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 238 CIVFELLGLST--------------YDFIKENGflPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDyte 303
Cdd:cd14077  76 CRLRDFLRTPNhyymlfeyvdggqlLDYIISHG--KLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSG--- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 304 aynpkikrdertlinpDIKVVDFG-SATYDDEHH-STLVSTRHYRAPEVILALGWSQP-CDVWSIGCILIEYYLGFTVFp 380
Cdd:cd14077 151 ----------------NIKIIDFGlSNLYDPRRLlRTFCGSLYFAAPELLQAQPYTGPeVDVWSFGVVLYVLVCGKVPF- 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 381 thDSKEHLAMMERIlgplpkhmiqKTRKRKYfhhdrldwdehssaGRYVSRRCKplkefmlsqdveherlfDLIQKMLEY 460
Cdd:cd14077 214 --DDENMPALHAKI----------KKGKVEY--------------PSYLSSECK-----------------SLISRMLVV 250
                       330
                ....*....|....*.
gi 67551261 461 DPAKRITLREALKHPF 476
Cdd:cd14077 251 DPKKRATLEQVLNHPW 266
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
160-370 1.53e-22

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: 97.04  E-value: 1.53e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDHKAGgRHVAVKIVKNvDRYCEAARSEIQVLEHLNTTD--------PNstfrCVQMLEWF 231
Cdd:cd13993   1 RYQLISPIGEGAYGVVYLAVDLRTG-RKYAIKCLYK-SGPNSKDGNDFQKLPQLREIDlhrrvsrhPN----IITLHDVF 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 232 EHHGHICIVFELLGLST-YDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYTeaynpkik 310
Cdd:cd13993  75 ETEVAIYIVLEYCPNGDlFEAITENRIYVGKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDEGT-------- 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 67551261 311 rdertlinpdIKVVDFGSATYDDEHHSTLVSTRHYRAPEVI---LALGWSQPC---DVWSIGCILI 370
Cdd:cd13993 147 ----------VKLCDFGLATTEKISMDFGVGSEFYMAPECFdevGRSLKGYPCaagDIWSLGIILL 202
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
239-477 1.53e-22

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: 97.17  E-value: 1.53e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 239 IVFELLGLSTYDFIKENGFL-PFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqsdyteaynpkikrdertlI 317
Cdd:cd07836  75 LVFEYMDKDLKKYMDTHGVRgALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLL---------------------I 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 318 NPD--IKVVDFGSA--------TYDDEhhstlVSTRHYRAPEVIL-ALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKE 386
Cdd:cd07836 134 NKRgeLKLADFGLArafgipvnTFSNE-----VVTLWYRAPDVLLgSRTYSTSIDIWSVGCIMAEMITGRPLFPGTNNED 208
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 387 HLAMMERILG-PLPKHMIQKTRKRKYfhhdrldwdehssagRYVSRRCKPlKEFMLSQDVEHERLFDLIQKMLEYDPAKR 465
Cdd:cd07836 209 QLLKIFRIMGtPTESTWPGISQLPEY---------------KPTFPRYPP-QDLQQLFPHADPLGIDLLHRLLQLNPELR 272
                       250
                ....*....|..
gi 67551261 466 ITLREALKHPFF 477
Cdd:cd07836 273 ISAHDALQHPWF 284
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
160-475 2.03e-22

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: 96.30  E-value: 2.03e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIdHKAGGRHVAVKIVK----NVDRYCEAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHG 235
Cdd:cd14073   2 RYELLETLGKGTYGKVKLAI-ERATGREVAIKSIKkdkiEDEQDMVRIRREIEIMSSLN--HPH----IIRIYEVFENKD 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 236 HICIVFELL-GLSTYDFIKENGFLPFRldHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQsdyteaynpkikrder 314
Cdd:cd14073  75 KIVIVMEYAsGGELYDYISERRRLPER--EARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQ---------------- 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 315 tliNPDIKVVDFGSATYDDEHH--STLVSTRHYRAPEVILALGWSQP-CDVWSIGCILieYYLGFTVFPtHDSKEHLAMM 391
Cdd:cd14073 137 ---NGNAKIADFGLSNLYSKDKllQTFCGSPLYASPEIVNGTPYQGPeVDCWSLGVLL--YTLVYGTMP-FDGSDFKRLV 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 392 ERIlgplpkhmiqktrkrkyfhhdrldwdehsSAGRYvSRRCKPLKEFMlsqdveherlfdLIQKMLEYDPAKRITLREA 471
Cdd:cd14073 211 KQI-----------------------------SSGDY-REPTQPSDASG------------LIRWMLTVNPKRRATIEDI 248

                ....
gi 67551261 472 LKHP 475
Cdd:cd14073 249 ANHW 252
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
170-477 2.49e-22

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: 96.52  E-value: 2.49e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 170 GAFGKVVECIdHKAGGRHVAVKIVKNVD----RYCEAARSEIQVLEHLNTtdpNSTfrcVQMLEWFEHHGHICIVFELL- 244
Cdd:cd05579   4 GAYGRVYLAK-KKSTGDLYAIKVIKKRDmirkNQVDSVLAERNILSQAQN---PFV---VKLYYSFQGKKNLYLVMEYLp 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 245 GLSTYDFIKENGFLPfrLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrdertlinpdIKVV 324
Cdd:cd05579  77 GGDLYSLLENVGALD--EDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGH-------------------LKLT 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 325 DFG------------------SATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTvfPTHDSKe 386
Cdd:cd05579 136 DFGlskvglvrrqiklsiqkkSNGAPEKEDRRIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIP--PFHAET- 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 387 hlammerilgplPKHMIQKTRKRKYfhhdrlDWDEhssagryvsrrckplkEFMLSQDveherLFDLIQKMLEYDPAKRI 466
Cdd:cd05579 213 ------------PEEIFQNILNGKI------EWPE----------------DPEVSDE-----AKDLISKLLTPDPEKRL 253
                       330
                ....*....|....
gi 67551261 467 TLR---EALKHPFF 477
Cdd:cd05579 254 GAKgieEIKNHPFF 267
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
170-477 3.01e-22

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: 96.01  E-value: 3.01e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 170 GAFGKVVeCIDHKAGGRHVAVKIVKNVD----RYCEAARSEIQVLeHLNTTDPNstfrcVQMLEW-FEHHGHICIVFELL 244
Cdd:cd05611   7 GAFGSVY-LAKKRSTGDYFAIKVLKKSDmiakNQVTNVKAERAIM-MIQGESPY-----VAKLYYsFQSKDYLYLVMEYL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 245 -GLSTYDFIKENGFLPfrLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrdertlinpdIKV 323
Cdd:cd05611  80 nGGDCASLIKTLGGLP--EDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGH-------------------LKL 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 324 VDFG--SATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKehlAMMERILgplpkh 401
Cdd:cd05611 139 TDFGlsRNGLEKRHNKKFVGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPD---AVFDNIL------ 209
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 67551261 402 miqktrkrkyfhHDRLDWDEHSsagryvsrrckplKEFMLSQDVeherlfDLIQKMLEYDPAKRI---TLREALKHPFF 477
Cdd:cd05611 210 ------------SRRINWPEEV-------------KEFCSPEAV------DLINRLLCMDPAKRLganGYQEIKSHPFF 257
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
159-476 3.08e-22

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: 95.68  E-value: 3.08e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 159 ARYEIVDTLGEGAFGKVVEcIDHKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTDpnstfrCVQMLEWFEHHGHIC 238
Cdd:cd14087   1 AKYDIKALIGRGSFSRVVR-VEHRVTRQPYAIKMIETKCRGREVCESELNVLRRVRHTN------IIQLIEVFETKERVY 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 239 IVFELL-GLSTYDFIKENGflPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteaYNPKIkrDERTLI 317
Cdd:cd14087  74 MVMELAtGGELFDRIIAKG--SFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLY--------YHPGP--DSKIMI 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 318 npdikvVDFGSA----TYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGciLIEYYLGFTVFPTHDSkehlammer 393
Cdd:cd14087 142 ------TDFGLAstrkKGPNCLMKTTCGTPEYIAPEILLRKPYTQSVDMWAVG--VIAYILLSGTMPFDDD--------- 204
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 394 ilgplpkhmiqkTRKRKYFHHDRLDWDEHSSAGRYVSRRCKplkefmlsqdveherlfDLIQKMLEYDPAKRITLREALK 473
Cdd:cd14087 205 ------------NRTRLYRQILRAKYSYSGEPWPSVSNLAK-----------------DFIDRLLTVNPGERLSATQALK 255

                ...
gi 67551261 474 HPF 476
Cdd:cd14087 256 HPW 258
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
160-478 4.09e-22

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 96.43  E-value: 4.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  160 RYEIVDTLGEGAFGKVvecidHKAGGRH----VAVKIVKnvdryceaarseiqvLEHLNTTDPNSTFRCVQMLEWFEH-- 233
Cdd:PLN00009   3 QYEKVEKIGEGTYGVV-----YKARDRVtnetIALKKIR---------------LEQEDEGVPSTAIREISLLKEMQHgn 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  234 --------HGHICI--VFELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqsdyte 303
Cdd:PLN00009  63 ivrlqdvvHSEKRLylVFEYLDLDLKKHMDSSPDFAKNPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLL-------- 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  304 aynpkIKRDERTLinpdiKVVDFGSA--------TYDDEhhstlVSTRHYRAPEVIL-ALGWSQPCDVWSIGCILIEYYL 374
Cdd:PLN00009 135 -----IDRRTNAL-----KLADFGLArafgipvrTFTHE-----VVTLWYRAPEILLgSRHYSTPVDIWSVGCIFAEMVN 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  375 GFTVFPTHDSKEHLAMMERILGPLPKHMiqktrkrkyfhhdrldWDEHSSAGRYVSR--RCKPLKEFMLSQDVEHERLfD 452
Cdd:PLN00009 200 QKPLFPGDSEIDELFKIFRILGTPNEET----------------WPGVTSLPDYKSAfpKWPPKDLATVVPTLEPAGV-D 262
                        330       340
                 ....*....|....*....|....*.
gi 67551261  453 LIQKMLEYDPAKRITLREALKHPFFD 478
Cdd:PLN00009 263 LLSKMLRLDPSKRITARAALEHEYFK 288
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
161-476 4.48e-22

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: 95.47  E-value: 4.48e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECiDHKAGGRHVAVKIVKNvdRYCEAARS---------EIQVLEHLNttDPNstfrCVQMLEWF 231
Cdd:cd14194   7 YDTGEELGSGQFAVVKKC-REKSTGLQYAAKFIKK--RRTKSSRRgvsredierEVSILKEIQ--HPN----VITLHEVY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 232 EHHGHICIVFELL-GLSTYDFIKENGFLPfrLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVqsdyteaynpkik 310
Cdd:cd14194  78 ENKTDVILILELVaGGELFDFLAEKESLT--EEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLL------------- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 311 rdERTLINPDIKVVDFGSATYDD--EHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHL 388
Cdd:cd14194 143 --DRNVPKPRIKIIDFGLAHKIDfgNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETL 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 389 AMMERIlgplpkhmiqktrkrkyfhhdRLDWDEHssagrYVSRRCKPLKEFmlsqdveherlfdlIQKMLEYDPAKRITL 468
Cdd:cd14194 221 ANVSAV---------------------NYEFEDE-----YFSNTSALAKDF--------------IRRLLVKDPKKRMTI 260

                ....*...
gi 67551261 469 REALKHPF 476
Cdd:cd14194 261 QDSLQHPW 268
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
160-476 5.15e-22

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: 95.16  E-value: 5.15e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDHKAGgRHVAVKIV---KNVD-RYCEAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHG 235
Cdd:cd14663   1 RYELGRTLGEGTFAKVKFARNTKTG-ESVAIKIIdkeQVAReGMVEQIKREIAIMKLLR--HPN----IVELHEVMATKT 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 236 HICIVFELL-GLSTYDFIKENGflPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteaynpkikrDEr 314
Cdd:cd14663  74 KIFFVMELVtGGELFSKIAKNG--RLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLL---------------DE- 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 315 tliNPDIKVVDFG-SATYDDEHHSTLVSTR----HYRAPEVILALGW-SQPCDVWSIGCILIEYYLGFtvFPTHDskEHL 388
Cdd:cd14663 136 ---DGNLKISDFGlSALSEQFRQDGLLHTTcgtpNYVAPEVLARRGYdGAKADIWSCGVILFVLLAGY--LPFDD--ENL 208
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 389 AMMERilgplpkhMIQKTrkrkyfhhdRLDWDEHSSAGryvSRRckplkefmlsqdveherlfdLIQKMLEYDPAKRITL 468
Cdd:cd14663 209 MALYR--------KIMKG---------EFEYPRWFSPG---AKS--------------------LIKRILDPNPSTRITV 248

                ....*...
gi 67551261 469 REALKHPF 476
Cdd:cd14663 249 EQIMASPW 256
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
161-484 5.66e-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: 5.66e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECiDHKAGGRHVAVKIVKNVD----RYCEAARSEIQVLEHLNttdpnSTFrCVQMLEWFEHHGH 236
Cdd:cd05580   3 FEFLKTLGTGSFGRVRLV-KHKDSGKYYALKILKKAKiiklKQVEHVLNEKRILSEVR-----HPF-IVNLLGSFQDDRN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELL-GLSTYDFIKENGFLPfrLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrdert 315
Cdd:cd05580  76 LYMVMEYVpGGELFSLLRRSGRFP--NDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGH-------------- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 316 linpdIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFpthDSKEHLAMMERIL 395
Cdd:cd05580 140 -----IKITDFGFAKRVKDRTYTLCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPF---FDENPMKIYEKIL 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 396 GplpkhmiqktrKRKYFHhdrldwdehssagRYVSRRCKplkefmlsqdveherlfDLIQKMLEYDPAKRITLR----EA 471
Cdd:cd05580 212 E-----------GKIRFP-------------SFFDPDAK-----------------DLIKRLLVVDLTKRLGNLkngvED 250
                       330       340
                ....*....|....*....|
gi 67551261 472 LK-HPFF------DLLKKSI 484
Cdd:cd05580 251 IKnHPWFagidwdALLQRKI 270
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
161-476 5.96e-22

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: 95.85  E-value: 5.96e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIdHKAGGRHVAVKIVknvDRYCEAARSEIQVLEHLNTtDPNstfrCVQMLEWFEHHGHICIV 240
Cdd:cd14178   5 YEIKEDIGIGSYSVCKRCV-HKATSTEYAVKII---DKSKRDPSEEIEILLRYGQ-HPN----IITLKDVYDDGKFVYLV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 241 FELL-GLSTYDFIKENGFLPFRldHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQsdytEAYNPKikrdertlinp 319
Cdd:cd14178  76 MELMrGGELLDRILRQKCFSER--EASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMD----ESGNPE----------- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 320 DIKVVDFGSATYDDEHHSTLVS---TRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPThdskehlammerilG 396
Cdd:cd14178 139 SIRICDFGFAKQLRAENGLLMTpcyTANFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPFAN--------------G 204
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 397 P--LPKHMIQKTRKRKYFHHDRlDWDEHSSAGRyvsrrckplkefmlsqdveherlfDLIQKMLEYDPAKRITLREALKH 474
Cdd:cd14178 205 PddTPEEILARIGSGKYALSGG-NWDSISDAAK------------------------DIVSKMLHVDPHQRLTAPQVLRH 259

                ..
gi 67551261 475 PF 476
Cdd:cd14178 260 PW 261
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
161-477 8.98e-22

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: 94.38  E-value: 8.98e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIdHKAGGRHVAVKIVKNV---------DRYCEAARSEIQVLEHLNTTD-PNstfrCVQMLEW 230
Cdd:cd14004   2 YTILKEMGEGAYGQVNLAI-YKSKGKEVVIKFIFKErilvdtwvrDRKLGTVPLEIHILDTLNKRShPN----IVKLLDF 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 231 FEHHGHICIVFEL--LGLSTYDFIKengFLPFRLDHIRKMAY-QICKSVNFLHSNKLTHTDLKPENILfVQSDYTeaynp 307
Cdd:cd14004  77 FEDDEFYYLVMEKhgSGMDLFDFIE---RKPNMDEKEAKYIFrQVADAVKHLHDQGIVHRDIKDENVI-LDGNGT----- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 308 kikrdertlinpdIKVVDFGSATYDDE-HHSTLVSTRHYRAPEVILALGW-SQPCDVWSIGCILieYYLGFTVFPTHDSK 385
Cdd:cd14004 148 -------------IKLIDFGSAAYIKSgPFDTFVGTIDYAAPEVLRGNPYgGKEQDIWALGVLL--YTLVFKENPFYNIE 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 386 EHLAMMERIlgplPKhmiqktrkrkyfhhdrldwdehssagryvsrrckplkefmlsqdVEHERLFDLIQKMLEYDPAKR 465
Cdd:cd14004 213 EILEADLRI----PY--------------------------------------------AVSEDLIDLISRMLNRDVGDR 244
                       330
                ....*....|..
gi 67551261 466 ITLREALKHPFF 477
Cdd:cd14004 245 PTIEELLTDPWL 256
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
167-468 1.05e-21

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: 95.49  E-value: 1.05e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIdHKAGGRHVAVKIVKNvdRYCEAARSEIQVLEhLNTTDPNstfrCVQMLEWFEHHGHICIVFELL-G 245
Cdd:cd14179  15 LGEGSFSICRKCL-HKKTNQEYAVKIVSK--RMEANTQREIAALK-LCEGHPN----IVKLHEVYHDQLHTFLVMELLkG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 246 LSTYDFI-KENGFLPFRLDHIRKmayQICKSVNFLHSNKLTHTDLKPENILFvqSDYTEaynpkikrdertliNPDIKVV 324
Cdd:cd14179  87 GELLERIkKKQHFSETEASHIMR---KLVSAVSHMHDVGVVHRDLKPENLLF--TDESD--------------NSEIKII 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 325 DFGSATY---DDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHD-SKEHLAMMErilgplpk 400
Cdd:cd14179 148 DFGFARLkppDNQPLKTPCFTLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQCHDkSLTCTSAEE-------- 219
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 67551261 401 hmIQKTRKRKYFHHDRLDWdehssagRYVSRRCKplkefmlsqdveherlfDLIQKMLEYDPAKRITL 468
Cdd:cd14179 220 --IMKKIKQGDFSFEGEAW-------KNVSQEAK-----------------DLIQGLLTVDPNKRIKM 261
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
162-393 1.16e-21

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: 94.10  E-value: 1.16e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261   162 EIVDTLGEGAFGKVVECI---DHKAGGRHVAVKIVKNV--DRYCEAARSEIQVLEHLNTtdPNstfrCVQMLEWFEHHGH 236
Cdd:pfam07714   2 TLGEKLGEGAFGEVYKGTlkgEGENTKIKVAVKTLKEGadEEEREDFLEEASIMKKLDH--PN----IVKLLGVCTQGEP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261   237 ICIVFELLGL-STYDFIKENGfLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfVQSDYTeaynpkikrdert 315
Cdd:pfam07714  76 LYIVTEYMPGgDLLDFLRKHK-RKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCL-VSENLV------------- 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261   316 linpdIKVVDFG--SATYDDEHHSTLVSTRH---YRAPEVILALGWSQPCDVWSIGCILIE-YYLGFTVFPTHDSKEHLA 389
Cdd:pfam07714 141 -----VKISDFGlsRDIYDDDYYRKRGGGKLpikWMAPESLKDGKFTSKSDVWSFGVLLWEiFTLGEQPYPGMSNEEVLE 215

                  ....
gi 67551261   390 MMER 393
Cdd:pfam07714 216 FLED 219
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
161-476 1.38e-21

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: 95.47  E-value: 1.38e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIdHKAGGRHVAVKIVKNVDRyceAARSEIQVLEHLNTtDPNstfrCVQMLEWFEHHGHICIV 240
Cdd:cd14176  21 YEVKEDIGVGSYSVCKRCI-HKATNMEFAVKIIDKSKR---DPTEEIEILLRYGQ-HPN----IITLKDVYDDGKYVYVV 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 241 FELL-GLSTYDFIKENGFLPFRldHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQsdytEAYNPKikrdertlinp 319
Cdd:cd14176  92 TELMkGGELLDKILRQKFFSER--EASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVD----ESGNPE----------- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 320 DIKVVDFGSATYDDEHHSTLVS---TRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPThdskehlammerilG 396
Cdd:cd14176 155 SIRICDFGFAKQLRAENGLLMTpcyTANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFAN--------------G 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 397 P--LPKHMIQKTRKRKYfhhdrldwdehSSAGRYVSRrckplkefmLSQDVEherlfDLIQKMLEYDPAKRITLREALKH 474
Cdd:cd14176 221 PddTPEEILARIGSGKF-----------SLSGGYWNS---------VSDTAK-----DLVSKMLHVDPHQRLTAALVLRH 275

                ..
gi 67551261 475 PF 476
Cdd:cd14176 276 PW 277
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
157-476 1.70e-21

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: 94.19  E-value: 1.70e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 157 LSARYEIVDTLGEGAFGKVVeCIDHKAGGRHVAVK-IVKNVDRYCEAA-RSEIQVLEHLNttDPNstfrCVQMLEWFEHH 234
Cdd:cd14169   1 INSVYELKEKLGEGAFSEVV-LAQERGSQRLVALKcIPKKALRGKEAMvENEIAVLRRIN--HEN----IVSLEDIYESP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 235 GHICIVFELL-GLSTYDFIKENGFlpFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteaynpkikrdE 313
Cdd:cd14169  74 THLYLAMELVtGGELFDRIIERGS--YTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLY----------------A 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 314 RTLINPDIKVVDFG-SATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEhlaMME 392
Cdd:cd14169 136 TPFEDSKIMISDFGlSKIEAQGMLSTACGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDSE---LFN 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 393 RILgplpkhmiqktrkRKYFHHDRLDWDEHSSAGRyvsrrckplkefmlsqdveherlfDLIQKMLEYDPAKRITLREAL 472
Cdd:cd14169 213 QIL-------------KAEYEFDSPYWDDISESAK------------------------DFIRHLLERDPEKRFTCEQAL 255

                ....
gi 67551261 473 KHPF 476
Cdd:cd14169 256 QHPW 259
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
160-477 1.86e-21

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: 94.27  E-value: 1.86e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIdHKAGGRHVAVKIV---------KNVDRYCEAARSEIQVLEHLnTTDPNstfrCVQMLEW 230
Cdd:cd14181  11 KYDPKEVIGRGVSSVVRRCV-HRHTGQEFAVKIIevtaerlspEQLEEVRSSTLKEIHILRQV-SGHPS----IITLIDS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 231 FEHHGHICIVFELLGLST-YDFIKENGFLPFRldHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteaynpki 309
Cdd:cd14181  85 YESSTFIFLVFDLMRRGElFDYLTEKVTLSEK--ETRSIMRSLLEAVSYLHANNIVHRDLKPENILL------------- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 310 krDErtliNPDIKVVDFGSATY--DDEHHSTLVSTRHYRAPEVILAL------GWSQPCDVWSIGCILIEYYLGFtvfPT 381
Cdd:cd14181 150 --DD----QLHIKLSDFGFSCHlePGEKLRELCGTPGYLAPEILKCSmdethpGYGKEVDLWACGVILFTLLAGS---PP 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 382 HDSKEHLAMMErilgplpkhMIQKTRkrkyFHHDRLDWDEHSSAGRyvsrrckplkefmlsqdveherlfDLIQKMLEYD 461
Cdd:cd14181 221 FWHRRQMLMLR---------MIMEGR----YQFSSPEWDDRSSTVK------------------------DLISRLLVVD 263
                       330
                ....*....|....*.
gi 67551261 462 PAKRITLREALKHPFF 477
Cdd:cd14181 264 PEIRLTAEQALQHPFF 279
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
161-477 4.26e-21

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: 92.28  E-value: 4.26e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKV--VECIDHKA----GGRHVAVK-IVKNVdrycEAAR--SEIQVLEHLNTTDpnstfRCVQMLEWF 231
Cdd:cd14019   3 YRIIEKIGEGTFSSVykAEDKLHDLydrnKGRLVALKhIYPTS----SPSRilNELECLERLGGSN-----NVSGLITAF 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 232 EHHGHICIVFELLGLSTY-DFIKENGFLpfrldHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqsdyteaYNPKIK 310
Cdd:cd14019  74 RNEDQVVAVLPYIEHDDFrDFYRKMSLT-----DIRIYLRNLFKALKHVHSFGIIHRDVKPGNFL---------YNRETG 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 311 RDertlinpdiKVVDFGSATYDDEHHSTLVS---TRHYRAPEVILALGwSQPC--DVWSIGCILIEYYLG-FTVFPTHDS 384
Cdd:cd14019 140 KG---------VLVDFGLAQREEDRPEQRAPragTRGFRAPEVLFKCP-HQTTaiDIWSAGVILLSILSGrFPFFFSSDD 209
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 385 KEHLAMMERILGplpkhmiqktrkrkyfhhdrldWDEhssagryvsrrckplkefmlsqdveherLFDLIQKMLEYDPAK 464
Cdd:cd14019 210 IDALAEIATIFG----------------------SDE----------------------------AYDLLDKLLELDPSK 239
                       330
                ....*....|...
gi 67551261 465 RITLREALKHPFF 477
Cdd:cd14019 240 RITAEEALKHPFF 252
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
167-475 4.63e-21

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: 92.29  E-value: 4.63e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIDhKAGGRHVAVKIVK---NVDRycEAARSEIQVLEHLNTTdpnstfRCVQMLEWFEHHGHICIVFEL 243
Cdd:cd14103   1 LGRGKFGTVYRCVE-KATGKELAAKFIKcrkAKDR--EDVRNEIEIMNQLRHP------RLLQLYDAFETPREMVLVMEY 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 244 L-GLSTYDFIKENGFLPFRLDHIRKMAyQICKSVNFLHSNKLTHTDLKPENILFVqsdyteayNPKIKRdertlinpdIK 322
Cdd:cd14103  72 VaGGELFERVVDDDFELTERDCILFMR-QICEGVQYMHKQGILHLDLKPENILCV--------SRTGNQ---------IK 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 323 VVDFGSATYDDEHHSTLVS--TRHYRAPEVILALGWSQPCDVWSIGciLIEYYL--GFTVFPTHDSKEHLAMMERIlgpl 398
Cdd:cd14103 134 IIDFGLARKYDPDKKLKVLfgTPEFVAPEVVNYEPISYATDMWSVG--VICYVLlsGLSPFMGDNDAETLANVTRA---- 207
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 67551261 399 pkhmiqktrkrkyfhhdrlDWDEHSSAGRYVSRRCKplkefmlsqdveherlfDLIQKMLEYDPAKRITLREALKHP 475
Cdd:cd14103 208 -------------------KWDFDDEAFDDISDEAK-----------------DFISKLLVKDPRKRMSAAQCLQHP 248
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
161-477 5.10e-21

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: 92.27  E-value: 5.10e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIDhKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHGHICIV 240
Cdd:cd06614   2 YKNLEKIGEGASGEVYKATD-RATGKEVAIKKMRLRKQNKELIINEILIMKECK--HPN----IVDYYDSYLVGDELWVV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 241 FELL-GLSTYDFIKENgFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQsdyteaynpkikrdertliNP 319
Cdd:cd06614  75 MEYMdGGSLTDIITQN-PVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSK-------------------DG 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 320 DIKVVDFGSA---TYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEyylgftvfpthdskehlaMMErilG 396
Cdd:cd06614 135 SVKLADFGFAaqlTKEKSKRNSVVGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIE------------------MAE---G 193
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 397 PlPKHMIQKTRKRKYfhhdrldwdehssagRYVSRRCKPLKE-FMLSQDveherLFDLIQKMLEYDPAKRITLREALKHP 475
Cdd:cd06614 194 E-PPYLEEPPLRALF---------------LITTKGIPPLKNpEKWSPE-----FKDFLNKCLVKDPEKRPSAEELLQHP 252

                ..
gi 67551261 476 FF 477
Cdd:cd06614 253 FL 254
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
161-476 5.28e-21

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: 93.33  E-value: 5.28e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIDHKAGgRHVAVKIVKnVDRYCEA----ARSEIQVLEHLNTTDPNSTFRCV----QMLEWFE 232
Cdd:cd07864   9 FDIIGIIGEGTYGQVYKAKDKDTG-ELVALKKVR-LDNEKEGfpitAIREIKILRQLNHRSVVNLKEIVtdkqDALDFKK 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 233 HHGHICIVFE-----LLGLStydfikENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDyteaynp 307
Cdd:cd07864  87 DKGAFYLVFEymdhdLMGLL------ESGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKG------- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 308 kikrdertlinpDIKVVDFGSATY----DDEHHSTLVSTRHYRAPEVILALGWSQPC-DVWSIGCILIEYYLGFTVFPTH 382
Cdd:cd07864 154 ------------QIKLADFGLARLynseESRPYTNKVITLWYRPPELLLGEERYGPAiDVWSCGCILGELFTKKPIFQAN 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 383 DSKEHLAMMERILG-PLPKHMIQKTrKRKYFHHDRLDwdehssagRYVSRRCKPLKEFMLSQDVeherlfDLIQKMLEYD 461
Cdd:cd07864 222 QELAQLELISRLCGsPCPAVWPDVI-KLPYFNTMKPK--------KQYRRRLREEFSFIPTPAL------DLLDHMLTLD 286
                       330
                ....*....|....*
gi 67551261 462 PAKRITLREALKHPF 476
Cdd:cd07864 287 PSKRCTAEQALNSPW 301
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
160-477 5.31e-21

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: 92.26  E-value: 5.31e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDhKAGGRHVAVKIVK---NVDRYceAARSEIQVLEHLNTTdpnstfRCVQMLEWFEHHGH 236
Cdd:cd14114   3 HYDILEELGTGAFGVVHRCTE-RATGNNFAAKFIMtphESDKE--TVRKEIQIMNQLHHP------KLINLHDAFEDDNE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELL-GLSTYDFIKENGFLPFRLDHIRKMAyQICKSVNFLHSNKLTHTDLKPENILFVQSDYTEaynpkikrdert 315
Cdd:cd14114  74 MVLILEFLsGGELFERIAAEHYKMSEAEVINYMR-QVCEGLCHMHENNIVHLDIKPENIMCTTKRSNE------------ 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 316 linpdIKVVDFGSATYDDEHHSTLVS--TRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMMER 393
Cdd:cd14114 141 -----VKLIDFGLATHLDPKESVKVTtgTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKS 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 394 IlgplpkhmiqktrkrkyfhhdrlDWDEHSSAGRYVSRRCKplkefmlsqdveherlfDLIQKMLEYDPAKRITLREALK 473
Cdd:cd14114 216 C-----------------------DWNFDDSAFSGISEEAK-----------------DFIRKLLLADPNKRMTIHQALE 255

                ....
gi 67551261 474 HPFF 477
Cdd:cd14114 256 HPWL 259
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
161-477 5.31e-21

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: 92.39  E-value: 5.31e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIDHKAGgRHVAVKIV---KNVDRYCEAARSEIQVleHLNTTDPNstfrcvqMLEWFEH--HG 235
Cdd:cd14069   3 WDLVQTLGEGAFGEVFLAVNRNTE-EAVAVKFVdmkRAPGDCPENIKKEVCI--QKMLSHKN-------VVRFYGHrrEG 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 236 HICIVF-ELL-GLSTYDFIK-ENGFLPfrlDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDyteaynpkikrd 312
Cdd:cd14069  73 EFQYLFlEYAsGGELFDKIEpDVGMPE---DVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDEND------------ 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 313 ertlinpDIKVVDFGSAT---YDDEHH--STLVSTRHYRAPEVILALGW-SQPCDVWSIGCILIeyylgftvfpthdske 386
Cdd:cd14069 138 -------NLKISDFGLATvfrYKGKERllNKMCGTLPYVAPELLAKKKYrAEPVDVWSCGIVLF---------------- 194
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 387 hlAMMeriLGPLPkhmiqktrkrkyfhhdrldWDEHSSA-GRYVS-RRCKPLKE---FMLSQDVeherlFDLIQKMLEYD 461
Cdd:cd14069 195 --AML---AGELP-------------------WDQPSDScQEYSDwKENKKTYLtpwKKIDTAA-----LSLLRKILTEN 245
                       330
                ....*....|....*.
gi 67551261 462 PAKRITLREALKHPFF 477
Cdd:cd14069 246 PNKRITIEDIKKHPWY 261
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
161-476 5.41e-21

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: 92.32  E-value: 5.41e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECiDHKAGGRHVAVKIV-KNVDRYCE-AARSEIQVLEHLntTDPNstfrCVQMLEWFEHHGHIC 238
Cdd:cd14185   2 YEIGRTIGDGNFAVVKEC-RHWNENQEYAMKIIdKSKLKGKEdMIESEILIIKSL--SHPN----IVKLFEVYETEKEIY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 239 IVFELL-GLSTYDFIKENgfLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfVQsdyteaYNPkikrDERTli 317
Cdd:cd14185  75 LILEYVrGGDLFDAIIES--VKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLL-VQ------HNP----DKST-- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 318 npDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVF--PTHDSKEHLAMMEriL 395
Cdd:cd14185 140 --TLKLADFGLAKYVTGPIFTVCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFrsPERDQEELFQIIQ--L 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 396 GplpkhmiqktrkrkyfHHDRLD--WDEHSSAGRyvsrrckplkefmlsqdveherlfDLIQKMLEYDPAKRITLREALK 473
Cdd:cd14185 216 G----------------HYEFLPpyWDNISEAAK------------------------DLISRLLVVDPEKRYTAKQVLQ 255

                ...
gi 67551261 474 HPF 476
Cdd:cd14185 256 HPW 258
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
160-476 6.17e-21

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: 92.31  E-value: 6.17e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDhKAGGRHVAVKIV---KNVDRYCEAARsEIQVLEHLNttDPNSTfrcvQMLEWFEHHGH 236
Cdd:cd06609   2 LFTLLERIGKGSFGEVYKGID-KRTNQVVAIKVIdleEAEDEIEDIQQ-EIQFLSQCD--SPYIT----KYYGSFLKGSK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELL-GLSTYDFIKENgflPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyTEaynpkikrdert 315
Cdd:cd06609  74 LWIIMEYCgGGSVLDLLKPG---PLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILL-----SE------------ 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 316 liNPDIKVVDFGSA---TYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGftvFPTHdSKEHlAMme 392
Cdd:cd06609 134 --EGDVKLADFGVSgqlTSTMSKRNTFVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKG---EPPL-SDLH-PM-- 204
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 393 RILGPLPKHMIqktrkrkyfhhDRLDWDEHSsagryvsrrcKPLKEFmlsqdveherlfdlIQKMLEYDPAKRITLREAL 472
Cdd:cd06609 205 RVLFLIPKNNP-----------PSLEGNKFS----------KPFKDF--------------VELCLNKDPKERPSAKELL 249

                ....
gi 67551261 473 KHPF 476
Cdd:cd06609 250 KHKF 253
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
162-476 6.87e-21

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: 91.88  E-value: 6.87e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 162 EIVDTLGEGAFGKVVECIdHKAGGRHVAVKIVKNVDRycEAARSEI-QVLEHLNTTDPNSTFRCVQMlewFEHHGHICIV 240
Cdd:cd06623   4 ERVKVLGQGSSGVVYKVR-HKPTGKIYALKKIHVDGD--EEFRKQLlRELKTLRSCESPYVVKCYGA---FYKEGEISIV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 241 FELL-GLSTYDFIKENGFLPFRLdhIRKMAYQICKSVNFLHSN-KLTHTDLKPENIlfvqsdyteaynpkikrdertLIN 318
Cdd:cd06623  78 LEYMdGGSLADLLKKVGKIPEPV--LAYIARQILKGLDYLHTKrHIIHRDIKPSNL---------------------LIN 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 319 PD--IKVVDFG-SATYDD--EHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGftVFPTHDSKEH--LAMM 391
Cdd:cd06623 135 SKgeVKIADFGiSKVLENtlDQCNTFVGTVTYMSPERIQGESYSYAADIWSLGLTLLECALG--KFPFLPPGQPsfFELM 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 392 ERIL-GPLPkhmiqktrkrkyfhhdRLDWDEHSsagryvsrrckplKEFMlsqdveherlfDLIQKMLEYDPAKRITLRE 470
Cdd:cd06623 213 QAICdGPPP----------------SLPAEEFS-------------PEFR-----------DFISACLQKDPKKRPSAAE 252

                ....*.
gi 67551261 471 ALKHPF 476
Cdd:cd06623 253 LLQHPF 258
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
161-477 8.93e-21

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: 91.56  E-value: 8.93e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIdHKAGGRHVAVKIVkNVDRYCEAARSEIQVLEhlNTTDPNstfrCVQMLEWFEHHGHICIV 240
Cdd:cd06612   5 FDILEKLGEGSYGSVYKAI-HKETGQVVAIKVV-PVEEDLQEIIKEISILK--QCDSPY----IVKYYGSYFKNTDLWIV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 241 FELLGL-STYDFIKENGfLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqsdyteaynpkikrdertlINP 319
Cdd:cd06612  77 MEYCGAgSVSDIMKITN-KTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNIL---------------------LNE 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 320 D--IKVVDFGSA---TYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTvfPTHDSKEHLAMMERI 394
Cdd:cd06612 135 EgqAKLADFGVSgqlTDTMAKRNTVIGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKP--PYSDIHPMRAIFMIP 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 395 LGPLPKHMIQKtrkrkyfhhdrlDWDehssagryvsrrckplKEFMlsqdveherlfDLIQKMLEYDPAKRITLREALKH 474
Cdd:cd06612 213 NKPPPTLSDPE------------KWS----------------PEFN-----------DFVKKCLVKDPEERPSAIQLLQH 253

                ...
gi 67551261 475 PFF 477
Cdd:cd06612 254 PFI 256
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
161-477 1.34e-20

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


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 91.67  E-value: 1.34e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIDhKAGGRHVAVKivknvdryceaarsEIQvLEHLNTTdPNSTFRCVQMLEWFEHHGHICI- 239
Cdd:cd07844   2 YKKLDKLGEGSYATVYKGRS-KLTGQLVALK--------------EIR-LEHEEGA-PFTAIREASLLKDLKHANIVTLh 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 240 -----------VFELL--GLSTYdFIKENGFLpfRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqSDYTEayn 306
Cdd:cd07844  65 diihtkktltlVFEYLdtDLKQY-MDDCGGGL--SMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLI--SERGE--- 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 307 pkikrdertlinpdIKVVDFGSA--------TYDDEhhstlVSTRHYRAPEVIL-ALGWSQPCDVWSIGCILIEYYLGFT 377
Cdd:cd07844 137 --------------LKLADFGLAraksvpskTYSNE-----VVTLWYRPPDVLLgSTEYSTSLDMWGVGCIFYEMATGRP 197
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 378 VFPTH-DSKEHLAMMERILG-PLPKHMIQKTRKRKYfhhdrldwdehsSAGRYVSRRCKPLKEFMLSQDVEHERlFDLIQ 455
Cdd:cd07844 198 LFPGStDVEDQLHKIFRVLGtPTEETWPGVSSNPEF------------KPYSFPFYPPRPLINHAPRLDRIPHG-EELAL 264
                       330       340
                ....*....|....*....|..
gi 67551261 456 KMLEYDPAKRITLREALKHPFF 477
Cdd:cd07844 265 KFLQYEPKKRISAAEAMKHPYF 286
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
157-475 1.92e-20

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: 90.52  E-value: 1.92e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 157 LSARYEIVDTLGEGAFGKVvECIDHKAGGRHVAVKIVKNVDRYCEAAR--SEIQVLEHLnttdpnstfrcvqmlewfeHH 234
Cdd:cd14078   1 LLKYYELHETIGSGGFAKV-KLATHILTGEKVAIKIMDKKALGDDLPRvkTEIEALKNL-------------------SH 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 235 GHICIVFELL--------------GLSTYDFIKENGFLPfrLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqsd 300
Cdd:cd14078  61 QHICRLYHVIetdnkifmvleycpGGELFDYIVAKDRLS--EDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLL----- 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 301 yteaynpkIKRDERtlinpdIKVVDFGSATYD----DEHHSTLVSTRHYRAPEVILALGWSQP-CDVWSIGCILIEYYLG 375
Cdd:cd14078 134 --------LDEDQN------LKLIDFGLCAKPkggmDHHLETCCGSPAYAAPELIQGKPYIGSeADVWSMGVLLYALLCG 199
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 376 FTVFpthDSKEHLAMMERILgplpkhmiqktrKRKYfhhDRLDWDEHSSAgryvsrrckplkefmlsqdveherlfDLIQ 455
Cdd:cd14078 200 FLPF---DDDNVMALYRKIQ------------SGKY---EEPEWLSPSSK--------------------------LLLD 235
                       330       340
                ....*....|....*....|
gi 67551261 456 KMLEYDPAKRITLREALKHP 475
Cdd:cd14078 236 QMLQVDPKKRITVKELLNHP 255
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
161-484 1.94e-20

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: 91.60  E-value: 1.94e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVEcidhkagGRHvavKIVKNVdryceAARSEIQvLEHlNTTDPNSTFRCVQMLEWFEH------- 233
Cdd:cd07873   4 YIKLDKLGEGTYATVYK-------GRS---KLTDNL-----VALKEIR-LEH-EEGAPCTAIREVSLLKDLKHanivtlh 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 234 -----HGHICIVFELLGLSTYDFIKENGFLpFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteaynpk 308
Cdd:cd07873  67 diihtEKSLTLVFEYLDKDLKQYLDDCGNS-INMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLI------------ 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 309 ikrDERTlinpDIKVVDFGSA--------TYDDEhhstlVSTRHYRAPEVIL-ALGWSQPCDVWSIGCILIEYYLGFTVF 379
Cdd:cd07873 134 ---NERG----ELKLADFGLAraksiptkTYSNE-----VVTLWYRPPDILLgSTDYSTQIDMWGVGCIFYEMSTGRPLF 201
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 380 PTHDSKEHLAMMERILGPLPKHMIQKTRKRKYFhhdrldwdehsSAGRYVSRRCKPLKEFMLSQDVEHerlFDLIQKMLE 459
Cdd:cd07873 202 PGSTVEEQLHFIFRILGTPTEETWPGILSNEEF-----------KSYNYPKYRADALHNHAPRLDSDG---ADLLSKLLQ 267
                       330       340
                ....*....|....*....|....*
gi 67551261 460 YDPAKRITLREALKHPFFDLLKKSI 484
Cdd:cd07873 268 FEGRKRISAEEAMKHPYFHSLGERI 292
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
160-475 2.26e-20

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: 90.94  E-value: 2.26e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDHKAGGRHVAVKIVK-NVDRYCEAAR--SEIQVLEHLnTTDPNSTFrcVQMLEWFEHHGH 236
Cdd:cd14052   1 RFANVELIGSGEFSQVYKVSERVPTGKVYAVKKLKpNYAGAKDRLRrlEEVSILREL-TLDGHDNI--VQLIDSWEYHGH 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELLGLSTYD-FIKENGFLPfRLDHIR--KMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyTEAYNpkikrde 313
Cdd:cd14052  78 LYIQTELCENGSLDvFLSELGLLG-RLDEFRvwKILVELSLGLRFIHDHHFVHLDLKPANVLI-----TFEGT------- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 314 rtlinpdIKVVDFGSAT-YDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGfTVFPthDSKEHLamme 392
Cdd:cd14052 145 -------LKIGDFGMATvWPLIRGIEREGDREYIAPEILSEHMYDKPADIFSLGLILLEAAAN-VVLP--DNGDAW---- 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 393 rilgplpkhmiQKTRKRKYFHHDRLDW-DEHSSAGRYVSRRCKPLKEFMLSQDVEHerlfdLIQKMLEYDPAKRITLREA 471
Cdd:cd14052 211 -----------QKLRSGDLSDAPRLSStDLHSASSPSSNPPPDPPNMPILSGSLDR-----VVRWMLSPEPDRRPTADDV 274

                ....
gi 67551261 472 LKHP 475
Cdd:cd14052 275 LATP 278
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
161-472 3.37e-20

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: 90.43  E-value: 3.37e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECiDHKAGGRHVAVKIVK--NVDRYCEAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHGHIC 238
Cdd:cd13996   8 FEEIELLGSGGFGSVYKV-RNKVDGVTYAIKKIRltEKSSASEKVLREVKALAKLN--HPN----IVRYYTAWVEEPPLY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 239 IVFELLGLST-YDFI-KENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYTeaynpkikrdertl 316
Cdd:cd13996  81 IQMELCEGGTlRDWIdRRNSSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDDLQ-------------- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 317 inpdIKVVDFGSATYDDEHHSTL-----------------VSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVF 379
Cdd:cd13996 147 ----VKIGDFGLATSIGNQKRELnnlnnnnngntsnnsvgIGTPLYASPEQLDGENYNEKADIYSLGIILFEMLHPFKTA 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 380 pthdskehlamMERIlgplpkHMIQKTRKRKYFHhdrldwdehssagryvsrrckplkEFMLSQDVEHerlfDLIQKMLE 459
Cdd:cd13996 223 -----------MERS------TILTDLRNGILPE------------------------SFKAKHPKEA----DLIQSLLS 257
                       330
                ....*....|...
gi 67551261 460 YDPAKRITLREAL 472
Cdd:cd13996 258 KNPEERPSAEQLL 270
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
167-477 3.44e-20

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: 90.06  E-value: 3.44e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGkVVECIDHKAGGRHV--AVKIVKNVD------RYCEAARSEIQVLEHLNTTDPNSTFRCVQMLewfehHGHIC 238
Cdd:cd13994   1 IGKGATS-VVRIVTKKNPRSGVlyAVKEYRRRDdeskrkDYVKRLTSEYIISSKLHHPNIVKVLDLCQDL-----HGKWC 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 239 IVFELL-GLSTYDFIKENGFLPFrlDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteaynpkikrDERTLi 317
Cdd:cd13994  75 LVMEYCpGGDLFTLIEKADSLSL--EEKDCFFKQILRGVAYLHSHGIAHRDLKPENILL---------------DEDGV- 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 318 npdIKVVDFGSA-----TYDDEHHST--LVSTRHYRAPEVILALGWS-QPCDVWSIGCILIEYYLGFtvfpthdskehla 389
Cdd:cd13994 137 ---LKLTDFGTAevfgmPAEKESPMSagLCGSEPYMAPEVFTSGSYDgRAVDVWSCGIVLFALFTGR------------- 200
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 390 mmerilGPLPKHMIQKTRKRKYFHHDRLDWDEHSSAGRYVSRRCKplkefmlsqdveherlfDLIQKMLEYDPAKRITLR 469
Cdd:cd13994 201 ------FPWRSAKKSDSAYKAYEKSGDFTNGPYEPIENLLPSECR-----------------RLIYRMLHPDPEKRITID 257

                ....*...
gi 67551261 470 EALKHPFF 477
Cdd:cd13994 258 EALNDPWV 265
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
160-476 4.14e-20

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: 90.56  E-value: 4.14e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIdHKAGGRHVAVKIV----------KNVDRYCEAARSeiqvLEHLNTtdpnstfrcVQMLE 229
Cdd:cd14086   2 EYDLKEELGKGAFSVVRRCV-QKSTGQEFAAKIIntkklsardhQKLEREARICRL----LKHPNI---------VRLHD 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 230 WFEHHGHICIVFELL-GLSTYDFIKENGFlpFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpk 308
Cdd:cd14086  68 SISEEGFHYLVFDLVtGGELFEDIVAREF--YSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSK------- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 309 ikrdertliNPDIKVVDFGSATY---DDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDsk 385
Cdd:cd14086 139 ---------GAAVKLADFGLAIEvqgDQQAWFGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDED-- 207
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 386 ehlammerilgplpKHMIQKTRKRKYFHHDRLDWDEhssagryVSRRCKplkefmlsqdveherlfDLIQKMLEYDPAKR 465
Cdd:cd14086 208 --------------QHRLYAQIKAGAYDYPSPEWDT-------VTPEAK-----------------DLINQMLTVNPAKR 249
                       330
                ....*....|.
gi 67551261 466 ITLREALKHPF 476
Cdd:cd14086 250 ITAAEALKHPW 260
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
167-476 4.32e-20

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: 89.65  E-value: 4.32e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIdHKAGGRH-VAVKIVKNVDRYCEAAR---SEIQVLEHLNttDPNstfrCVQMLEWFEHHGHICIVFE 242
Cdd:cd14121   3 LGSGTYATVYKAY-RKSGAREvVAVKCVSKSSLNKASTEnllTEIELLKKLK--HPH----IVELKDFQWDEEHIYLIME 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 243 LLG---LSTydFIKENGFLPFRLdhIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDyteaynpkikrdertliNP 319
Cdd:cd14121  76 YCSggdLSR--FIRSRRTLPEST--VRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRY-----------------NP 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 320 DIKVVDFGSATY--DDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEhlaMMERILGP 397
Cdd:cd14121 135 VLKLADFGFAQHlkPNDEAHSLRGSPLYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFASRSFEE---LEEKIRSS 211
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 67551261 398 LPKHMiqktrkrkyfhhdrldwdehsSAGRYVSRRCKplkefmlsqdveherlfDLIQKMLEYDPAKRITLREALKHPF 476
Cdd:cd14121 212 KPIEI---------------------PTRPELSADCR-----------------DLLLRLLQRDPDRRISFEEFFAHPF 252
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
161-476 4.62e-20

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: 90.02  E-value: 4.62e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIDhKAGGRHVAVKIVKNvdRYCEAARS---------EIQVLEHLNttDPNstfrCVQMLEWF 231
Cdd:cd14196   7 YDIGEELGSGQFAIVKKCRE-KSTGLEYAAKFIKK--RQSRASRRgvsreeierEVSILRQVL--HPN----IITLHDVY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 232 EHHGHICIVFELL-GLSTYDFIKENGFLpfRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVqsdyteaynpkik 310
Cdd:cd14196  78 ENRTDVVLILELVsGGELFDFLAQKESL--SEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLL------------- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 311 rdERTLINPDIKVVDFGSA--TYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHL 388
Cdd:cd14196 143 --DKNIPIPHIKLIDFGLAheIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETL 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 389 AMMERIlgplpkhmiqktrkrkyfhhdRLDWDEhssagryvsrrckplkEFmLSQDVEHERlfDLIQKMLEYDPAKRITL 468
Cdd:cd14196 221 ANITAV---------------------SYDFDE----------------EF-FSHTSELAK--DFIRKLLVKETRKRLTI 260

                ....*...
gi 67551261 469 REALKHPF 476
Cdd:cd14196 261 QEALRHPW 268
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
159-477 7.54e-20

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: 90.12  E-value: 7.54e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 159 ARYEIVDTLGEGAFGKVVECIDHKAGgRHVAVKIVKnVDRYCE----AARSEIQVLehLNTTDPNstfrCVQMLEWF--E 232
Cdd:cd07845   7 TEFEKLNRIGEGTYGIVYRARDTTSG-EIVALKKVR-MDNERDgipiSSLREITLL--LNLRHPN----IVELKEVVvgK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 233 HHGHICIVFE--------LLglstydfikENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQsdytea 304
Cdd:cd07845  79 HLDSIFLVMEyceqdlasLL---------DNMPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTD------ 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 305 ynpkikrdertliNPDIKVVDFGSA---TYDDEHHSTLVSTRHYRAPEVIL-ALGWSQPCDVWSIGCILIEYYLGFTVFP 380
Cdd:cd07845 144 -------------KGCLKIADFGLArtyGLPAKPMTPKVVTLWYRAPELLLgCTTYTTAIDMWAVGCILAELLAHKPLLP 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 381 THDSKEHLAMMERILGPlPKHMIQKtrkrkyfhhdrlDWDEHSSAGRYVSRRcKP---LK-EF-MLSQDVeherlFDLIQ 455
Cdd:cd07845 211 GKSEIEQLDLIIQLLGT-PNESIWP------------GFSDLPLVGKFTLPK-QPynnLKhKFpWLSEAG-----LRLLN 271
                       330       340
                ....*....|....*....|..
gi 67551261 456 KMLEYDPAKRITLREALKHPFF 477
Cdd:cd07845 272 FLLMYDPKKRATAEEALESSYF 293
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
162-371 8.34e-20

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: 88.76  E-value: 8.34e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261    162 EIVDTLGEGAFGKVVECI-DHKAGGRH--VAVKIVKN--VDRYCEAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHGH 236
Cdd:smart00221   2 TLGKKLGEGAFGEVYKGTlKGKGDGKEveVAVKTLKEdaSEQQIEEFLREARIMRKLD--HPN----IVKLLGVCTEEEP 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261    237 ICIVFELL-GLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfVQSDYTeaynpkikrdert 315
Cdd:smart00221  76 LMIVMEYMpGGDLLDYLRKNRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCL-VGENLV------------- 141
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261    316 linpdIKVVDFGSA--TYDDEHHSTLVSTRHYR--APEVILALGWSQPCDVWSIGCILIE 371
Cdd:smart00221 142 -----VKISDFGLSrdLYDDDYYKVKGGKLPIRwmAPESLKEGKFTSKSDVWSFGVLLWE 196
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
161-394 8.61e-20

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: 89.39  E-value: 8.61e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVeCIDHKAGGRHVAVKIVKNVD----RYCEAARSEIQVLEHLNTtdPNstfrCVQMLEWFEHHGH 236
Cdd:cd14209   3 FDRIKTLGTGSFGRVM-LVRHKETGNYYAMKILDKQKvvklKQVEHTLNEKRILQAINF--PF----LVKLEYSFKDNSN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELL-GLSTYDFIKENGflPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrdert 315
Cdd:cd14209  76 LYMVMEYVpGGEMFSHLRRIG--RFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGY-------------- 139
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 67551261 316 linpdIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHdskEHLAMMERI 394
Cdd:cd14209 140 -----IKVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFAD---QPIQIYEKI 210
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
160-477 1.41e-19

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: 88.64  E-value: 1.41e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDHKAGgRHVAVKIVKnvdryceaarseiqvLEHLNTTDPNSTFRCVQMLEWFEH------ 233
Cdd:cd07839   1 KYEKLEKIGEGTYGTVFKAKNRETH-EIVALKRVR---------------LDDDDEGVPSSALREICLLKELKHknivrl 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 234 ----HGH--ICIVFELL--GLSTYdFIKENGflpfRLDH--IRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQsdyte 303
Cdd:cd07839  65 ydvlHSDkkLTLVFEYCdqDLKKY-FDSCNG----DIDPeiVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINK----- 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 304 aynpkikrdertliNPDIKVVDFGSA--------TYDDEhhstlVSTRHYRAPEVIL-ALGWSQPCDVWSIGCILIEYY- 373
Cdd:cd07839 135 --------------NGELKLADFGLArafgipvrCYSAE-----VVTLWYRPPDVLFgAKLYSTSIDMWSAGCIFAELAn 195
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 374 LGFTVFPTHDSKEHLAMMERILGPlPKHMIqktrkrkyfhhdrldWDEHSSAGRYVSRrckPLKEFMLSQDVEHERLF-- 451
Cdd:cd07839 196 AGRPLFPGNDVDDQLKRIFRLLGT-PTEES---------------WPGVSKLPDYKPY---PMYPATTSLVNVVPKLNst 256
                       330       340
                ....*....|....*....|....*...
gi 67551261 452 --DLIQKMLEYDPAKRITLREALKHPFF 477
Cdd:cd07839 257 grDLLQNLLVCNPVQRISAEEALQHPYF 284
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
167-476 1.50e-19

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: 88.05  E-value: 1.50e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECiDHKAGGRHVAVKIV---KNVDRYCEAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHGHICIVFEL 243
Cdd:cd14009   1 IGRGSFATVWKG-RHKQTGEVVAIKEIsrkKLNKKLQENLESEIAILKSIK--HPN----IVRLYDVQKTEDFIYLVLEY 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 244 LGLSTY-DFIKENGFLPfrLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrdertliNPDIK 322
Cdd:cd14009  74 CAGGDLsQYIRKRGRLP--EAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGD----------------DPVLK 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 323 VVDFGSATY--DDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFpthDSKEHLAMMERilgplpk 400
Cdd:cd14009 136 IADFGFARSlqPASMAETLCGSPLYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPF---RGSNHVQLLRN------- 205
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 67551261 401 hmIQKTRKRKYFHHDRLdwdehssagryVSRRCKplkefmlsqdveherlfDLIQKMLEYDPAKRITLREALKHPF 476
Cdd:cd14009 206 --IERSDAVIPFPIAAQ-----------LSPDCK-----------------DLLRRLLRRDPAERISFEEFFAHPF 251
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
161-476 3.95e-19

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: 87.39  E-value: 3.95e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTL-GEGAFGKVVECIDHKaGGRHVAVKIVKNvdrycEAARSEIQVLEHLNTTdpnstFRC------VQMLEWFEH 233
Cdd:cd14174   3 YRLTDELlGEGAYAKVQGCVSLQ-NGKEYAVKIIEK-----NAGHSRSRVFREVETL-----YQCqgnkniLELIEFFED 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 234 HGHICIVFE-LLGLSTYDFIKENGFlpFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqSDYTEAYNPkikrd 312
Cdd:cd14174  72 DTRFYLVFEkLRGGSILAHIQKRKH--FNEREASRVVRDIASALDFLHTKGIAHRDLKPENIL---CESPDKVSP----- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 313 ertlinpdIKVVDF--GSATYDDEHHSTLVS--------TRHYRAPEVI-----LALGWSQPCDVWSIGCILIEYYLGFT 377
Cdd:cd14174 142 --------VKICDFdlGSGVKLNSACTPITTpelttpcgSAEYMAPEVVevftdEATFYDKRCDLWSLGVILYIMLSGYP 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 378 VFPTHDSKEHLAMMERILGPLPKHMIQKTRKRKYFHHDRlDWDEHSSAGRyvsrrckplkefmlsqdveherlfDLIQKM 457
Cdd:cd14174 214 PFVGHCGTDCGWDRGEVCRVCQNKLFESIQEGKYEFPDK-DWSHISSEAK------------------------DLISKL 268
                       330
                ....*....|....*....
gi 67551261 458 LEYDPAKRITLREALKHPF 476
Cdd:cd14174 269 LVRDAKERLSAAQVLQHPW 287
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
165-476 4.48e-19

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: 86.89  E-value: 4.48e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 165 DTLGEGAFGKVVECIDhKAGGRHVAVKIVK-NVDRYCEAARSEIQVLEHLNTTDpnstfrCVQMLEWFEHHGHICIVFEL 243
Cdd:cd14193  10 EILGGGRFGQVHKCEE-KSSGLKLAAKIIKaRSQKEKEEVKNEIEVMNQLNHAN------LIQLYDAFESRNDIVLVMEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 244 L-GLSTYDFIKENGFLPFRLDHIRKMAyQICKSVNFLHSNKLTHTDLKPENILFVQSDYTEaynpkikrdertlinpdIK 322
Cdd:cd14193  83 VdGGELFDRIIDENYNLTELDTILFIK-QICEGIQYMHQMYILHLDLKPENILCVSREANQ-----------------VK 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 323 VVDFGSATYDDEHHSTLVS--TRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLammERILGplpk 400
Cdd:cd14193 145 IIDFGLARRYKPREKLRVNfgTPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETL---NNILA---- 217
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 67551261 401 hmiqktrkrkyfhhdrLDWDEHSSAGRYVSRRCKplkefmlsqdveherlfDLIQKMLEYDPAKRITLREALKHPF 476
Cdd:cd14193 218 ----------------CQWDFEDEEFADISEEAK-----------------DFISKLLIKEKSWRMSASEALKHPW 260
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
162-477 7.10e-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: 86.24  E-value: 7.10e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 162 EIVDTLGEGAFGkVVECIDHKAGGRHVAVKIVK-NVDrycEAAR----SEIQVLEHLNTtdPNstfrCVQMLEWFEHHGH 236
Cdd:cd06605   4 EYLGELGEGNGG-VVSKVRHRPSGQIMAVKVIRlEID---EALQkqilRELDVLHKCNS--PY----IVGFYGAFYSEGD 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELLGLSTYD-FIKENGFLPfrLDHIRKMAYQICKSVNFLHSN-KLTHTDLKPENILFvqsdyteaynpkikrDER 314
Cdd:cd06605  74 ISICMEYMDGGSLDkILKEVGRIP--ERILGKIAVAVVKGLIYLHEKhKIIHRDVKPSNILV---------------NSR 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 315 TlinpDIKVVDFGSATY-DDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLA---M 390
Cdd:cd06605 137 G----QVKLCDFGVSGQlVDSLAKTFVGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPYPPPNAKPSMMifeL 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 391 MERIL-GPLPKhmiqktrkrkyfhhdrldwdehssagryvsrrckplkefmLSQDVEHERLFDLIQKMLEYDPAKRITLR 469
Cdd:cd06605 213 LSYIVdEPPPL----------------------------------------LPSGKFSPDFQDFVSQCLQKDPTERPSYK 252

                ....*...
gi 67551261 470 EALKHPFF 477
Cdd:cd06605 253 ELMEHPFI 260
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
165-421 1.24e-18

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: 85.83  E-value: 1.24e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 165 DTLGEGAFGKVVEcidhkagGRH-------VAVKIV--KNVDRYCEAARSEIQVLEHLNTTDpnstfrCVQMLEWFEHHG 235
Cdd:cd14202   8 DLIGHGAFAVVFK-------GRHkekhdleVAVKCInkKNLAKSQTLLGKEIKILKELKHEN------IVALYDFQEIAN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 236 HICIVFELL-GLSTYDFIKENGFLpfRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYTEAyNPKikrder 314
Cdd:cd14202  75 SVYLVMEYCnGGDLADYLHTMRTL--SEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGGRKS-NPN------ 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 315 tliNPDIKVVDFGSATY--DDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMME 392
Cdd:cd14202 146 ---NIRIKIADFGFARYlqNNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQDLRLFYE 222
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 67551261 393 --RILGP-LP-------KHMIQKTRKRKyfHHDRLDWDE 421
Cdd:cd14202 223 knKSLSPnIPretsshlRQLLLGLLQRN--QKDRMDFDE 259
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
162-371 1.36e-18

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 85.28  E-value: 1.36e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261    162 EIVDTLGEGAFGKVVECI---DHKAGGRHVAVKIVKNV--DRYCEAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHGH 236
Cdd:smart00219   2 TLGKKLGEGAFGEVYKGKlkgKGGKKKVEVAVKTLKEDasEQQIEEFLREARIMRKLD--HPN----VVKLLGVCTEEEP 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261    237 ICIVFELL-GLSTYDFIKENGfLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfVQSDYTeaynpkikrdert 315
Cdd:smart00219  76 LYIVMEYMeGGDLLSYLRKNR-PKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCL-VGENLV------------- 140
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261    316 linpdIKVVDFGSA--TYDDEHHSTLVSTRHYR--APEVILALGWSQPCDVWSIGCILIE 371
Cdd:smart00219 141 -----VKISDFGLSrdLYDDDYYRKRGGKLPIRwmAPESLKEGKFTSKSDVWSFGVLLWE 195
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
160-384 1.47e-18

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: 85.46  E-value: 1.47e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDHkAGGRHVAVK--IVKNVDRYcEAARSEIQVLEHLnTTDPNstfrCVQMLewfeHHGHI 237
Cdd:cd13985   1 RYQVTKQLGEGGFSYVYLAHDV-NTGRRYALKrmYFNDEEQL-RVAIKEIEIMKRL-CGHPN----IVQYY----DSAIL 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 238 --------CIVFELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNK--LTHTDLKPENILFvqsdyteaynp 307
Cdd:cd13985  70 ssegrkevLLLMEYCPGSLVDILEKSPPSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILF----------- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 308 kikRDERTlinpdIKVVDFGSAT--------------YDDE--HHSTLVstrhYRAPEVI---LALGWSQPCDVWSIGCI 368
Cdd:cd13985 139 ---SNTGR-----FKLCDFGSATtehypleraeevniIEEEiqKNTTPM----YRAPEMIdlySKKPIGEKADIWALGCL 206
                       250
                ....*....|....*.
gi 67551261 369 LieYYLGFTVFPTHDS 384
Cdd:cd13985 207 L--YKLCFFKLPFDES 220
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
161-477 1.79e-18

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: 85.40  E-value: 1.79e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIDhKAGGRHVAVKIVknvdryceaarseiqvleHLNTTD--PNSTFRCVQMLEWFEH----- 233
Cdd:cd07870   2 YLNLEKLGEGSYATVYKGIS-RINGQLVALKVI------------------SMKTEEgvPFTAIREASLLKGLKHanivl 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 234 -HGHI------CIVFELL--GLSTYDFIKENGFLPFrldHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqSDYTEa 304
Cdd:cd07870  63 lHDIIhtketlTFVFEYMhtDLAQYMIQHPGGLHPY---NVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLI--SYLGE- 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 305 ynpkikrdertlinpdIKVVDFGSA---TYDDEHHSTLVSTRHYRAPEVIL-ALGWSQPCDVWSIGCILIEYYLGFTVFP 380
Cdd:cd07870 137 ----------------LKLADFGLArakSIPSQTYSSEVVTLWYRPPDVLLgATDYSSALDIWGAGCIFIEMLQGQPAFP 200
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 381 -THDSKEHLAMMERILGPLPKHMIQKTRKRKYFHHDRLDWDEHSSAgRYVSRRckplkefmLSQDVEHErlfDLIQKMLE 459
Cdd:cd07870 201 gVSDVFEQLEKIWTVLGVPTEDTWPGVSKLPNYKPEWFLPCKPQQL-RVVWKR--------LSRPPKAE---DLASQMLM 268
                       330
                ....*....|....*...
gi 67551261 460 YDPAKRITLREALKHPFF 477
Cdd:cd07870 269 MFPKDRISAQDALLHPYF 286
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
160-477 1.80e-18

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: 85.35  E-value: 1.80e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIdHKAGGRHVAVKIV----------KNVDRYCEAARSEIQVLEHLnTTDPNstfrCVQMLE 229
Cdd:cd14182   4 KYEPKEILGRGVSSVVRRCI-HKPTRQEYAVKIIditgggsfspEEVQELREATLKEIDILRKV-SGHPN----IIQLKD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 230 WFEHHGHICIVFELLGLST-YDFIKENGFLPFRldHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteaynpk 308
Cdd:cd14182  78 TYETNTFFFLVFDLMKKGElFDYLTEKVTLSEK--ETRKIMRALLEVICALHKLNIVHRDLKPENILL------------ 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 309 ikrDErtliNPDIKVVDFGSATYDDEHH--STLVSTRHYRAPEVILAL------GWSQPCDVWSIGCILIEYYLGftvFP 380
Cdd:cd14182 144 ---DD----DMNIKLTDFGFSCQLDPGEklREVCGTPGYLAPEIIECSmddnhpGYGKEVDMWSTGVIMYTLLAG---SP 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 381 THDSKEHLAMMERILGplpkhmiqktrkrKYFHHDRLDWDEHSSAGRyvsrrckplkefmlsqdveherlfDLIQKMLEY 460
Cdd:cd14182 214 PFWHRKQMLMLRMIMS-------------GNYQFGSPEWDDRSDTVK------------------------DLISRFLVV 256
                       330
                ....*....|....*..
gi 67551261 461 DPAKRITLREALKHPFF 477
Cdd:cd14182 257 QPQKRYTAEEALAHPFF 273
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
167-476 2.69e-18

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: 84.66  E-value: 2.69e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIdHKAGGRHVAVKIVKNvdryCEAARSEIQVleHLNTTDPNstfRCVQMLEWFE--HHGHIC--IVFE 242
Cdd:cd14172  12 LGLGVNGKVLECF-HRRTGQKCALKLLYD----SPKARREVEH--HWRASGGP---HIVHILDVYEnmHHGKRCllIIME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 243 LL-GLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrdertliNPDI 321
Cdd:cd14172  82 CMeGGELFSRIQERGDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKEK----------------DAVL 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 322 KVVDFGSATYDDEHHS--TLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMMERilgplp 399
Cdd:cd14172 146 KLTDFGFAKETTVQNAlqTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTGQAISPGMKR------ 219
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 67551261 400 khmiqKTRKRKYfHHDRLDWDEhssagryVSRRCKplkefmlsqdveherlfDLIQKMLEYDPAKRITLREALKHPF 476
Cdd:cd14172 220 -----RIRMGQY-GFPNPEWAE-------VSEEAK-----------------QLIRHLLKTDPTERMTITQFMNHPW 266
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
158-379 6.19e-18

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: 83.47  E-value: 6.19e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 158 SARYEI--VDTLGEGAFGKVVECIDhKAGGRHVAVKIVK---NVDRycEAARSEIQVLEHLNTTDpnstfrCVQMLEWFE 232
Cdd:cd14192   1 NSYYAVcpHEVLGGGRFGQVHKCTE-LSTGLTLAAKIIKvkgAKER--EEVKNEINIMNQLNHVN------LIQLYDAFE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 233 HHGHICIVFELL-GLSTYDFIKENGFLPFRLDHIRkMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYTEaynpkikr 311
Cdd:cd14192  72 SKTNLTLIMEYVdGGELFDRITDESYQLTELDAIL-FTRQICEGVHYLHQHYILHLDLKPENILCVNSTGNQ-------- 142
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 312 dertlinpdIKVVDFGSATYDDEHHSTLVS--TRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVF 379
Cdd:cd14192 143 ---------IKIIDFGLARRYKPREKLKVNfgTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPF 203
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
152-474 6.63e-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: 6.63e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 152 QSGDVlsarYEIVDTLGEGAFGKVVECIdHKAGGRHVAVKIVknvDRYCEAARSEIQVLEHLNTtDPNstfrCVQMLEWF 231
Cdd:cd14177   1 QFTDV----YELKEDIGVGSYSVCKRCI-HRATNMEFAVKII---DKSKRDPSEEIEILMRYGQ-HPN----IITLKDVY 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 232 EHHGHICIVFELL-GLSTYDFIKENGFLPFRldHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVqsdyteaynpkik 310
Cdd:cd14177  68 DDGRYVYLVTELMkGGELLDRILRQKFFSER--EASAVLYTITKTVDYLHCQGVVHRDLKPSNILYM------------- 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 311 rDERTliNPD-IKVVDFGSATYDDEHHSTLVS---TRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPThdske 386
Cdd:cd14177 133 -DDSA--NADsIRICDFGFAKQLRGENGLLLTpcyTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFAN----- 204
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 387 hlammerilGP--LPKHMIQKTRKRKyFHHDRLDWDEHSSAGRyvsrrckplkefmlsqdveherlfDLIQKMLEYDPAK 464
Cdd:cd14177 205 ---------GPndTPEEILLRIGSGK-FSLSGGNWDTVSDAAK------------------------DLLSHMLHVDPHQ 250
                       330
                ....*....|
gi 67551261 465 RITLREALKH 474
Cdd:cd14177 251 RYTAEQVLKH 260
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
161-477 9.23e-18

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: 82.83  E-value: 9.23e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGkVVECIDHKAGGRHVAVKIVKNvdryceaarseiqvlEHLNTTDPNSTFRCVQMLEWFEHHgHICIV 240
Cdd:cd14071   2 YDIERTIGKGNFA-VVKLARHRITKTEVAIKIIDK---------------SQLDEENLKKIYREVQIMKMLNHP-HIIKL 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 241 FE------LLGLST--------YDFIKENGFLPfrLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteayn 306
Cdd:cd14071  65 YQvmetkdMLYLVTeyasngeiFDYLAQHGRMS--EKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLL---------- 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 307 pkikrDErtliNPDIKVVDFGSATY--DDEHHSTLVSTRHYRAPEVILALGWSQP-CDVWSIGCILieYYLGFTVFPtHD 383
Cdd:cd14071 133 -----DA----NMNIKIADFGFSNFfkPGELLKTWCGSPPYAAPEVFEGKEYEGPqLDIWSLGVVL--YVLVCGALP-FD 200
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 384 SKEHLAMMERILgplpkhmiqktrkrkyfhhdrldwdehssAGRYvsrRCKplkeFMLSQDVEHerlfdLIQKMLEYDPA 463
Cdd:cd14071 201 GSTLQTLRDRVL-----------------------------SGRF---RIP----FFMSTDCEH-----LIRRMLVLDPS 239
                       330
                ....*....|....
gi 67551261 464 KRITLREALKHPFF 477
Cdd:cd14071 240 KRLTIEQIKKHKWM 253
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
161-476 9.80e-18

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: 83.56  E-value: 9.80e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVeCIDHKAGGRHVAVKIV--KNVDRYCEAARSEIQVLEHLNTTDpnstfrCVQMLEWFEHHGHIC 238
Cdd:cd14168  12 FEFKEVLGTGAFSEVV-LAEERATGKLFAVKCIpkKALKGKESSIENEIAVLRKIKHEN------IVALEDIYESPNHLY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 239 IVFELL-GLSTYDFIKENGFlpFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteaYNPkikrDERTli 317
Cdd:cd14168  85 LVMQLVsGGELFDRIVEKGF--YTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLY--------FSQ----DEES-- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 318 npDIKVVDFGSATYDDEHH--STLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVF-PTHDSKehlaMMERI 394
Cdd:cd14168 149 --KIMISDFGLSKMEGKGDvmSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFyDENDSK----LFEQI 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 395 LgplpkhmiqktrkRKYFHHDRLDWDEHSSAGRyvsrrckplkefmlsqdveherlfDLIQKMLEYDPAKRITLREALKH 474
Cdd:cd14168 223 L-------------KADYEFDSPYWDDISDSAK------------------------DFIRNLMEKDPNKRYTCEQALRH 265

                ..
gi 67551261 475 PF 476
Cdd:cd14168 266 PW 267
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
160-371 9.98e-18

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: 82.94  E-value: 9.98e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVeCIDHKAGGRHVAVK---IVKNVDRYCEAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHGH 236
Cdd:cd08218   1 KYVRIKKIGEGSFGKAL-LVKSKEDGKQYVIKeinISKMSPKEREESRKEVAVLSKMK--HPN----IVQYQESFEENGN 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELL-GLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrdert 315
Cdd:cd08218  74 LYIVMDYCdGGDLYKRINAQRGVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGI-------------- 139
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 67551261 316 linpdIKVVDFGSATYDD---EHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIE 371
Cdd:cd08218 140 -----IKLGDFGIARVLNstvELARTCIGTPYYLSPEICENKPYNNKSDIWALGCVLYE 193
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
161-480 1.16e-17

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: 83.15  E-value: 1.16e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIDHKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHGHICIV 240
Cdd:cd06643   7 WEIVGELGDGAFGKVYKAQNKETGILAAAKVIDTKSEEELEDYMVEIDILASCD--HPN----IVKLLDAFYYENNLWIL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 241 FELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVqsdyteaynpkikrdertlINPD 320
Cdd:cd06643  81 IEFCAGGAVDAVMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFT-------------------LDGD 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 321 IKVVDFGSA---TYDDEHHSTLVSTRHYRAPEVILA-----LGWSQPCDVWSIGCILIEYYlgfTVFPTHDSKEHLAMME 392
Cdd:cd06643 142 IKLADFGVSaknTRTLQRRDSFIGTPYWMAPEVVMCetskdRPYDYKADVWSLGVTLIEMA---QIEPPHHELNPMRVLL 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 393 RILGPLPKHMIQKTRkrkyfhhdrldWDEHSSagryvsrrckplkefmlsqdveherlfDLIQKMLEYDPAKRITLREAL 472
Cdd:cd06643 219 KIAKSEPPTLAQPSR-----------WSPEFK---------------------------DFLRKCLEKNVDARWTTSQLL 260

                ....*...
gi 67551261 473 KHPFFDLL 480
Cdd:cd06643 261 QHPFVSVL 268
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
225-476 1.40e-17

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: 82.73  E-value: 1.40e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 225 VQMLEWFEHHGHICIVFEL-LGLSTYDFIKENGFLPfrLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyte 303
Cdd:cd14010  57 LKFYEWYETSNHLWLVVEYcTGGDLETLLRQDGNLP--ESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILL------- 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 304 aynpkikrDErtliNPDIKVVDFG----------------SATYDDEHHSTLVSTR---HYRAPEVILALGWSQPCDVWS 364
Cdd:cd14010 128 --------DG----NGTLKLSDFGlarregeilkelfgqfSDEGNVNKVSKKQAKRgtpYYMAPELFQGGVHSFASDLWA 195
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 365 IGCILIEYYLGFTVFpTHDSKEHLAmmERILGPLPKHMIQKTrkrkyfhhdrldwdehssagryvsrRCKPLKEFMlsqd 444
Cdd:cd14010 196 LGCVLYEMFTGKPPF-VAESFTELV--EKILNEDPPPPPPKV-------------------------SSKPSPDFK---- 243
                       250       260       270
                ....*....|....*....|....*....|..
gi 67551261 445 veherlfDLIQKMLEYDPAKRITLREALKHPF 476
Cdd:cd14010 244 -------SLLKGLLEKDPAKRLSWDELVKHPF 268
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
161-476 1.43e-17

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: 82.53  E-value: 1.43e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKV-----VECIDHKaGGRHVAVKIVK--NVDRYCEAAR--SEIQVLEHLntTDPNstfrCVQMLEWF 231
Cdd:cd14076   3 YILGRTLGEGEFGKVklgwpLPKANHR-SGVQVAIKLIRrdTQQENCQTSKimREINILKGL--THPN----IVRLLDVL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 232 EHHGHICIVFELL-GLSTYDFIKENGFLpfRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQsdyteaynpkik 310
Cdd:cd14076  76 KTKKYIGIVLEFVsGGELFDYILARRRL--KDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDK------------ 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 311 rdertliNPDIKVVDFGSATYDDEHHSTLVSTR----HYRAPEVIL--ALGWSQPCDVWSIGCILIEYYLGFTVFpthDS 384
Cdd:cd14076 142 -------NRNLVITDFGFANTFDHFNGDLMSTScgspCYAAPELVVsdSMYAGRKADIWSCGVILYAMLAGYLPF---DD 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 385 KEHLAMMERIlgplpkhmiqkTRKRKYFHHDRLDWDEH-SSAGRyvsrrckplkefmlsqdveherlfDLIQKMLEYDPA 463
Cdd:cd14076 212 DPHNPNGDNV-----------PRLYRYICNTPLIFPEYvTPKAR------------------------DLLRRILVPNPR 256
                       330
                ....*....|...
gi 67551261 464 KRITLREALKHPF 476
Cdd:cd14076 257 KRIRLSAIMRHAW 269
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
167-476 1.75e-17

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: 82.21  E-value: 1.75e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIdHKAGGRHVAVKIVKNVdrycEAARSEIQVLEH-LNTTDPNSTFRCVQMLEWFEHHGHICIVFELL- 244
Cdd:cd14097   9 LGQGSFGVVIEAT-HKETQTKWAIKKINRE----KAGSSAVKLLEReVDILKHVNHAHIIHLEEVFETPKRMYLVMELCe 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 245 GLSTYDFIKENGFlpFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYTEAynpkikrdertlINPDIKVV 324
Cdd:cd14097  84 DGELKELLLRKGF--FSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSIIDNN------------DKLNIKVT 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 325 DFGSATYD----DEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILieyYLGFTVFPTHDSKEHLAMMERIlgplpk 400
Cdd:cd14097 150 DFGLSVQKyglgEDMLQETCGTPIYMAPEVISAHGYSQQCDIWSIGVIM---YMLLCGEPPFVAKSEEKLFEEI------ 220
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 67551261 401 hmiqktrKRKYFHHDRLDWDEHSSAGRYVsrrckplkefmlsqdveherlfdlIQKMLEYDPAKRITLREALKHPF 476
Cdd:cd14097 221 -------RKGDLTFTQSVWQSVSDAAKNV------------------------LQQLLKVDPAHRMTASELLDNPW 265
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
161-477 3.01e-17

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: 81.59  E-value: 3.01e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIDhKAGGRHVAVKIVKNVD-RYCEAARSEIQVLEHLNTTdpnstfRCVQMLEWFEHHGHICI 239
Cdd:cd14191   4 YDIEERLGSGKFGQVFRLVE-KKTKKVWAGKFFKAYSaKEKENIRQEISIMNCLHHP------KLVQCVDAFEEKANIVM 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 240 VFELL-GLSTYDFIKENGFLPFRLDHIRKMaYQICKSVNFLHSNKLTHTDLKPENILFVQSDYTEaynpkikrdertlin 318
Cdd:cd14191  77 VLEMVsGGELFERIIDEDFELTERECIKYM-RQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTK--------------- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 319 pdIKVVDFGSATYDDEHHS--TLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAmmerilg 396
Cdd:cd14191 141 --IKLIDFGLARRLENAGSlkVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLA------- 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 397 plpkHMIQKTrkrkyfhhdrldWDEHSSAGRYVSRRCKplkefmlsqdveherlfDLIQKMLEYDPAKRITLREALKHPF 476
Cdd:cd14191 212 ----NVTSAT------------WDFDDEAFDEISDDAK-----------------DFISNLLKKDMKARLTCTQCLQHPW 258

                .
gi 67551261 477 F 477
Cdd:cd14191 259 L 259
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
167-395 3.09e-17

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: 81.50  E-value: 3.09e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVvECIDHKAGGRHVAVKIVKN---VDRYCEA-ARSEIQVLEHLNttdpnSTFrCVQMLEWFEHHGHICIVFE 242
Cdd:cd05572   1 LGVGGFGRV-ELVQLKSKGRTFALKCVKKrhiVQTRQQEhIFSEKEILEECN-----SPF-IVKLYRTFKDKKYLYMLME 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 243 L-LGLSTYDFIKENGFLPfrLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrdertlinpdI 321
Cdd:cd05572  74 YcLGGELWTILRDRGLFD--EYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGY-------------------V 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 322 KVVDFGSA--------TYddehhsTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFpTHDSKEHLAMMER 393
Cdd:cd05572 133 KLVDFGFAkklgsgrkTW------TFCGTPEYVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPF-GGDDEDPMKIYNI 205

                ..
gi 67551261 394 IL 395
Cdd:cd05572 206 IL 207
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
161-476 3.36e-17

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: 82.20  E-value: 3.36e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIdHKAGGRHVAVKIVkNVDRYCEAArseiqvleHLNTTDPNSTFRCVQMLEwfehHGHIC-- 238
Cdd:cd14094   5 YELCEVIGKGPFSVVRRCI-HRETGQQFAVKIV-DVAKFTSSP--------GLSTEDLKREASICHMLK----HPHIVel 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 239 -----------IVFELLGLS--TYDFIK--ENGFLpFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYTE 303
Cdd:cd14094  71 letyssdgmlyMVFEFMDGAdlCFEIVKraDAGFV-YSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 304 AynpkikrdertlinpdIKVVDFGSATYDDEHHSTL---VSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFtvFP 380
Cdd:cd14094 150 P----------------VKLGGFGVAIQLGESGLVAggrVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGC--LP 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 381 THDSKEHLamMERILgplpkhmiqktrkRKYFHHDRLDWDEHSSAGRyvsrrckplkefmlsqdveherlfDLIQKMLEY 460
Cdd:cd14094 212 FYGTKERL--FEGII-------------KGKYKMNPRQWSHISESAK------------------------DLVRRMLML 252
                       330
                ....*....|....*.
gi 67551261 461 DPAKRITLREALKHPF 476
Cdd:cd14094 253 DPAERITVYEALNHPW 268
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
157-385 3.43e-17

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: 81.15  E-value: 3.43e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 157 LSARYEIVDTLGEGAFGKVVECIDHKagGRHVAVKIVKNvDRYCEAA-----RSEIQVLEHLNttDPNstfrCVQMLEWF 231
Cdd:cd14161   1 LKHRYEFLETLGKGTYGRVKKARDSS--GRLVAIKSIRK-DRIKDEQdllhiRREIEIMSSLN--HPH----IISVYEVF 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 232 EHHGHICIVFELLGLST-YDFIKENGFLPFRldHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteaynpkik 310
Cdd:cd14161  72 ENSSKIVIVMEYASRGDlYDYISERQRLSEL--EARHFFRQIVSAVHYCHANGIVHRDLKLENILL-------------- 135
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 67551261 311 rDErtliNPDIKVVDFG-SATYD-DEHHSTLVSTRHYRAPEVILALGWSQP-CDVWSIGCILIEYYLGFTVFPTHDSK 385
Cdd:cd14161 136 -DA----NGNIKIADFGlSNLYNqDKFLQTYCGSPLYASPEIVNGRPYIGPeVDSWSLGVLLYILVHGTMPFDGHDYK 208
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
160-371 5.13e-17

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: 80.79  E-value: 5.13e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVeCIDHKAGGRHVAVKIVK--NVDRYCEAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHGHI 237
Cdd:cd08219   1 QYNVLRVVGEGSFGRAL-LVQHVNSDQKYAMKEIRlpKSSSAVEDSRKEAVLLAKMK--HPN----IVAFKESFEADGHL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 238 CIVFELL-GLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQsdyteaynpkikrdertl 316
Cdd:cd08219  74 YIVMEYCdGGDLMQKIKLQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQ------------------ 135
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 67551261 317 iNPDIKVVDFGSA---TYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIE 371
Cdd:cd08219 136 -NGKVKLGDFGSArllTSPGAYACTYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYE 192
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
167-476 6.68e-17

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: 81.23  E-value: 6.68e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIDHKAGGRhVAVKIVKNvdryCEAARSEIQVleHLNTTDPNSTFRCVQMLE-WFEHHGHICIVFELL- 244
Cdd:cd14170  10 LGLGINGKVLQIFNKRTQEK-FALKMLQD----CPKARREVEL--HWRASQCPHIVRIVDVYEnLYAGRKCLLIVMECLd 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 245 GLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQsdyteaynpkiKRDertliNPDIKVV 324
Cdd:cd14170  83 GGELFSRIQDRGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTS-----------KRP-----NAILKLT 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 325 DFGSATYDDEHHS--TLVSTRHYRAPEVILALGWSQPCDVWSIGCILieyYLGFTVFPTHDSKEHLAmmerilgpLPKHM 402
Cdd:cd14170 147 DFGFAKETTSHNSltTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIM---YILLCGYPPFYSNHGLA--------ISPGM 215
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 67551261 403 IQKTRKRKYfHHDRLDWDEHSsagryvsrrckplkefmlsqdvehERLFDLIQKMLEYDPAKRITLREALKHPF 476
Cdd:cd14170 216 KTRIRMGQY-EFPNPEWSEVS------------------------EEVKMLIRNLLKTEPTQRMTITEFMNHPW 264
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
161-371 7.75e-17

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: 80.15  E-value: 7.75e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIdHKAGGRHVAVK---IVKNVDRYCEAARSEIQVLEHLNTTdpnstfRCVQMLEWFEHHGHI 237
Cdd:cd08529   2 FEILNKLGKGSFGVVYKVV-RKVDGRVYALKqidISRMSRKMREEAIDEARVLSKLNSP------YVIKYYDSFVDKGKL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 238 CIVFELL-GLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDyteaynpkikrdertl 316
Cdd:cd08529  75 NIVMEYAeNGDLHSLIKSQRGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGD---------------- 138
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 67551261 317 inpDIKVVDFGSATYDDEHH---STLVSTRHYRAPEVILALGWSQPCDVWSIGCILIE 371
Cdd:cd08529 139 ---NVKIGDLGVAKILSDTTnfaQTIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYE 193
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
161-476 9.85e-17

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: 79.76  E-value: 9.85e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGkVVECIDHKAGGRHVAVKIVKNVdRYCEAARSEI-------QVLEHlnttdPNstfrCVQMLEWFEH 233
Cdd:cd14074   5 YDLEETLGRGHFA-VVKLARHVFTGEKVAVKVIDKT-KLDDVSKAHLfqevrcmKLVQH-----PN----VVRLYEVIDT 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 234 HGHICIVFEL-LGLSTYDFI--KENGFLPfrlDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYTeaynpkik 310
Cdd:cd14074  74 QTKLYLILELgDGGDMYDYImkHENGLNE---DLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKQGL-------- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 311 rdertlinpdIKVVDFG-SATYD-DEHHSTLVSTRHYRAPEVILALGWSQPC-DVWSIGCILIEYYLGFTVFPTHDSKEH 387
Cdd:cd14074 143 ----------VKLTDFGfSNKFQpGEKLETSCGSLAYSAPEILLGDEYDAPAvDIWSLGVILYMLVCGQPPFQEANDSET 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 388 LAMMERILGPLPKHmiqktrkrkyfhhdrldwdehssagryVSRRCKplkefmlsqdveherlfDLIQKMLEYDPAKRIT 467
Cdd:cd14074 213 LTMIMDCKYTVPAH---------------------------VSPECK-----------------DLIRRMLIRDPKKRAS 248

                ....*....
gi 67551261 468 LREALKHPF 476
Cdd:cd14074 249 LEEIENHPW 257
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
160-371 1.36e-16

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: 79.36  E-value: 1.36e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVEcIDHKAGGRHVAVKIVK---NVDRYCEAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHGH 236
Cdd:cd08530   1 DFKVLKKLGKGSYGSVYK-VKRLSDNQVYALKEVNlgsLSQKEREDSVNEIRLLASVN--HPN----IIRYKEAFLDGNR 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFEL--LG-LSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDyteaynpkikrde 313
Cdd:cd08530  74 LCIVMEYapFGdLSKLISKRKKKRRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGD------------- 140
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 67551261 314 rtlinpDIKVVDFGSATYDDEHHS-TLVSTRHYRAPEVILALGWSQPCDVWSIGCILIE 371
Cdd:cd08530 141 ------LVKIGDLGISKVLKKNLAkTQIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYE 193
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
167-476 1.39e-16

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: 80.16  E-value: 1.39e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIdHKAGGRHVAVKIVkNVDRYCEAARseiQVLEHLNTTDPNSTFRCVQMLEWF--EHHGHICIVFELL 244
Cdd:cd06621   9 LGEGAGGSVTKCR-LRNTKTIFALKTI-TTDPNPDVQK---QILRELEINKSCASPYIVKYYGAFldEQDSSIGIAMEYC 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 245 GLSTYDFI-----KENGFLPFRLdhIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQsdyteaynpkikrdertliNP 319
Cdd:cd06621  84 EGGSLDSIykkvkKKGGRIGEKV--LGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTR-------------------KG 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 320 DIKVVDFG-SATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSK-----EHLAMMER 393
Cdd:cd06621 143 QVKLCDFGvSGELVNSLAGTFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFPPEGEPplgpiELLSYIVN 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 394 ILGPLPKhmiqktrkrkyfhhdrldwDEhSSAGRYVSRrckPLKEFmlsqdveherlfdlIQKMLEYDPAKRITLREALK 473
Cdd:cd06621 223 MPNPELK-------------------DE-PENGIKWSE---SFKDF--------------IEKCLEKDGTRRPGPWQMLA 265

                ...
gi 67551261 474 HPF 476
Cdd:cd06621 266 HPW 268
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
160-476 1.44e-16

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: 79.65  E-value: 1.44e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDHKAGgRHVAVKIVKNVDRYCEAARSEIQVLEHLnTTDPN-STF---------RCVQMLE 229
Cdd:cd06608   7 IFELVEVIGEGTYGKVYKARHKKTG-QLAAIKIMDIIEDEEEEIKLEINILRKF-SNHPNiATFygafikkdpPGGDDQL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 230 WFehhghiciVFELL-GLSTYDFIKENGFLPFRL--DHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyTEayn 306
Cdd:cd06608  85 WL--------VMEYCgGGSVTDLVKGLRKKGKRLkeEWIAYILRETLRGLAYLHENKVIHRDIKGQNILL-----TE--- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 307 pkikrdertliNPDIKVVDFG-SATYDDEHH--STLVSTRHYRAPEVI-----LALGWSQPCDVWSIGCILIEyyLGFTV 378
Cdd:cd06608 149 -----------EAEVKLVDFGvSAQLDSTLGrrNTFIGTPYWMAPEVIacdqqPDASYDARCDVWSLGITAIE--LADGK 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 379 FPTHDSKEHLAMMERILGPLPKhMIQKTRKRKYFHhdrldwdehssagryvsrrckplkefmlsqdveherlfDLIQKML 458
Cdd:cd06608 216 PPLCDMHPMRALFKIPRNPPPT-LKSPEKWSKEFN--------------------------------------DFISECL 256
                       330
                ....*....|....*...
gi 67551261 459 EYDPAKRITLREALKHPF 476
Cdd:cd06608 257 IKNYEQRPFTEELLEHPF 274
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
161-369 1.59e-16

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: 79.38  E-value: 1.59e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIV--DTLGEGAFGKVVECIdHKAGGRHVAVKIVKNV---DRYCEAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHG 235
Cdd:cd14082   3 YQIFpdEVLGSGQFGIVYGGK-HRKTGRDVAIKVIDKLrfpTKQESQLRNEVAILQQLS--HPG----VVNLECMFETPE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 236 HICIVFELLGLSTYDFI--KENGFLPFRLdhIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDyteAYnpkikrde 313
Cdd:cd14082  76 RVFVVMEKLHGDMLEMIlsSEKGRLPERI--TKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAE---PF-------- 142
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 67551261 314 rtlinPDIKVVDFGSATYDDEH--HSTLVSTRHYRAPEVILALGWSQPCDVWSIGCIL 369
Cdd:cd14082 143 -----PQVKLCDFGFARIIGEKsfRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVII 195
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
161-476 2.27e-16

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: 79.38  E-value: 2.27e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIV-DTLGEGAFGKVVECIDhKAGGRHVAVKIVknvDRYCEAARS----EIQVLeHLNTTDPNstfrCVQMLEWFEHHG 235
Cdd:cd14090   3 YKLTgELLGEGAYASVQTCIN-LYTGKEYAVKII---EKHPGHSRSrvfrEVETL-HQCQGHPN----ILQLIEYFEDDE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 236 HICIVFELL-GLSTYDFIKENGFlpFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrder 314
Cdd:cd14090  74 RFYLVFEKMrGGPLLSHIEKRVH--FTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDK------------- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 315 tlINPdIKVVDF--GSATYDDEHHSTLVST---------RHYRAPEVI-----LALGWSQPCDVWSIGCILIEYYLGFTV 378
Cdd:cd14090 139 --VSP-VKICDFdlGSGIKLSSTSMTPVTTpelltpvgsAEYMAPEVVdafvgEALSYDKRCDLWSLGVILYIMLCGYPP 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 379 FPTH-------DSKEHLAMMERILgplpKHMIQKTrkrKYFHHDRlDWDEHSSAGRyvsrrckplkefmlsqdveherlf 451
Cdd:cd14090 216 FYGRcgedcgwDRGEACQDCQELL----FHSIQEG---EYEFPEK-EWSHISAEAK------------------------ 263
                       330       340
                ....*....|....*....|....*
gi 67551261 452 DLIQKMLEYDPAKRITLREALKHPF 476
Cdd:cd14090 264 DLISHLLVRDASQRYTAEQVLQHPW 288
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
157-476 4.39e-16

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: 78.11  E-value: 4.39e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 157 LSARYEIVDTLGEGAFGKVVECIDHKAGgRHVAVKIVKNVDryCEAA----RSEIQVLEHLNttDPNstfrCVQMLEWFE 232
Cdd:cd14183   4 ISERYKVGRTIGDGNFAVVKECVERSTG-REYALKIINKSK--CRGKehmiQNEVSILRRVK--HPN----IVLLIEEMD 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 233 HHGHICIVFELL-GLSTYDFIKENGFLPFRldHIRKMAYQICKSVNFLHSNKLTHTDLKPENIL-FVQSDYTEAynpkik 310
Cdd:cd14183  75 MPTELYLVMELVkGGDLFDAITSTNKYTER--DASGMLYNLASAIKYLHSLNIVHRDIKPENLLvYEHQDGSKS------ 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 311 rdertlinpdIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAM 390
Cdd:cd14183 147 ----------LKLGDFGLATVVDGPLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGSGDDQEVLF 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 391 MERILG----PLPKhmiqktrkrkyfhhdrldWDEHSSAGRyvsrrckplkefmlsqdveherlfDLIQKMLEYDPAKRI 466
Cdd:cd14183 217 DQILMGqvdfPSPY------------------WDNVSDSAK------------------------ELITMMLQVDVDQRY 254
                       330
                ....*....|
gi 67551261 467 TLREALKHPF 476
Cdd:cd14183 255 SALQVLEHPW 264
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
167-477 5.81e-16

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: 77.78  E-value: 5.81e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIdHKAGGRHVAVKIVKNvDRYCEAARSEIQ----VLEHLNTTDpnstfRCVQMLEWFEHHGHICIVFE 242
Cdd:cd14106  16 LGRGKFAVVRKCI-HKETGKEYAAKFLRK-RRRGQDCRNEILheiaVLELCKDCP-----RVVNLHEVYETRSELILILE 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 243 L-LGLSTYDFIKENGFLPFRlDHIRKMAyQICKSVNFLHSNKLTHTDLKPENILFVQSDyteaynpkikrdertlINPDI 321
Cdd:cd14106  89 LaAGGELQTLLDEEECLTEA-DVRRLMR-QILEGVQYLHERNIVHLDLKPQNILLTSEF----------------PLGDI 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 322 KVVDFGSATY--DDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMMERIlgplp 399
Cdd:cd14106 151 KLCDFGISRVigEGEEIREILGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQC----- 225
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 67551261 400 khmiqktrkrkyfhhdRLDWDEHssagryvsrrckplkefmLSQDVEhERLFDLIQKMLEYDPAKRITLREALKHPFF 477
Cdd:cd14106 226 ----------------NLDFPEE------------------LFKDVS-PLAIDFIKRLLVKDPEKRLTAKECLEHPWL 268
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
161-369 8.15e-16

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: 77.21  E-value: 8.15e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIDHKAGGRhVAVKIVKNVDRYCEAARS----EIQVLEHLNttDPNstfrCVQMLEWFE-HHG 235
Cdd:cd14164   2 YTLGTTIGEGSFSKVKLATSQKYCCK-VAIKIVDRRRASPDFVQKflprELSILRRVN--HPN----IVQMFECIEvANG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 236 HICIVFELLGLSTYDFIKENGFLPfrLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqsdyteaynpkIKRDERt 315
Cdd:cd14164  75 RLYIVMEAAATDLLQKIQEVHHIP--KDLARDMFAQMVGAVNYLHDMNIVHRDLKCENIL-------------LSADDR- 138
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 67551261 316 linpDIKVVDFGSA----TYDDEHHsTLVSTRHYRAPEVILALGW-SQPCDVWSIGCIL 369
Cdd:cd14164 139 ----KIKIADFGFArfveDYPELST-TFCGSRAYTPPEVILGTPYdPKKYDVWSLGVVL 192
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
161-399 9.16e-16

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are three PIM2 isoforms resulting from alternative translation initiation sites. PIM2 is highly expressed in leukemia and lymphomas and has been shown to promote the survival and proliferation of tumor cells. The PIM2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 77.20  E-value: 9.16e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVEciDHK-AGGRHVAVKIVKNvDRYCEAAR--------SEIQVLEHLNTTDPNSTFrcVQMLEWF 231
Cdd:cd14101   2 YTMGNLLGKGGFGTVYA--GHRiSDGLQVAIKQISR-NRVQQWSKlpgvnpvpNEVALLQSVGGGPGHRGV--IRLLDWF 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 232 EHHGHICIVFE--LLGLSTYDFIKENGFLPFRLDhiRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteaynpki 309
Cdd:cd14101  77 EIPEGFLLVLErpQHCQDLFDYITERGALDESLA--RRFFKQVVEAVQHCHSKGVVHRDIKDENILV------------- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 310 krDERTlinPDIKVVDFGS-ATYDDEHHSTLVSTRHYRAPEVILALGW-SQPCDVWSIGCILIEYYLG------------ 375
Cdd:cd14101 142 --DLRT---GDIKLIDFGSgATLKDSMYTDFDGTRVYSPPEWILYHQYhALPATVWSLGILLYDMVCGdipferdtdilk 216
                       250       260
                ....*....|....*....|....*
gi 67551261 376 -FTVFPTHDSKEHLAMMERILGPLP 399
Cdd:cd14101 217 aKPSFNKRVSNDCRSLIRSCLAYNP 241
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
161-476 9.24e-16

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: 77.35  E-value: 9.24e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECiDHKAGGRHVAVKIVKN---------VDRycEAARSEIQVLEHLNttDPNstfrCVQMLEWF 231
Cdd:cd14195   7 YEMGEELGSGQFAIVRKC-REKGTGKEYAAKFIKKrrlsssrrgVSR--EEIEREVNILREIQ--HPN----IITLHDIF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 232 EHHGHICIVFELL-GLSTYDFIKENGFLPfrLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVqsdyteaynpkik 310
Cdd:cd14195  78 ENKTDVVLILELVsGGELFDFLAEKESLT--EEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLL------------- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 311 rdERTLINPDIKVVDFGSATYDD--EHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHL 388
Cdd:cd14195 143 --DKNVPNPRIKLIDFGIAHKIEagNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETL 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 389 AMMERIlgplpkhmiqktrkrkyfhhdRLDWDEhssagRYVSRRCKPLKEFmlsqdveherlfdlIQKMLEYDPAKRITL 468
Cdd:cd14195 221 TNISAV---------------------NYDFDE-----EYFSNTSELAKDF--------------IRRLLVKDPKKRMTI 260

                ....*...
gi 67551261 469 REALKHPF 476
Cdd:cd14195 261 AQSLEHSW 268
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
167-421 1.06e-15

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: 76.64  E-value: 1.06e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVEcidhkagGRH-------VAVKIV--KNVDRYCEAARSEIQVLEHLNTTDpnstfrCVQMLEWFEHHGHI 237
Cdd:cd14120   1 IGHGAFAVVFK-------GRHrkkpdlpVAIKCItkKNLSKSQNLLGKEIKILKELSHEN------VVALLDCQETSSSV 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 238 CIVFELL-GLSTYDFIKENGFLPfrLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYTEAYNPKIKrdertl 316
Cdd:cd14120  68 YLVMEYCnGGDLADYLQAKGTLS--EDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSGRKPSPNDIR------ 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 317 inpdIKVVDFGSATY--DDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKE--HLAMME 392
Cdd:cd14120 140 ----LKIADFGFARFlqDGMMAATLCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQAQTPQElkAFYEKN 215
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 67551261 393 RILGP-LP-------KHMIQKTRKRKyfHHDRLDWDE 421
Cdd:cd14120 216 ANLRPnIPsgtspalKDLLLGLLKRN--PKDRIDFED 250
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
165-388 1.14e-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: 76.88  E-value: 1.14e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 165 DTLGEGAFGKVVECIDHKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHGHICIVFELL 244
Cdd:cd14190  10 EVLGGGKFGKVHTCTEKRTGLKLAAKVINKQNSKDKEMVLLEIQVMNQLN--HRN----LIQLYEAIETPNEIVLFMEYV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 245 -GLSTYDFIKENGFlpfRLDHIRKMAY--QICKSVNFLHSNKLTHTDLKPENILFVQSDyteaynpkikrdertliNPDI 321
Cdd:cd14190  84 eGGELFERIVDEDY---HLTEVDAMVFvrQICEGIQFMHQMRVLHLDLKPENILCVNRT-----------------GHQV 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 67551261 322 KVVDFGSATYDDEHHSTLVS--TRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHL 388
Cdd:cd14190 144 KIIDFGLARRYNPREKLKVNfgTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETL 212
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
160-384 1.44e-15

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: 76.78  E-value: 1.44e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDHKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLnTTDPNSTFRCVQMLEWFEHHGHIC- 238
Cdd:cd14036   1 KLRIKRVIAEGGFAFVYEAQDVGTGKEYALKRLLSNEEEKNKAIIQEINFMKKL-SGHPNIVQFCSAASIGKEESDQGQa 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 239 ---IVFELLGLSTYDFIKE-NGFLPFRLDHIRKMAYQICKSVNFLHSNK--LTHTDLKPENILfVQSDYTeaynpkikrd 312
Cdd:cd14036  80 eylLLTELCKGQLVDFVKKvEAPGPFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLL-IGNQGQ---------- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 313 ertlinpdIKVVDFGSAT----YDD-----------EHHSTLVSTRHYRAPEVI-----LALGWSQpcDVWSIGCILieY 372
Cdd:cd14036 149 --------IKLCDFGSATteahYPDyswsaqkrslvEDEITRNTTPMYRTPEMIdlysnYPIGEKQ--DIWALGCIL--Y 216
                       250
                ....*....|..
gi 67551261 373 YLGFTVFPTHDS 384
Cdd:cd14036 217 LLCFRKHPFEDG 228
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
167-407 1.57e-15

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: 76.62  E-value: 1.57e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIDHKAGgRHVAVKIVK------NVDRYCEAARSEIQVLEHLNTTDPNSTFRCVQMlewfEHHGHICIV 240
Cdd:cd06652  10 LGQGAFGRVYLCYDADTG-RELAVKQVQfdpespETSKEVNALECEIQLLKNLLHERIVQYYGCLRD----PQERTLSIF 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 241 FELL-GLSTYDFIKENGFLPFRLdhIRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqsdyteaynpkikRDErtliNP 319
Cdd:cd06652  85 MEYMpGGSIKDQLKSYGALTENV--TRKYTRQILEGVHYLHSNMIVHRDIKGANIL---------------RDS----VG 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 320 DIKVVDFGSAT------YDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYylgFTVFPTHDSKEHLAMMER 393
Cdd:cd06652 144 NVKLGDFGASKrlqticLSGTGMKSVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEM---LTEKPPWAEFEAMAAIFK 220
                       250
                ....*....|....*....
gi 67551261 394 I----LGP-LPKHMIQKTR 407
Cdd:cd06652 221 IatqpTNPqLPAHVSDHCR 239
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
161-420 1.63e-15

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: 76.59  E-value: 1.63e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIDHKAGGRHVAVKIV--KNVDRYCEAARSEIQVLEHLNTTDpnstfrCVQMLEWFEHHGHIC 238
Cdd:cd14201   8 YSRKDLVGHGAFAVVFKGRHRKKTDWEVAIKSInkKNLSKSQILLGKEIKILKELQHEN------IVALYDVQEMPNSVF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 239 IVFELL-GLSTYDFIKENGFLpfRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDyteaynpkikRDERTLI 317
Cdd:cd14201  82 LVMEYCnGGDLADYLQAKGTL--SEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYAS----------RKKSSVS 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 318 NPDIKVVDFGSATY--DDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMMER-- 393
Cdd:cd14201 150 GIRIKIADFGFARYlqSNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQDLRMFYEKnk 229
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 67551261 394 -ILGPLPKH-----------MIQKTRKrkyfhhDRLDWD 420
Cdd:cd14201 230 nLQPSIPREtspyladlllgLLQRNQK------DRMDFE 262
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
161-477 1.64e-15

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: 76.36  E-value: 1.64e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIDHKAGgRHVAVKIV---KNVDRYCEA-ARSEIQVLEHLNTTDpnstfrCVQMLEWFE-HHG 235
Cdd:cd14165   3 YILGINLGEGSYAKVKSAYSERLK-CNVAIKIIdkkKAPDDFVEKfLPRELEILARLNHKS------IIKTYEIFEtSDG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 236 HICIVFEL-LGLSTYDFIKENGFLPfrLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQsdyteaynpkikrder 314
Cdd:cd14165  76 KVYIVMELgVQGDLLEFIKLRGALP--EDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDK---------------- 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 315 tliNPDIKVVDFGSA---TYDDEHHSTLVST----RHYRAPEVILALGWsQP--CDVWSIGCILieYYLGFTVFPTHDSK 385
Cdd:cd14165 138 ---DFNIKLTDFGFSkrcLRDENGRIVLSKTfcgsAAYAAPEVLQGIPY-DPriYDIWSLGVIL--YIMVCGSMPYDDSN 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 386 ehlammerilgplpkhmIQKTRKRKYFHHDRldwdehssagryvsrrckplkeFMLSQDVEHErLFDLIQKMLEYDPAKR 465
Cdd:cd14165 212 -----------------VKKMLKIQKEHRVR----------------------FPRSKNLTSE-CKDLIYRLLQPDVSQR 251
                       330
                ....*....|..
gi 67551261 466 ITLREALKHPFF 477
Cdd:cd14165 252 LCIDEVLSHPWL 263
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
161-379 1.91e-15

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 77.17  E-value: 1.91e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  161 YEIVDTLGEGAFGKVVECiDHKAGGRHVAVKIVKNVD----RYCEAARSEIQVLEHLNttdpnSTFrCVQMLEWFEHHGH 236
Cdd:PTZ00263  20 FEMGETLGTGSFGRVRIA-KHKGTGEYYAIKCLKKREilkmKQVQHVAQEKSILMELS-----HPF-IVNMMCSFQDENR 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  237 ICIVFE-LLGLSTYDFIKENGFLPFrlDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDyteaynpkikrdert 315
Cdd:PTZ00263  93 VYFLLEfVVGGELFTHLRKAGRFPN--DVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKG--------------- 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 67551261  316 linpDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVF 379
Cdd:PTZ00263 156 ----HVKVTDFGFAKKVPDRTFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPF 215
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
161-477 2.00e-15

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: 76.18  E-value: 2.00e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIDHKAgGRHVAVKIVKN-------VDRYCEaarSEIQVLEHLnttDPNSTFRCVQMLEwfEH 233
Cdd:cd14163   2 YQLGKTIGEGTYSKVKEAFSKKH-QRKVAIKIIDKsggpeefIQRFLP---RELQIVERL---DHKNIIHVYEMLE--SA 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 234 HGHICIVFELL-GLSTYDFIKENGFLPfrLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqsdyteaynpkikrd 312
Cdd:cd14163  73 DGKIYLVMELAeDGDVFDCVLHGGPLP--EHRAKALFRQLVEAIRYCHGCGVAHRDLKCENAL----------------- 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 313 ertLINPDIKVVDFGSATYDDEHHSTLVST----RHYRAPEVILALGW-SQPCDVWSIGCILieYYLGFTVFPTHDSKeh 387
Cdd:cd14163 134 ---LQGFTLKLTDFGFAKQLPKGGRELSQTfcgsTAYAAPEVLQGVPHdSRKGDIWSMGVVL--YVMLCAQLPFDDTD-- 206
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 388 lammerilgpLPKHMIQKTRKRKYFHHdrldwdehssagRYVSRRCKplkefmlsqdveherlfDLIQKMLEYDPAKRIT 467
Cdd:cd14163 207 ----------IPKMLCQQQKGVSLPGH------------LGVSRTCQ-----------------DLLKRLLEPDMVLRPS 247
                       330
                ....*....|
gi 67551261 468 LREALKHPFF 477
Cdd:cd14163 248 IEEVSWHPWL 257
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
161-402 2.19e-15

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: 76.00  E-value: 2.19e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIDHKAGGRHVAVKIV-----------KNVDRYCEAARSEI----QVLEHlnttdPNstfrCV 225
Cdd:cd08528   2 YAVLELLGSGAFGCVYKVRKKSNGQTLLALKEInmtnpafgrteQERDKSVGDIISEVniikEQLRH-----PN----IV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 226 QMLEWFEHHGHICIVFELL-GLSTYDFI---KENGfLPFRLDHIRKMAYQICKSVNFLHSNK-LTHTDLKPENILFVQSD 300
Cdd:cd08528  73 RYYKTFLENDRLYIVMELIeGAPLGEHFsslKEKN-EHFTEDRIWNIFVQMVLALRYLHKEKqIVHRDLKPNNIMLGEDD 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 301 yteaynpkikrdertlinpDIKVVDFGSATYDDEHHSTLVS---TRHYRAPEVILALGWSQPCDVWSIGCILieyYLGFT 377
Cdd:cd08528 152 -------------------KVTITDFGLAKQKGPESSKMTSvvgTILYSCPEIVQNEPYGEKADIWALGCIL---YQMCT 209
                       250       260
                ....*....|....*....|....*....
gi 67551261 378 VFPTHDSKEHLAMMERILG----PLPKHM 402
Cdd:cd08528 210 LQPPFYSTNMLTLATKIVEaeyePLPEGM 238
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
167-369 2.35e-15

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: 76.83  E-value: 2.35e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIdHKAGGRHVAVKIVKNvdRYCEAARSEIQVLEhLNTTDPNstfrCVQMLEWFEHHGHICIVFELLgl 246
Cdd:cd14180  14 LGEGSFSVCRKCR-HRQSGQEYAVKIISR--RMEANTQREVAALR-LCQSHPN----IVALHEVLHDQYHTYLVMELL-- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 247 stydfikENGFLpfrLDHIRKM-------AYQICKS----VNFLHSNKLTHTDLKPENILFvqSDYTEaynpkikrdert 315
Cdd:cd14180  84 -------RGGEL---LDRIKKKarfseseASQLMRSlvsaVSFMHEAGVVHRDLKPENILY--ADESD------------ 139
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 67551261 316 liNPDIKVVDFGSATY---DDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCIL 369
Cdd:cd14180 140 --GAVLKVIDFGFARLrpqGSRPLQTPCFTLQYAAPELFSNQGYDESCDLWSLGVIL 194
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
161-476 2.86e-15

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: 76.22  E-value: 2.86e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIDHKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTdpnstfRCVQMLEWFEHHGHICIV 240
Cdd:cd06644  14 WEIIGELGDGAFGKVYKAKNKETGALAAAKVIETKSEEELEDYMVEIEILATCNHP------YIVKLLGAFYWDGKLWIM 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 241 FELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQsdyteaynpkikrdertliNPD 320
Cdd:cd06644  88 IEFCPGGAVDAIMLELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTL-------------------DGD 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 321 IKVVDFGSATYDD---EHHSTLVSTRHYRAPEVILA-----LGWSQPCDVWSIGCILIEYYlgfTVFPTHDSKEHLAMME 392
Cdd:cd06644 149 IKLADFGVSAKNVktlQRRDSFIGTPYWMAPEVVMCetmkdTPYDYKADIWSLGITLIEMA---QIEPPHHELNPMRVLL 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 393 RILGPLPKHMIQKTRKRKYFHhdrldwdehssagryvsrrckplkefmlsqdveherlfDLIQKMLEYDPAKRITLREAL 472
Cdd:cd06644 226 KIAKSEPPTLSQPSKWSMEFR--------------------------------------DFLKTALDKHPETRPSAAQLL 267

                ....
gi 67551261 473 KHPF 476
Cdd:cd06644 268 EHPF 271
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
167-476 3.53e-15

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: 75.96  E-value: 3.53e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIdHKAGGRHVAVKIVknVDRycEAARSEIQvLEHLNTTDPNstfrCVQMLEWF----------EHHGH 236
Cdd:cd14171  14 LGTGISGPVRVCV-KKSTGERFALKIL--LDR--PKARTEVR-LHMMCSGHPN----IVQIYDVYansvqfpgesSPRAR 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELL-GLSTYDFI-KENGFLPfrlDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteaynpKIKRDER 314
Cdd:cd14171  84 LLIVMELMeGGELFDRIsQHRHFTE---KQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLL-----------KDNSEDA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 315 TlinpdIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILA-----------------LGWSQPCDVWSIGCILIEYYLGFT 377
Cdd:cd14171 150 P-----IKLCDFGFAKVDQGDLMTPQFTPYYVAPQVLEAqrrhrkersgiptsptpYTYDKSCDMWSLGVIIYIMLCGYP 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 378 VF-PTHDSKEhlammerilgpLPKHMIQKTRKRKYFHHDRlDWdehssagRYVSRRCKplkefmlsqdveherlfDLIQK 456
Cdd:cd14171 225 PFySEHPSRT-----------ITKDMKRKIMTGSYEFPEE-EW-------SQISEMAK-----------------DIVRK 268
                       330       340
                ....*....|....*....|
gi 67551261 457 MLEYDPAKRITLREALKHPF 476
Cdd:cd14171 269 LLCVDPEERMTIEEVLHHPW 288
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
161-484 3.66e-15

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: 76.18  E-value: 3.66e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVEcidhkagGRHvavKIVKNVdryceAARSEIQvLEHlNTTDPNSTFRCVQMLEWFEHHG----- 235
Cdd:cd07872   8 YIKLEKLGEGTYATVFK-------GRS---KLTENL-----VALKEIR-LEH-EEGAPCTAIREVSLLKDLKHANivtlh 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 236 -------HICIVFELLGLSTYDFIKENGFLpFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteaynpk 308
Cdd:cd07872  71 divhtdkSLTLVFEYLDKDLKQYMDDCGNI-MSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLI------------ 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 309 ikrDERTlinpDIKVVDFGSA---TYDDEHHSTLVSTRHYRAPEVILALG-WSQPCDVWSIGCILIEYYLGFTVFPTHDS 384
Cdd:cd07872 138 ---NERG----ELKLADFGLArakSVPTKTYSNEVVTLWYRPPDVLLGSSeYSTQIDMWGVGCIFFEMASGRPLFPGSTV 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 385 KEHLAMMERILGPLPKHmiqktrkrkyfhhdrlDWDEHSSAGRYVS-----RRCKPLKEFMLSQDVEHerlFDLIQKMLE 459
Cdd:cd07872 211 EDELHLIFRLLGTPTEE----------------TWPGISSNDEFKNynfpkYKPQPLINHAPRLDTEG---IELLTKFLQ 271
                       330       340
                ....*....|....*....|....*
gi 67551261 460 YDPAKRITLREALKHPFFDLLKKSI 484
Cdd:cd07872 272 YESKKRISAEEAMKHAYFRSLGTRI 296
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
160-476 3.80e-15

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: 75.45  E-value: 3.80e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDhKAGGRHVAVKIVKNvDRYC---EAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHGH 236
Cdd:cd14184   2 KYKIGKVIGDGNFAVVKECVE-RSTGKEFALKIIDK-AKCCgkeHLIENEVSILRRVK--HPN----IIMLIEEMDTPAE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELL-GLSTYDFIKENgfLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQsdyteaYNPKIKrdert 315
Cdd:cd14184  74 LYLVMELVkGGDLFDAITSS--TKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVCE------YPDGTK----- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 316 linpDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMMERIL 395
Cdd:cd14184 141 ----SLKLGDFGLATVVEGPLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSENNLQEDLFDQILL 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 396 G----PLPKhmiqktrkrkyfhhdrldWDEHSSAGRyvsrrckplkefmlsqdveherlfDLIQKMLEYDPAKRITLREA 471
Cdd:cd14184 217 GklefPSPY------------------WDNITDSAK------------------------ELISHMLQVNVEARYTAEQI 254

                ....*
gi 67551261 472 LKHPF 476
Cdd:cd14184 255 LSHPW 259
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
165-371 4.49e-15

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: 74.88  E-value: 4.49e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 165 DTLGEGAFGKVV--ECIDHKAGGRHVAVKIVKN----VDRycEAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHGHIC 238
Cdd:cd00192   1 KKLGEGAFGEVYkgKLKGGDGKTVDVAVKTLKEdaseSER--KDFLKEARVMKKLG--HPN----VVRLLGVCTEEEPLY 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 239 IVFELLG---LSTY-----DFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfVQSDYTeaynpkik 310
Cdd:cd00192  73 LVMEYMEggdLLDFlrksrPVFPSPEPSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCL-VGEDLV-------- 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 67551261 311 rdertlinpdIKVVDFGSA--TYDDEHHSTLVSTR-HYR--APEVILALGWSQPCDVWSIGCILIE 371
Cdd:cd00192 144 ----------VKISDFGLSrdIYDDDYYRKKTGGKlPIRwmAPESLKDGIFTSKSDVWSFGVLLWE 199
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
168-371 4.78e-15

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: 74.61  E-value: 4.78e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 168 GEGAFGKVVECIdHKAGGRHVAVKIVKNVDRYCEAarseIQVLEHLNTtdpnstfrcVQMLEWFEHHGHICIVFELLGL- 246
Cdd:cd14060   2 GGGSFGSVYRAI-WVSQDKEVAVKKLLKIEKEAEI----LSVLSHRNI---------IQFYGAILEAPNYGIVTEYASYg 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 247 STYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSN---KLTHTDLKPENILfVQSDYTeaynpkikrdertlinpdIKV 323
Cdd:cd14060  68 SLFDYLNSNESEEMDMDQIMTWATDIAKGMHYLHMEapvKVIHRDLKSRNVV-IAADGV------------------LKI 128
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 67551261 324 VDFGSATYDDEH-HSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIE 371
Cdd:cd14060 129 CDFGASRFHSHTtHMSLVGTFPWMAPEVIQSLPVSETCDTYSYGVVLWE 177
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
167-477 5.75e-15

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: 75.75  E-value: 5.75e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVeCIDHKAGGRHVAVKIVKN----VDRYCEAARSEIQVLEhLNTTDPNSTfrcvQMLEWFEHHGHICIVFE 242
Cdd:cd05620   3 LGKGSFGKVL-LAELKGKGEYFAVKALKKdvvlIDDDVECTMVEKRVLA-LAWENPFLT----HLYCTFQTKEHLFFVME 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 243 LLGLSTYDF-IKENGflpfRLDHIRKMAY--QICKSVNFLHSNKLTHTDLKPENILfvqsdyteaynpkIKRDERtlinp 319
Cdd:cd05620  77 FLNGGDLMFhIQDKG----RFDLYRATFYaaEIVCGLQFLHSKGIIYRDLKLDNVM-------------LDRDGH----- 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 320 dIKVVDFG---SATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEhlaMMERIlg 396
Cdd:cd05620 135 -IKIADFGmckENVFGDNRASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDE---LFESI-- 208
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 397 plpkhmiqktrkrkyfhhdRLDWDEHSsagRYVSRRCKplkefmlsqdveherlfDLIQKMLEYDPAKRITLREALK-HP 475
Cdd:cd05620 209 -------------------RVDTPHYP---RWITKESK-----------------DILEKLFERDPTRRLGVVGNIRgHP 249

                ..
gi 67551261 476 FF 477
Cdd:cd05620 250 FF 251
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
161-477 6.04e-15

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: 74.70  E-value: 6.04e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKV--VECIDHKaggRHVAVKIVkNVDRY---CEAARSEIQVL---EHLNTTDPNSTFRCVQMLeWfe 232
Cdd:cd06610   3 YELIEVIGSGATAVVyaAYCLPKK---EKVAIKRI-DLEKCqtsMDELRKEIQAMsqcNHPNVVSYYTSFVVGDEL-W-- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 233 hhghicIVFELL-GLSTYDFIK---ENGFLPFRLdhIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQsdyteaynpk 308
Cdd:cd06610  76 ------LVMPLLsGGSLLDIMKssyPRGGLDEAI--IATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGE---------- 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 309 ikrdertliNPDIKVVDFG-SATY----DDEHHS--TLVSTRHYRAPEVILAL-GWSQPCDVWSIGCILIEYYLGFTvfP 380
Cdd:cd06610 138 ---------DGSVKIADFGvSASLatggDRTRKVrkTFVGTPCWMAPEVMEQVrGYDFKADIWSFGITAIELATGAA--P 206
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 381 THDSKEHLAMMERILGPLPKHMIQKTRKrKYfhhdrldwdehSSAGRyvsrrckplkefmlsqdveherlfDLIQKMLEY 460
Cdd:cd06610 207 YSKYPPMKVLMLTLQNDPPSLETGADYK-KY-----------SKSFR------------------------KMISLCLQK 250
                       330
                ....*....|....*..
gi 67551261 461 DPAKRITLREALKHPFF 477
Cdd:cd06610 251 DPSKRPTAEELLKHKFF 267
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
161-477 7.39e-15

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: 74.26  E-value: 7.39e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVvecidHKAGGRH----VAVKIVKNVDR-YCEAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHG 235
Cdd:cd06613   2 YELIQRIGSGTYGDV-----YKARNIAtgelAAVKVIKLEPGdDFEIIQQEISMLKECR--HPN----IVAYFGSYLRRD 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 236 HICIVFELL-GLSTYDFIKENGflPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyTEaynpkikrder 314
Cdd:cd06613  71 KLWIVMEYCgGGSLQDIYQVTG--PLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILL-----TE----------- 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 315 tliNPDIKVVDFGSATYDDEHHS---TLVSTRHYRAPEVILAL---GWSQPCDVWSIGCILIEYYLGF-TVFPTHDSKEh 387
Cdd:cd06613 133 ---DGDVKLADFGVSAQLTATIAkrkSFIGTPYWMAPEVAAVErkgGYDGKCDIWALGITAIELAELQpPMFDLHPMRA- 208
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 388 LAMMERILGPLPKhMIQKTRKRKYFHhdrldwdehssagryvsrrckplkefmlsqdveherlfDLIQKMLEYDPAKRIT 467
Cdd:cd06613 209 LFLIPKSNFDPPK-LKDKEKWSPDFH--------------------------------------DFIKKCLTKNPKKRPT 249
                       330
                ....*....|
gi 67551261 468 LREALKHPFF 477
Cdd:cd06613 250 ATKLLQHPFV 259
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
271-477 7.65e-15

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: 74.58  E-value: 7.65e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 271 QICKSVNFLHSNKLTHTDLKPENiLFVQSDYteaynpkikrdertlinpDIKVVDFGSAT---YDDEHHSTLVSTRHYRA 347
Cdd:cd14187 115 QIILGCQYLHRNRVIHRDLKLGN-LFLNDDM------------------EVKIGDFGLATkveYDGERKKTLCGTPNYIA 175
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 348 PEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMMERILGPLPKHMiqktrkrkyfhhdrldwdehssagr 427
Cdd:cd14187 176 PEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHI------------------------- 230
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 67551261 428 yvsrrcKPLKEfmlsqdveherlfDLIQKMLEYDPAKRITLREALKHPFF 477
Cdd:cd14187 231 ------NPVAA-------------SLIQKMLQTDPTARPTINELLNDEFF 261
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
167-371 8.38e-15

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: 74.29  E-value: 8.38e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIDHKAGgRHVAVKIV------KNVDRYCEAARSEIQVLEHLNTTDPNSTFRCVQMLEwfehHGHICIV 240
Cdd:cd06653  10 LGRGAFGEVYLCYDADTG-RELAVKQVpfdpdsQETSKEVNALECEIQLLKNLRHDRIVQYYGCLRDPE----EKKLSIF 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 241 FELL-GLSTYDFIKENGFLPFRLdhIRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqsdyteaynpkikRDERTlinp 319
Cdd:cd06653  85 VEYMpGGSVKDQLKAYGALTENV--TRRYTRQILQGVSYLHSNMIVHRDIKGANIL---------------RDSAG---- 143
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 67551261 320 DIKVVDFGSAT------YDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIE 371
Cdd:cd06653 144 NVKLGDFGASKriqticMSGTGIKSVTGTPYWMSPEVISGEGYGRKADVWSVACTVVE 201
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
161-476 9.18e-15

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: 74.13  E-value: 9.18e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKV--VECIDhkaGGRHVAVKIV--KNVDRYCEAARSEIQVLEHLNTTDPNstfrCVQMLEWFEHHGH 236
Cdd:cd14186   3 FKVLNLLGKGSFACVyrARSLH---TGLEVAIKMIdkKAMQKAGMVQRVRNEVEIHCQLKHPS----ILELYNYFEDSNY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQsdyteaynpkikrdertl 316
Cdd:cd14186  76 VYLVLEMCHNGEMSRYLKNRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTR------------------ 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 317 iNPDIKVVDFGSAT---YDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMMER 393
Cdd:cd14186 138 -NMNIKIADFGLATqlkMPHEKHFTMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVL 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 394 ILGPLPKHmiqktrkrkyfhhdrldwdehssagryVSRRCKplkefmlsqdveherlfDLIQKMLEYDPAKRITLREALK 473
Cdd:cd14186 217 ADYEMPAF---------------------------LSREAQ-----------------DLIHQLLRKNPADRLSLSSVLD 252

                ...
gi 67551261 474 HPF 476
Cdd:cd14186 253 HPF 255
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
158-371 1.04e-14

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: 74.64  E-value: 1.04e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 158 SARYEIVDTLGEGAFGKVVEcIDHKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLnTTDPNsTFRCVQMLEWFEHH--G 235
Cdd:cd06639  21 SDTWDIIETIGKGTYGKVYK-VTNKKDGSLAAVKILDPISDVDEEIEAEYNILRSL-PNHPN-VVKFYGMFYKADQYvgG 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 236 HICIVFELL-GLSTYDFIKenGFLPF--RLDH--IRKMAYQICKSVNFLHSNKLTHTDLKPENILFVqsdyTEAynpkik 310
Cdd:cd06639  98 QLWLVLELCnGGSVTELVK--GLLKCgqRLDEamISYILYGALLGLQHLHNNRIIHRDVKGNNILLT----TEG------ 165
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 67551261 311 rdertlinpDIKVVDFGSA---TYDDEHHSTLVSTRHYRAPEVILA-----LGWSQPCDVWSIGCILIE 371
Cdd:cd06639 166 ---------GVKLVDFGVSaqlTSARLRRNTSVGTPFWMAPEVIACeqqydYSYDARCDVWSLGITAIE 225
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
161-477 1.12e-14

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: 73.87  E-value: 1.12e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIDHKAGgRHVAVKIV---KNVDRYCEA--ARsEIQVLEHLNttDPNstfrCVQMLEWFEHHG 235
Cdd:cd14162   2 YIVGKTLGHGSYAVVKKAYSTKHK-CKVAIKIVskkKAPEDYLQKflPR-EIEVIKGLK--HPN----LICFYEAIETTS 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 236 HICIVFELL-GLSTYDFIKENGFLPFRLDhiRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteaynpkikrDEr 314
Cdd:cd14162  74 RVYIIMELAeNGDLLDYIRKNGALPEPQA--RRWFRQLVAGVEYCHSKGVVHRDLKCENLLL---------------DK- 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 315 tliNPDIKVVDFGSA-----TYDDEHH--STLVSTRHYRAPEVILALGWS-QPCDVWSIGCILieYYLGFTVFPTHDSKE 386
Cdd:cd14162 136 ---NNNLKITDFGFArgvmkTKDGKPKlsETYCGSYAYASPEILRGIPYDpFLSDIWSMGVVL--YTMVYGRLPFDDSNL 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 387 hlammerilgplpKHMIQKTRKRKYFhhdrldwdehsSAGRYVSRRCKplkefmlsqdveherlfDLIQKMLEYDPaKRI 466
Cdd:cd14162 211 -------------KVLLKQVQRRVVF-----------PKNPTVSEECK-----------------DLILRMLSPVK-KRI 248
                       330
                ....*....|.
gi 67551261 467 TLREALKHPFF 477
Cdd:cd14162 249 TIEEIKRDPWF 259
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
167-476 1.72e-14

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: 73.57  E-value: 1.72e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIDhKAGGRHVAVKIV--------KNVDR---YCEAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHG 235
Cdd:cd06629   9 IGKGTYGRVYLAMN-ATTGEMLAVKQVelpktssdRADSRqktVVDALKSEIDTLKDLD--HPN----IVQYLGFEETED 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 236 HICIVFELL-GLSTYDFIKENGflPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqSDYTEAYnpkikrder 314
Cdd:cd06629  82 YFSIFLEYVpGGSIGSCLRKYG--KFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNIL---VDLEGIC--------- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 315 tlinpdiKVVDFGSA-----TYDDEHHSTLVSTRHYRAPEVILAL--GWSQPCDVWSIGCILIEYYLGFTVFPThdsKEH 387
Cdd:cd06629 148 -------KISDFGISkksddIYGNNGATSMQGSVFWMAPEVIHSQgqGYSAKVDIWSLGCVVLEMLAGRRPWSD---DEA 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 388 LAMMERILGplpkhmiqktrkrkyfhhdrldwdehssagryvSRRCKPLKE-FMLSQDVEherlfDLIQKMLEYDPAKRI 466
Cdd:cd06629 218 IAAMFKLGN---------------------------------KRSAPPVPEdVNLSPEAL-----DFLNACFAIDPRDRP 259
                       330
                ....*....|
gi 67551261 467 TLREALKHPF 476
Cdd:cd06629 260 TAAELLSHPF 269
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
157-386 1.84e-14

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: 73.43  E-value: 1.84e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 157 LSARYEIV--DTLGEGAFGKVVECIDhKAGGRHVAVKIVKNvDRYCEAARSEI----QVLEhLNTTDPnstfRCVQMLEW 230
Cdd:cd14197   5 FQERYSLSpgRELGRGKFAVVRKCVE-KDSGKEFAAKFMRK-RRKGQDCRMEIiheiAVLE-LAQANP----WVINLHEV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 231 FEHHGHICIVFELL-GLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteaynpki 309
Cdd:cd14197  78 YETASEMILVLEYAaGGEIFNQCVADREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILL------------- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 310 krderTLINP--DIKVVDFGSATY--DDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSK 385
Cdd:cd14197 145 -----TSESPlgDIKIVDFGLSRIlkNSEELREIMGTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDKQ 219

                .
gi 67551261 386 E 386
Cdd:cd14197 220 E 220
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
160-296 1.92e-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: 73.26  E-value: 1.92e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDHKaGGRHVAVKIVKNvDRYCEAARSEIQVLEHLNTTdpnstfRCVQMLEWFEHHGHI-C 238
Cdd:cd14016   1 RYKLVKKIGSGSFGEVYLGIDLK-TGEEVAIKIEKK-DSKHPQLEYEAKVYKLLQGG------PGIPRLYWFGQEGDYnV 72
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 67551261 239 IVFELLGLSTYDFIKENGflpfrldhiRKM--------AYQICKSVNFLHSNKLTHTDLKPENILF 296
Cdd:cd14016  73 MVMDLLGPSLEDLFNKCG---------RKFslktvlmlADQMISRLEYLHSKGYIHRDIKPENFLM 129
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
167-371 2.08e-14

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: 72.85  E-value: 2.08e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVvecidHKA--GGRHVAVKIVKNvdrycEAARSEIQV-LEHLNTTD-PNstfrCVQMLEWFEHHGHICIVFE 242
Cdd:cd14058   1 VGRGSFGVV-----CKArwRNQIVAVKIIES-----ESEKKAFEVeVRQLSRVDhPN----IIKLYGACSNQKPVCLVME 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 243 LL-GLSTYDFIKENGFLP-FRLDHIRKMAYQICKSVNFLHSNK---LTHTDLKPENILFVQSdyteaynpkikrdertli 317
Cdd:cd14058  67 YAeGGSLYNVLHGKEPKPiYTAAHAMSWALQCAKGVAYLHSMKpkaLIHRDLKPPNLLLTNG------------------ 128
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 67551261 318 NPDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIE 371
Cdd:cd14058 129 GTVLKICDFGTACDISTHMTNNKGSAAWMAPEVFEGSKYSEKCDVFSWGIILWE 182
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
167-476 2.50e-14

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: 72.82  E-value: 2.50e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIDHKAGGrHVAVKIVKNVDRYCEAARS------EIQVLEHLNttDPNST-FRCVQMLEwfehhGHICI 239
Cdd:cd06632   8 LGSGSFGSVYEGFNGDTGD-FFAVKEVSLVDDDKKSRESvkqleqEIALLSKLR--HPNIVqYYGTEREE-----DNLYI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 240 VFELL-GLSTYDFIKENGflPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfVQSdyteaynpkikrdertliN 318
Cdd:cd06632  80 FLEYVpGGSIHKLLQRYG--AFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANIL-VDT------------------N 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 319 PDIKVVDFGSATYDDE--HHSTLVSTRHYRAPEVILA--LGWSQPCDVWSIGCILIEYYLGftvFPTHDSKEHLAMMERI 394
Cdd:cd06632 139 GVVKLADFGMAKHVEAfsFAKSFKGSPYWMAPEVIMQknSGYGLAVDIWSLGCTVLEMATG---KPPWSQYEGVAAIFKI 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 395 -----LGPLPKHmiqktrkrkyfhhdrldwdehssagryvsrrckplkefmLSQDVEherlfDLIQKMLEYDPAKRITLR 469
Cdd:cd06632 216 gnsgeLPPIPDH---------------------------------------LSPDAK-----DFIRLCLQRDPEDRPTAS 251

                ....*..
gi 67551261 470 EALKHPF 476
Cdd:cd06632 252 QLLEHPF 258
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
160-371 2.53e-14

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: 72.69  E-value: 2.53e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIdHKAGGRHVAVKIVKNVDRYCEAARS----EIQVLEHLNttDPNstfrCVQMLEWFEHHG 235
Cdd:cd08224   1 NYEIEKKIGKGQFSVVYRAR-CLLDGRLVALKKVQIFEMMDAKARQdclkEIDLLQQLN--HPN----IIKYLASFIENN 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 236 HICIVFELL---GLSTydFIKE--NGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENIlFVQSdyteaynpkik 310
Cdd:cd08224  74 ELNIVLELAdagDLSR--LIKHfkKQKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANV-FITA----------- 139
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 67551261 311 rdertliNPDIKVVDFGSATYDDEH----HStLVSTRHYRAPEVILALGWSQPCDVWSIGCILIE 371
Cdd:cd08224 140 -------NGVVKLGDLGLGRFFSSKttaaHS-LVGTPYYMSPERIREQGYDFKSDIWSLGCLLYE 196
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
161-368 2.56e-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: 73.09  E-value: 2.56e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECiDHKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTdpnstfRCVQMLEWFEHHGHICIV 240
Cdd:cd14113   9 YSEVAELGRGRFSVVKKC-DQRGTKRAVATKFVNKKLMKRDQVTHELGVLQSLQHP------QLVGLLDTFETPTSYILV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 241 FELLGLSTY-DFIKENGFLPfrLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSdyteaynpkikrdertLINP 319
Cdd:cd14113  82 LEMADQGRLlDYVVRWGNLT--EEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQS----------------LSKP 143
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 67551261 320 DIKVVDFGSA-----TYddeHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCI 368
Cdd:cd14113 144 TIKLADFGDAvqlntTY---YIHQLLGSPEFAAPEIILGNPVSLTSDLWSIGVL 194
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
160-476 2.63e-14

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: 73.12  E-value: 2.63e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDHKAGgRHVAVKI---------------VKNVDRYCEAARSeiqvLEHLnttdpnstfRC 224
Cdd:cd13990   1 RYLLLNLLGKGGFSEVYKAFDLVEQ-RYVACKIhqlnkdwseekkqnyIKHALREYEIHKS----LDHP---------RI 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 225 VQMLEWFEH-HGHICIVFELLGLSTYDF-IKENGFLPFRLdhIRKMAYQICKSVNFL--HSNKLTHTDLKPENILFVQSD 300
Cdd:cd13990  67 VKLYDVFEIdTDSFCTVLEYCDGNDLDFyLKQHKSIPERE--ARSIIMQVVSALKYLneIKPPIIHYDLKPGNILLHSGN 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 301 YTEaynpkikrdertlinpDIKVVDFG-SATYDDEHHST----LVS----TRHYRAPEvILALGWSQP-----CDVWSIG 366
Cdd:cd13990 145 VSG----------------EIKITDFGlSKIMDDESYNSdgmeLTSqgagTYWYLPPE-CFVVGKTPPkisskVDVWSVG 207
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 367 CILIEYYLGFTVFpTHDSKEHLAMMERIlgplpkhmIQKTRKrkyfhhdrldwdEHSSAGRYVSRRCKplkefmlsqdve 446
Cdd:cd13990 208 VIFYQMLYGRKPF-GHNQSQEAILEENT--------ILKATE------------VEFPSKPVVSSEAK------------ 254
                       330       340       350
                ....*....|....*....|....*....|
gi 67551261 447 herlfDLIQKMLEYDPAKRITLREALKHPF 476
Cdd:cd13990 255 -----DFIRRCLTYRKEDRPDVLQLANDPY 279
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
165-476 3.41e-14

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: 73.14  E-value: 3.41e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 165 DTLGEGAFGKVVECIDhKAGGRHVAVKIVKNVDRYceaARSEI-QVLEHLNTTDPNSTFrcVQMLEWFEHHGHICIVFE- 242
Cdd:cd14173   8 EVLGEGAYARVQTCIN-LITNKEYAVKIIEKRPGH---SRSRVfREVEMLYQCQGHRNV--LELIEFFEEEDKFYLVFEk 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 243 LLGLSTYDFIKENGFlpFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrdertlINPdIK 322
Cdd:cd14173  82 MRGGSILSHIHRRRH--FNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQ---------------VSP-VK 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 323 VVDF--GSATYDDEHHS--------TLVSTRHYRAPEVILALG-----WSQPCDVWSIGCILIEYYLGFTVFPTH----- 382
Cdd:cd14173 144 ICDFdlGSGIKLNSDCSpistpellTPCGSAEYMAPEVVEAFNeeasiYDKRCDLWSLGVILYIMLSGYPPFVGRcgsdc 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 383 --DSKEHLAMMERILgplpkhmIQKTRKRKYFHHDRlDWDEHSSAGRyvsrrckplkefmlsqdveherlfDLIQKMLEY 460
Cdd:cd14173 224 gwDRGEACPACQNML-------FESIQEGKYEFPEK-DWAHISCAAK------------------------DLISKLLVR 271
                       330
                ....*....|....*.
gi 67551261 461 DPAKRITLREALKHPF 476
Cdd:cd14173 272 DAKQRLSAAQVLQHPW 287
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
160-476 3.47e-14

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: 72.33  E-value: 3.47e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGkVVECIDHKAGGRHVAVKIVKNVDRYCEAARSEIqvLEHLNTTDPNstfrCVQMLEWFEHHGHICI 239
Cdd:cd14665   1 RYELVKDIGSGNFG-VARLMRDKQTKELVAVKYIERGEKIDENVQREI--INHRSLRHPN----IVRFKEVILTPTHLAI 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 240 VFELL-GLSTYDFIKENGflPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsDYTEAynpkikrdertlin 318
Cdd:cd14665  74 VMEYAaGGELFERICNAG--RFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLL---DGSPA-------------- 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 319 PDIKVVDFG---SATYDDEHHSTlVSTRHYRAPEVILALGWS-QPCDVWSIGCILieYYLGFTVFPTHDSKEhlammeri 394
Cdd:cd14665 135 PRLKICDFGyskSSVLHSQPKST-VGTPAYIAPEVLLKKEYDgKIADVWSCGVTL--YVMLVGAYPFEDPEE-------- 203
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 395 lgplPKHM---IQKTRKRKYFHHDRLdwdehssagrYVSRRCKplkefmlsqdveherlfDLIQKMLEYDPAKRITLREA 471
Cdd:cd14665 204 ----PRNFrktIQRILSVQYSIPDYV----------HISPECR-----------------HLISRIFVADPATRITIPEI 252

                ....*
gi 67551261 472 LKHPF 476
Cdd:cd14665 253 RNHEW 257
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
160-474 3.77e-14

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: 72.37  E-value: 3.77e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDHKAGGRHVAVKIVKNVDRYC-EAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHGHIC 238
Cdd:cd14088   2 RYDLGQVIKTEEFCEIFRAKDKTTGKLYTCKKFLKRDGRKVrKAAKNEINILKMVK--HPN----ILQLVDVFETRKEYF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 239 IVFELL-GLSTYDFIKENGFLPFRldHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteaYNpkikrderTLI 317
Cdd:cd14088  76 IFLELAtGREVFDWILDQGYYSER--DTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVY--------YN--------RLK 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 318 NPDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILieYYLGFTVFPTHDSKEhlammERILGP 397
Cdd:cd14088 138 NSKIVISDFHLAKLENGLIKEPCGTPEYLAPEVVGRQRYGRPVDCWAIGVIM--YILLSGNPPFYDEAE-----EDDYEN 210
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 67551261 398 LPKHMIQKTRKRKYfHHDRLDWDEHSSAGRyvsrrckplkefmlsqdveherlfDLIQKMLEYDPAKRITLREALKH 474
Cdd:cd14088 211 HDKNLFRKILAGDY-EFDSPYWDDISQAAK------------------------DLVTRLMEVEQDQRITAEEAISH 262
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
158-371 4.02e-14

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: 72.74  E-value: 4.02e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 158 SARYEIVDTLGEGAFGKVVECIDhKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLnTTDPNST-FRCVQMLEWFEHHGH 236
Cdd:cd06638  17 SDTWEIIETIGKGTYGKVFKVLN-KKNGSKAAVKILDPIHDIDEEIEAEYNILKAL-SDHPNVVkFYGMYYKKDVKNGDQ 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELL-GLSTYDFIKenGFLPF--RLDH--IRKMAYQICKSVNFLHSNKLTHTDLKPENILFVqsdyTEAynpkikr 311
Cdd:cd06638  95 LWLVLELCnGGSVTDLVK--GFLKRgeRMEEpiIAYILHEALMGLQHLHVNKTIHRDVKGNNILLT----TEG------- 161
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 67551261 312 dertlinpDIKVVDFG-SATYDDEHH--STLVSTRHYRAPEVI-----LALGWSQPCDVWSIGCILIE 371
Cdd:cd06638 162 --------GVKLVDFGvSAQLTSTRLrrNTSVGTPFWMAPEVIaceqqLDSTYDARCDVWSLGITAIE 221
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
161-480 4.07e-14

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: 72.44  E-value: 4.07e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVeCIDHKAGGRHVAVKivkNVDRYCEAARSEIQ--VLEHLNTTDPNSTFrCVQMLEWFEHHGHIC 238
Cdd:cd05609   2 FETIKLISNGAYGAVY-LVRHRETRQRFAMK---KINKQNLILRNQIQqvFVERDILTFAENPF-VVSMYCSFETKRHLC 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 239 IVFELL-GLSTYDFIKENGFLPfrLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrdertli 317
Cdd:cd05609  77 MVMEYVeGGDCATLLKNIGPLP--VDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGH---------------- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 318 npdIKVVDFG--------SATYDDEHH----------STLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVF 379
Cdd:cd05609 139 ---IKLTDFGlskiglmsLTTNLYEGHiekdtrefldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPF 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 380 pthdskehlammeriLGPLPKHMIQKTRKrkyfhhDRLDWDEHSSAgryvsrrckplkefmLSQDVEherlfDLIQKMLE 459
Cdd:cd05609 216 ---------------FGDTPEELFGQVIS------DEIEWPEGDDA---------------LPDDAQ-----DLITRLLQ 254
                       330       340
                ....*....|....*....|....
gi 67551261 460 YDPAKRITLREALK---HPFFDLL 480
Cdd:cd05609 255 QNPLERLGTGGAEEvkqHPFFQDL 278
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
167-407 4.47e-14

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: 72.42  E-value: 4.47e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIDHKAGgRHVAVKIVK------NVDRYCEAARSEIQVLEHLNTTdpnstfRCVQMLEWFEHHGH--IC 238
Cdd:cd06651  15 LGQGAFGRVYLCYDVDTG-RELAAKQVQfdpespETSKEVSALECEIQLLKNLQHE------RIVQYYGCLRDRAEktLT 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 239 IVFELL-GLSTYDFIKENGFLPFRLdhIRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqsdyteaynpkikRDERTli 317
Cdd:cd06651  88 IFMEYMpGGSVKDQLKAYGALTESV--TRKYTRQILEGMSYLHSNMIVHRDIKGANIL---------------RDSAG-- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 318 npDIKVVDFGSAT------YDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYylgFTVFPTHDSKEHLAMM 391
Cdd:cd06651 149 --NVKLGDFGASKrlqticMSGTGIRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEM---LTEKPPWAEYEAMAAI 223
                       250       260
                ....*....|....*....|.
gi 67551261 392 ERILG-----PLPKHMIQKTR 407
Cdd:cd06651 224 FKIATqptnpQLPSHISEHAR 244
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
167-477 4.75e-14

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: 72.26  E-value: 4.75e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIDhKAGGRHVAVKIVKNVDRY--CEA-ARSEIQVLEhLNTTDPnstfRCVQMLEWFEHHGHICIV--- 240
Cdd:cd14198  16 LGRGKFAVVRQCIS-KSTGQEYAAKFLKKRRRGqdCRAeILHEIAVLE-LAKSNP----RVVNLHEVYETTSEIILIley 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 241 ------FELLGLSTYDFIKENgflpfrldHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteaynpkikrder 314
Cdd:cd14198  90 aaggeiFNLCVPDLAEMVSEN--------DIIRLIRQILEGVYYLHQNNIVHLDLKPQNILL------------------ 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 315 TLINP--DIKVVDFGSATyDDEHHSTL---VSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLA 389
Cdd:cd14198 144 SSIYPlgDIKIVDFGMSR-KIGHACELreiMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDNQETFL 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 390 MMERIlgplpkhmiqktrkrkyfhhdRLDWDEHSsagryVSRRCKPLKEFmlsqdveherlfdlIQKMLEYDPAKRITLR 469
Cdd:cd14198 223 NISQV---------------------NVDYSEET-----FSSVSQLATDF--------------IQKLLVKNPEKRPTAE 262

                ....*...
gi 67551261 470 EALKHPFF 477
Cdd:cd14198 263 ICLSHSWL 270
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
158-474 4.95e-14

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: 72.40  E-value: 4.95e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 158 SARY----EIVDTLGEGAFGKVVECiDHKAGGRHVAVKIVKNVDRYCEAAR--SEIQVLEHLNTTDPNSTFRCvqmleWF 231
Cdd:cd14046   1 FSRYltdfEELQVLGKGAFGQVVKV-RNKLDGRYYAIKKIKLRSESKNNSRilREVMLLSRLNHQHVVRYYQA-----WI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 232 EHHgHICIVFELLGLST-YDFIKENGFLPfrLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteaynpkik 310
Cdd:cd14046  75 ERA-NLYIQMEYCEKSTlRDLIDSGLFQD--TDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFL-------------- 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 311 rDErtliNPDIKVVDFGSAT---------YDDEHHSTL------------VSTRHYRAPEViLALGWS---QPCDVWSIG 366
Cdd:cd14046 138 -DS----NGNVKIGDFGLATsnklnvelaTQDINKSTSaalgssgdltgnVGTALYVAPEV-QSGTKStynEKVDMYSLG 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 367 CILIE--YYLGFTvfpthdskehlamMERIlgplpkHMIQKTRKRKYFHHDRLDWDEHSSAGRyvsrrckplkefmlsqd 444
Cdd:cd14046 212 IIFFEmcYPFSTG-------------MERV------QILTALRSVSIEFPPDFDDNKHSKQAK----------------- 255
                       330       340       350
                ....*....|....*....|....*....|
gi 67551261 445 veherlfdLIQKMLEYDPAKRITLREALKH 474
Cdd:cd14046 256 --------LIRWLLNHDPAKRPSAQELLKS 277
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
160-476 5.16e-14

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: 72.07  E-value: 5.16e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDHKAGgRHVAVKIVKNV-------DRYCEAARsEIQVLEHLNttDPNstfrCVQMLEWFE 232
Cdd:cd08222   1 RYRVVRKLGSGNFGTVYLVSDLKAT-ADEELKVLKEIsvgelqpDETVDANR-EAKLLSKLD--HPA----IVKFHDSFV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 233 HHGHICIVFELLglstydfikENGFLPFRLDHIRK----------MAY--QICKSVNFLHSNKLTHTDLKPENILfvqsd 300
Cdd:cd08222  73 EKESFCIVTEYC---------EGGDLDDKISEYKKsgttidenqiLDWfiQLLLAVQYMHERRILHRDLKAKNIF----- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 301 yteaynpkikrdertLINPDIKVVDFG-----SATYDDEhhSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLG 375
Cdd:cd08222 139 ---------------LKNNVIKVGDFGisrilMGTSDLA--TTFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCL 201
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 376 FTVFpthDSKEHLAMMERIL-GPLPKhmiqktrkrkyfhhdrldwdehssagrYVSRRCKPLKEFMLSqdveherlfdli 454
Cdd:cd08222 202 KHAF---DGQNLLSVMYKIVeGETPS---------------------------LPDKYSKELNAIYSR------------ 239
                       330       340
                ....*....|....*....|..
gi 67551261 455 qkMLEYDPAKRITLREALKHPF 476
Cdd:cd08222 240 --MLNKDPALRPSAAEILKIPF 259
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
162-479 5.26e-14

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: 72.46  E-value: 5.26e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 162 EIVDTLGEGAFGkVVECIDHKAGGRHVAVKIVknvdRYCEAARSEIQVLEHLNTTdpNSTFRCVQMLEWFE---HHGHIC 238
Cdd:cd06617   4 EVIEELGRGAYG-VVDKMRHVPTGTIMAVKRI----RATVNSQEQKRLLMDLDIS--MRSVDCPYTVTFYGalfREGDVW 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 239 IVFELLGLSTYDFIKENGFLPFRL--DHIRKMAYQICKSVNFLHSN-KLTHTDLKPENILfvqsdyteaynpkIKRdert 315
Cdd:cd06617  77 ICMEVMDTSLDKFYKKVYDKGLTIpeDILGKIAVSIVKALEYLHSKlSVIHRDVKPSNVL-------------INR---- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 316 liNPDIKVVDFGSATY--DDEHHSTLVSTRHYRAPEVI----LALGWSQPCDVWSIGCILIEYYLGftVFPTHDSKEHLA 389
Cdd:cd06617 140 --NGQVKLCDFGISGYlvDSVAKTIDAGCKPYMAPERInpelNQKGYDVKSDVWSLGITMIELATG--RFPYDSWKTPFQ 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 390 MMERIL-GPLPKhmiqktrkrkyfhhdrldwdehssagryvsrrckpLKEFMLSQDVEherlfDLIQKMLEYDPAKRITL 468
Cdd:cd06617 216 QLKQVVeEPSPQ-----------------------------------LPAEKFSPEFQ-----DFVNKCLKKNYKERPNY 255
                       330
                ....*....|.
gi 67551261 469 REALKHPFFDL 479
Cdd:cd06617 256 PELLQHPFFEL 266
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
166-380 6.44e-14

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: 72.13  E-value: 6.44e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 166 TLGEGAFGKVVEC----IDHKAGGRHVAVKIVKNVDRYCE--AARSEIQVLEHLnttdpNSTFRCVQMLEWFEHHGHICI 239
Cdd:cd05055  42 TLGAGAFGKVVEAtaygLSKSDAVMKVAVKMLKPTAHSSEreALMSELKIMSHL-----GNHENIVNLLGACTIGGPILV 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 240 VFELL---GLSTYDFIKENGFLPFrlDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSdyteaynpKIkrdertl 316
Cdd:cd05055 117 ITEYCcygDLLNFLRRKRESFLTL--EDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTHG--------KI------- 179
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 67551261 317 inpdIKVVDFGSATyDDEHHSTLVSTRHYR------APEVILALGWSQPCDVWSIGCILIEYY-LGFTVFP 380
Cdd:cd05055 180 ----VKICDFGLAR-DIMNDSNYVVKGNARlpvkwmAPESIFNCVYTFESDVWSYGILLWEIFsLGSNPYP 245
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
161-477 6.98e-14

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


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 72.70  E-value: 6.98e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGkVVECIDHKAGGRHVAVKIVKN---VDRYCEAA-RSEIQVLehlntTDPNSTFrCVQMLEWFEHHGH 236
Cdd:cd05573   3 FEVIKVIGRGAFG-EVWLVRDKDTGQVYAMKILRKsdmLKREQIAHvRAERDIL-----ADADSPW-IVRLHYAFQDEDH 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELLG-------LSTYDFIKEngflpfrlDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILF------------V 297
Cdd:cd05573  76 LYLVMEYMPggdlmnlLIKYDVFPE--------ETARFYIAELVLALDSLHKLGFIHRDIKPDNILLdadghikladfgL 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 298 QSDYTEAYNPKIKRDERTLINPDIKVVDFGSATYDDEHHS-TLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGF 376
Cdd:cd05573 148 CTKMNKSGDRESYLNDSVNTLFQDNVLARRRPHKQRRVRAySAVGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGF 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 377 TVFPTHDSKEhlammerilgplpkhmiqkTRKRKyfhhdrLDWDEHssagryvsrrckpLKeFMLSQDVEHERLfDLIQK 456
Cdd:cd05573 228 PPFYSDSLVE-------------------TYSKI------MNWKES-------------LV-FPDDPDVSPEAI-DLIRR 267
                       330       340
                ....*....|....*....|..
gi 67551261 457 MLEyDPAKRITLREALK-HPFF 477
Cdd:cd05573 268 LLC-DPEDRLGSAEEIKaHPFF 288
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
160-475 8.79e-14

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: 71.26  E-value: 8.79e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDhKAGGRHVAVKIVKN-----VDRycEAARSEIQVLEHLNTTDpnstfRCVQMLEWFEHH 234
Cdd:cd13997   1 HFHELEQIGSGSFSEVFKVRS-KVDGCLYAVKKSKKpfrgpKER--ARALREVEAHAALGQHP-----NIVRYYSSWEEG 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 235 GHICIVFELLGL-STYDFIKENGfLPFRLDH--IRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqsdyteaynpkIKR 311
Cdd:cd13997  73 GHLYIQMELCENgSLQDALEELS-PISKLSEaeVWDLLLQVALGLAFIHSKGIVHLDIKPDNIF-------------ISN 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 312 DERtlinpdIKVVDFGSATYDDEHHSTLVSTRHYRAPEVI-LALGWSQPCDVWSigcilieyyLGFTVFpthdskehlam 390
Cdd:cd13997 139 KGT------CKIGDFGLATRLETSGDVEEGDSRYLAPELLnENYTHLPKADIFS---------LGVTVY----------- 192
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 391 mERILG-PLPkhmiqktRKRKYFHHDRLDwdehssagryvsrRCKPLKEFMLSQDveherLFDLIQKMLEYDPAKRITLR 469
Cdd:cd13997 193 -EAATGePLP-------RNGQQWQQLRQG-------------KLPLPPGLVLSQE-----LTRLLKVMLDPDPTRRPTAD 246

                ....*.
gi 67551261 470 EALKHP 475
Cdd:cd13997 247 QLLAHD 252
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
161-477 1.04e-13

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: 71.65  E-value: 1.04e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECiDHKAGGRHVAVKIVknvdRYCEAARSEIQVLEHLNTTDPNSTFRCVQMLEWFEHHGHICIV 240
Cdd:cd07869   7 YEKLEKLGEGSYATVYKG-KSKVNGKLVALKVI----RLQEEEGTPFTAIREASLLKGLKHANIVLLHDIIHTKETLTLV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 241 FELLGLSTYDFIKEN--GFLPfrlDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqSDYTEaynpkikrdertlin 318
Cdd:cd07869  82 FEYVHTDLCQYMDKHpgGLHP---ENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLI--SDTGE--------------- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 319 pdIKVVDFGSA---TYDDEHHSTLVSTRHYRAPEVIL-ALGWSQPCDVWSIGCILIEYYLGFTVFP-THDSKEHLAMMER 393
Cdd:cd07869 142 --LKLADFGLArakSVPSHTYSNEVVTLWYRPPDVLLgSTEYSTCLDMWGVGCIFVEMIQGVAAFPgMKDIQDQLERIFL 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 394 ILGPLPKHMIQKTRKRKYFHHDRLDWdehssagrYVSRRCKplKEFMLSQDVEHERlfDLIQKMLEYDPAKRITLREALK 473
Cdd:cd07869 220 VLGTPNEDTWPGVHSLPHFKPERFTL--------YSPKNLR--QAWNKLSYVNHAE--DLASKLLQCFPKNRLSAQAALS 287

                ....
gi 67551261 474 HPFF 477
Cdd:cd07869 288 HEYF 291
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
265-477 1.09e-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: 72.02  E-value: 1.09e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 265 IRKMAYQICKSVNFLHSNKLTHTDLKPENILFVqsdyteAYNPKIKRdertlinpdIKVVDFGSATYDDEHHSTL----- 339
Cdd:cd07867 111 VKSLLYQILDGIHYLHANWVLHRDLKPANILVM------GEGPERGR---------VKIADMGFARLFNSPLKPLadldp 175
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 340 -VSTRHYRAPEVIL-ALGWSQPCDVWSIGCILIEYYLGFTVFptHDSKEHLammeRILGPLPKHMIQKTRKRKYFHHDRl 417
Cdd:cd07867 176 vVVTFWYRAPELLLgARHYTKAIDIWAIGCIFAELLTSEPIF--HCRQEDI----KTSNPFHHDQLDRIFSVMGFPADK- 248
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 418 DWDEHSSAGRYVS-----RRC----KPLKEFMLSQDVEHE-RLFDLIQKMLEYDPAKRITLREALKHPFF 477
Cdd:cd07867 249 DWEDIRKMPEYPTlqkdfRRTtyanSSLIKYMEKHKVKPDsKVFLLLQKLLTMDPTKRITSEQALQDPYF 318
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
167-405 1.17e-13

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: 71.21  E-value: 1.17e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIDHKAGGRHVAVKIVKN--VDRYCEA-ARSEIQVLEHLNTtdpnstfRCVQMLEW-FEHHGHICIVFE 242
Cdd:cd05630   8 LGKGGFGEVCACQVRATGKMYACKKLEKKriKKRKGEAmALNEKQILEKVNS-------RFVVSLAYaYETKDALCLVLT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 243 LLGLSTYDF----IKENGFlpfrlDHIRKMAY--QICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrdertl 316
Cdd:cd05630  81 LMNGGDLKFhiyhMGQAGF-----PEARAVFYaaEICCGLEDLHRERIVYRDLKPENILLDDHGH--------------- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 317 inpdIKVVDFGSATYDDEHHST--LVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMMERI 394
Cdd:cd05630 141 ----IRISDLGLAVHVPEGQTIkgRVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVERL 216
                       250
                ....*....|.
gi 67551261 395 LGPLPKHMIQK 405
Cdd:cd05630 217 VKEVPEEYSEK 227
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
161-477 1.32e-13

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: 71.31  E-value: 1.32e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAfGKVVECIDHKAGGRHVAVKIVKNVDRycEAARSEI----QVLEhlnttDPNSTFrCVQMLEWFEHHGH 236
Cdd:cd06615   3 FEKLGELGAGN-GGVVTKVLHRPSGLIMARKLIHLEIK--PAIRNQIirelKVLH-----ECNSPY-IVGFYGAFYSDGE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELL-GLSTYDFIKENGFLPfrLDHIRKMAYQICKSVNFLHSN-KLTHTDLKPENILfVQSdyteaynpkikrder 314
Cdd:cd06615  74 ISICMEHMdGGSLDQVLKKAGRIP--ENILGKISIAVLRGLTYLREKhKIMHRDVKPSNIL-VNS--------------- 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 315 tliNPDIKVVDFG-SATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMMER 393
Cdd:cd06615 136 ---RGEIKLCDFGvSGQLIDSMANSFVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGRYPIPPPDAKELEAMFGR 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 394 ---------ILGPLPKHMIQKTRKRKYFhhDRLDWDEHSSAGRyvsrrckplkefmLSQDVEHERLFDLIQKMLEYDPAK 464
Cdd:cd06615 213 pvsegeakeSHRPVSGHPPDSPRPMAIF--ELLDYIVNEPPPK-------------LPSGAFSDEFQDFVDKCLKKNPKE 277
                       330
                ....*....|...
gi 67551261 465 RITLREALKHPFF 477
Cdd:cd06615 278 RADLKELTKHPFI 290
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
161-385 1.83e-13

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 isoforms resulting from alternative translation initiation sites. PIM1 is the founding member of the PIM subfamily. It is involved in regulating cell growth, differentiation, and apoptosis. It promotes cancer development when overexpressed by inhibiting apoptosis, promoting cell proliferation, and promoting genomic instability. The PIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 70.38  E-value: 1.83e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIdHKAGGRHVAVKIVKNvDRYCE------AAR--SEIQVLEHLNttdpnSTFRCV-QMLEWF 231
Cdd:cd14100   2 YQVGPLLGSGGFGSVYSGI-RVADGAPVAIKHVEK-DRVSEwgelpnGTRvpMEIVLLKKVG-----SGFRGViRLLDWF 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 232 EHHGHICIVFELLGL--STYDFIKENGFLPFRLdhIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteaynpki 309
Cdd:cd14100  75 ERPDSFVLVLERPEPvqDLFDFITERGALPEEL--ARSFFRQVLEAVRHCHNCGVLHRDIKDENILI------------- 139
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 67551261 310 krDERTlinPDIKVVDFGS-ATYDDEHHSTLVSTRHYRAPEVILALGW-SQPCDVWSIGCILIEYYLGFTVFpTHDSK 385
Cdd:cd14100 140 --DLNT---GELKLIDFGSgALLKDTVYTDFDGTRVYSPPEWIRFHRYhGRSAAVWSLGILLYDMVCGDIPF-EHDEE 211
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
167-397 4.05e-13

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: 70.03  E-value: 4.05e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVeCIDHKAGGRHVAVKIVKN--VDRYCEAARS--EIQVLEhlNTTDPNSTfrcvqMLEW-FEHHGHICIVF 241
Cdd:cd05595   3 LGKGTFGKVI-LVREKATGRYYAMKILRKevIIAKDEVAHTvtESRVLQ--NTRHPFLT-----ALKYaFQTHDRLCFVM 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 242 ELL--GLSTYDFIKENGFLPfrlDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrdertlinp 319
Cdd:cd05595  75 EYAngGELFFHLSRERVFTE---DRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGH------------------ 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 320 dIKVVDFG---SATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKE--HLAMMERI 394
Cdd:cd05595 134 -IKITDFGlckEGITDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERlfELILMEEI 212

                ...
gi 67551261 395 LGP 397
Cdd:cd05595 213 RFP 215
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
265-477 4.32e-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: 70.09  E-value: 4.32e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 265 IRKMAYQICKSVNFLHSNKLTHTDLKPENILFVqsdyteAYNPKIKRdertlinpdIKVVDFGSATYDDEHHSTL----- 339
Cdd:cd07868 126 VKSLLYQILDGIHYLHANWVLHRDLKPANILVM------GEGPERGR---------VKIADMGFARLFNSPLKPLadldp 190
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 340 -VSTRHYRAPEVIL-ALGWSQPCDVWSIGCILIEYYLGFTVFptHDSKEHLammeRILGPLPKHMIQKTRKRKYFHHDRl 417
Cdd:cd07868 191 vVVTFWYRAPELLLgARHYTKAIDIWAIGCIFAELLTSEPIF--HCRQEDI----KTSNPYHHDQLDRIFNVMGFPADK- 263
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 418 DWD------EHSSAGRYVSR----RCKPLKEFMLSQDVEHERLFDLIQKMLEYDPAKRITLREALKHPFF 477
Cdd:cd07868 264 DWEdikkmpEHSTLMKDFRRntytNCSLIKYMEKHKVKPDSKAFHLLQKLLTMDPIKRITSEQAMQDPYF 333
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
160-371 4.47e-13

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: 69.22  E-value: 4.47e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDhKAGGRHVAVK---IVKNVDRYCEAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHGH 236
Cdd:cd08225   1 RYEIIKKIGEGSFGKIYLAKA-KSDSEHCVIKeidLTKMPVKEKEASKKEVILLAKMK--HPN----IVTFFASFQENGR 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELL-GLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENIlFVQSDYTEAynpkikrdert 315
Cdd:cd08225  74 LFIVMEYCdGGDLMKRINRQRGVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNI-FLSKNGMVA----------- 141
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 67551261 316 linpdiKVVDFGSA-TYDD--EHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIE 371
Cdd:cd08225 142 ------KLGDFGIArQLNDsmELAYTCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYE 194
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
162-375 4.47e-13

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: 69.39  E-value: 4.47e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 162 EIVDTLGEGAFGKVVEcIDHKAGGRHVAVKIVknvdrYCEAARS-------EIQVLEHLnttdpnstfRCVQMLEWF--- 231
Cdd:cd06620   8 ETLKDLGAGNGGSVSK-VLHIPTGTIMAKKVI-----HIDAKSSvrkqilrELQILHEC---------HSPYIVSFYgaf 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 232 -EHHGHICIVFELLGLSTYDFI-KENGflPFRLDHIRKMAYQICKSVNFLHS-NKLTHTDLKPENILFvqsdyteayNPK 308
Cdd:cd06620  73 lNENNNIIICMEYMDCGSLDKIlKKKG--PFPEEVLGKIAVAVLEGLTYLYNvHRIIHRDIKPSNILV---------NSK 141
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 67551261 309 ikrdertlinPDIKVVDFG-SATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLG 375
Cdd:cd06620 142 ----------GQIKLCDFGvSGELINSIADTFVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALG 199
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
165-399 4.72e-13

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: 69.30  E-value: 4.72e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 165 DTLGEGAFGKVVECIdhkAGGRHVAVKIVK-----NVDRYCEAARSEIQVLEHLntTDPN-STFRCVQMLEwfehhGHIC 238
Cdd:cd14145  12 EIIGIGGFGKVYRAI---WIGDEVAVKAARhdpdeDISQTIENVRQEAKLFAML--KHPNiIALRGVCLKE-----PNLC 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 239 IVFELLGLSTYDFIKENGFLPfrLDHIRKMAYQICKSVNFLHSNKLT---HTDLKPENILFVQsdyteaynpKIKRDErt 315
Cdd:cd14145  82 LVMEFARGGPLNRVLSGKRIP--PDILVNWAVQIARGMNYLHCEAIVpviHRDLKSSNILILE---------KVENGD-- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 316 LINPDIKVVDFGSATydDEHHSTLVS---TRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHD--SKEHLAM 390
Cdd:cd14145 149 LSNKILKITDFGLAR--EWHRTTKMSaagTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPFRGIDglAVAYGVA 226

                ....*....
gi 67551261 391 MERILGPLP 399
Cdd:cd14145 227 MNKLSLPIP 235
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
161-476 5.26e-13

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 1; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. MEK1 also plays a role in cell cycle control. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 69.70  E-value: 5.26e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAfGKVVECIDHKAGGRHVAVKIVKNVDRycEAARS----EIQVLEHLNTTdpnstfRCVQMLEWFEHHGH 236
Cdd:cd06650   7 FEKISELGAGN-GGVVFKVSHKPSGLVMARKLIHLEIK--PAIRNqiirELQVLHECNSP------YIVGFYGAFYSDGE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELL-GLSTYDFIKENGFLPFRLdhIRKMAYQICKSVNFL-HSNKLTHTDLKPENILfVQSdyteaynpkikRDEr 314
Cdd:cd06650  78 ISICMEHMdGGSLDQVLKKAGRIPEQI--LGKVSIAVIKGLTYLrEKHKIMHRDVKPSNIL-VNS-----------RGE- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 315 tlinpdIKVVDFG-SATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEhlamMER 393
Cdd:cd06650 143 ------IKLCDFGvSGQLIDSMANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIPPPDAKE----LEL 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 394 ILGplpkhmiqKTRKRKYFHHDRLDWDEHSSAGRYVSRRCKPLKEFMLSQDVEHE------------RLFDLIQKMLEYD 461
Cdd:cd06650 213 MFG--------CQVEGDAAETPPRPRTPGRPLSSYGMDSRPPMAIFELLDYIVNEpppklpsgvfslEFQDFVNKCLIKN 284
                       330
                ....*....|....*
gi 67551261 462 PAKRITLREALKHPF 476
Cdd:cd06650 285 PAERADLKQLMVHAF 299
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
167-373 6.24e-13

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: 68.63  E-value: 6.24e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVecIDHKAGGRHVAVKIVKnvdrycEAARSEIQVLEHLNTTDPNSTFRCVQMLEWFEHHGHICIVFELLGL 246
Cdd:cd05059  12 LGSGQFGVVH--LGKWRGKIDVAIKMIK------EGSMSEDDFIEEAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEYMAN 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 247 -STYDFIKENGFLpFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfVQSDYTeaynpkikrdertlinpdIKVVD 325
Cdd:cd05059  84 gCLLNYLRERRGK-FQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCL-VGEQNV------------------VKVSD 143
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 67551261 326 FGSATY--DDEHHSTlVSTR---HYRAPEVILALGWSQPCDVWSIGCILIEYY 373
Cdd:cd05059 144 FGLARYvlDDEYTSS-VGTKfpvKWSPPEVFMYSKFSSKSDVWSFGVLMWEVF 195
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
167-379 7.48e-13

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: 68.84  E-value: 7.48e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIdHKAGGRHVAVK------IVKNVDRYCeaarSEIQVLEHLNTTDPNSTFRCVQMLEWFEHHGHICIV 240
Cdd:cd14038   2 LGTGGFGNVLRWI-NQETGEQVAIKqcrqelSPKNRERWC----LEIQIMKRLNHPNVVAARDVPEGLQKLAPNDLPLLA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 241 FELL---GLSTYDFIKENgFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSdyteaynpkikrdERTLI 317
Cdd:cd14038  77 MEYCqggDLRKYLNQFEN-CCGLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQG-------------EQRLI 142
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 67551261 318 NpdiKVVDFGSATYDDEHH--STLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVF 379
Cdd:cd14038 143 H---KIIDLGYAKELDQGSlcTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPF 203
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
160-473 7.99e-13

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


Pssm-ID: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 68.32  E-value: 7.99e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVvECIDHKAGGRHVAVKIVKNVdryceaarseiqvleHLNTTDPNSTFRCVQMLEWFeHHGHICI 239
Cdd:cd14072   1 NYRLLKTIGKGNFAKV-KLARHVLTGREVAIKIIDKT---------------QLNPSSLQKLFREVRIMKIL-NHPNIVK 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 240 VFELL--------------GLSTYDFIKENGFLpfRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQsdyteay 305
Cdd:cd14072  64 LFEVIetektlylvmeyasGGEVFDYLVAHGRM--KEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDA------- 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 306 npkikrdertliNPDIKVVDFGsatYDDEHHS-----TLVSTRHYRAPEVILALGWSQP-CDVWSIGCILIEYYLGFTVF 379
Cdd:cd14072 135 ------------DMNIKIADFG---FSNEFTPgnkldTFCGSPPYAAPELFQGKKYDGPeVDVWSLGVILYTLVSGSLPF 199
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 380 PTHDSKEhlaMMERILgplpkhmiqktrkrkyfhhdrldwdehssagryvsrRCKPLKEFMLSQDVEherlfDLIQKMLE 459
Cdd:cd14072 200 DGQNLKE---LRERVL------------------------------------RGKYRIPFYMSTDCE-----NLLKKFLV 235
                       330
                ....*....|....
gi 67551261 460 YDPAKRITLREALK 473
Cdd:cd14072 236 LNPSKRGTLEQIMK 249
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
161-399 1.09e-12

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: 67.92  E-value: 1.09e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIdHKAGGRHVAVKIVKN----VDRYC-EAARSE---IQVLEHLNTTdpnstfrcvQMLEWFE 232
Cdd:cd14070   4 YLIGRKLGEGSFAKVREGL-HAVTGEKVAIKVIDKkkakKDSYVtKNLRREgriQQMIRHPNIT---------QLLDILE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 233 HHGHICIVFEL-LGLSTYDFIKENGFLPFRldHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteaynpkikr 311
Cdd:cd14070  74 TENSYYLVMELcPGGNLMHRIYDKKRLEER--EARRYIRQLVSAVEHLHRAGVVHRDLKIENLLL--------------- 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 312 DErtliNPDIKVVDFG-SATYDDEHHSTLVSTR----HYRAPEVILALGWSQPCDVWSIGCILIEYYLG---FTVFPTHD 383
Cdd:cd14070 137 DE----NDNIKLIDFGlSNCAGILGYSDPFSTQcgspAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGtlpFTVEPFSL 212
                       250
                ....*....|....*.
gi 67551261 384 SKEHLAMMERILGPLP 399
Cdd:cd14070 213 RALHQKMVDKEMNPLP 228
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
167-477 1.14e-12

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: 68.07  E-value: 1.14e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVecIDHKAGGRHVAVKIVknVDRYCEAARSEIQVL----EHLNttdpnstfrcvqMLEWF---EHHGHICI 239
Cdd:cd13982   9 LGYGSEGTIV--FRGTFDGRPVAVKRL--LPEFFDFADREVQLLresdEHPN------------VIRYFcteKDRQFLYI 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 240 VFELLGLSTYDFIK---------ENGFLPFRLdhirkmAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYTEaynpkik 310
Cdd:cd13982  73 ALELCAASLQDLVEspresklflRPGLEPVRL------LRQIASGLAHLHSLNIVHRDLKPQNILISTPNAHG------- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 311 rdertliNPDIKVVDFG-SATYDDEHHS-----TLVSTRHYRAPEVIlalgwSQPC--------DVWSIGCILieYYLgf 376
Cdd:cd13982 140 -------NVRAMISDFGlCKKLDVGRSSfsrrsGVAGTSGWIAPEML-----SGSTkrrqtravDIFSLGCVF--YYV-- 203
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 377 tvfpthdskehLAMMERILGplpkhmiqktrkrkyfhhDRLDWDEHSSAGRYVSRRCKPLKEFmlsqDVEHErlfDLIQK 456
Cdd:cd13982 204 -----------LSGGSHPFG------------------DKLEREANILKGKYSLDKLLSLGEH----GPEAQ---DLIER 247
                       330       340
                ....*....|....*....|.
gi 67551261 457 MLEYDPAKRITLREALKHPFF 477
Cdd:cd13982 248 MIDFDPEKRPSAEEVLNHPFF 268
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
167-477 1.67e-12

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: 68.18  E-value: 1.67e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVeCIDHKAGGRHVAVKIVKN----VDRYCEAARSEIQVLEhLNTTDPnstFRCvQMLEWFEHHGHICIVFE 242
Cdd:cd05592   3 LGKGSFGKVM-LAELKGTNQYFAIKALKKdvvlEDDDVECTMIERRVLA-LASQHP---FLT-HLFCTFQTESHLFFVME 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 243 LLGLSTYDF-IKENGflPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqsdyteaynpkIKRDERtlinpdI 321
Cdd:cd05592  77 YLNGGDLMFhIQQSG--RFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVL-------------LDREGH------I 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 322 KVVDFGSA---TYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKE--HLAMMERILG 396
Cdd:cd05592 136 KIADFGMCkenIYGENKASTFCGTPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDElfWSICNDTPHY 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 397 PlpkhmiqktrkrkyfhhdrldwdehssagRYVSRRCKplkefmlsqdveherlfDLIQKMLEYDPAKRITLREALK--- 473
Cdd:cd05592 216 P-----------------------------RWLTKEAA-----------------SCLSLLLERNPEKRLGVPECPAgdi 249

                ....*.
gi 67551261 474 --HPFF 477
Cdd:cd05592 250 rdHPFF 255
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
167-465 1.98e-12

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: 67.63  E-value: 1.98e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVveCI-DHKAGGRHVAVKI------VKNVDRYCEaarsEIQVLEHLNttDPNSTFRCvQMLEWFEHHGHICI 239
Cdd:cd14039   1 LGTGGFGNV--CLyQNQETGEKIAIKScrlelsVKNKDRWCH----EIQIMKKLN--HPNVVKAC-DVPEEMNFLVNDVP 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 240 VFELLGLSTYDFIK-----ENgFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdytEAYNPKIKRder 314
Cdd:cd14039  72 LLAMEYCSGGDLRKllnkpEN-CCGLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVL------QEINGKIVH--- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 315 tlinpdiKVVDFGSATYDDEHH--STLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHdskehlamme 392
Cdd:cd14039 142 -------KIIDLGYAKDLDQGSlcTSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPFLHN---------- 204
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 67551261 393 riLGPLPKHmiQKTRKRKyfHHDRLDWDEHSSAGRYVSRRCKP--LKEFMLsqdvehERLFDLIQKMLEYDPAKR 465
Cdd:cd14039 205 --LQPFTWH--EKIKKKD--PKHIFAVEEMNGEVRFSTHLPQPnnLCSLIV------EPMEGWLQLMLNWDPVQR 267
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
167-477 2.11e-12

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: 67.71  E-value: 2.11e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIDHKAGGRHVAVKIVKN--VDRYCEA-ARSEIQVLEHLNttdpnSTFrCVQMLEWFEHHGHICIVFEL 243
Cdd:cd05631   8 LGKGGFGEVCACQVRATGKMYACKKLEKKriKKRKGEAmALNEKRILEKVN-----SRF-VVSLAYAYETKDALCLVLTI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 244 LGLSTYDF----IKENGFlpfrlDHIRKMAY--QICKSVNFLHSNKLTHTDLKPENILFvqsdyteaynpkikrDERTli 317
Cdd:cd05631  82 MNGGDLKFhiynMGNPGF-----DEQRAIFYaaELCCGLEDLQRERIVYRDLKPENILL---------------DDRG-- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 318 npDIKVVDFGSATYDDEHHSTL--VSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFpthdskehlammeril 395
Cdd:cd05631 140 --HIRISDLGLAVQIPEGETVRgrVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPF---------------- 201
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 396 gplpkhmiqktRKRKyfhhDRLDWDEhssagryVSRRCKPLKEFMLSQDVEHERlfDLIQKMLEYDPAKRITLR-----E 470
Cdd:cd05631 202 -----------RKRK----ERVKREE-------VDRRVKEDQEEYSEKFSEDAK--SICRMLLTKNPKERLGCRgngaaG 257

                ....*..
gi 67551261 471 ALKHPFF 477
Cdd:cd05631 258 VKQHPIF 264
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
167-465 2.47e-12

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: 67.47  E-value: 2.47e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIdHKAGGRHVAVKIVK----NVDRYCEAARSEIQVLEHLNTTDPNSTFRCVQMLEWFEHHGHICIVFE 242
Cdd:cd13989   1 LGSGGFGYVTLWK-HQDTGEYVAIKKCRqelsPSDKNRERWCLEVQIMKKLNHPNVVSARDVPPELEKLSPNDLPLLAME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 243 ----------LLGLSTYDFIKENgflpfrldHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYTEAYnpkikrd 312
Cdd:cd13989  80 ycsggdlrkvLNQPENCCGLKES--------EVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGRVIY------- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 313 ertlinpdiKVVDFGSATYDDEHH--STLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHdskehlam 390
Cdd:cd13989 145 ---------KLIDLGYAKELDQGSlcTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPFLPN-------- 207
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 67551261 391 meriLGPLPKHMIQKTRKRKyfhHDRLdWDEHSSAGRYVSrrcKPLKEFMLSQDVEhERLFDLIQKMLEYDPAKR 465
Cdd:cd13989 208 ----WQPVQWHGKVKQKKPE---HICA-YEDLTGEVKFSS---ELPSPNHLSSILK-EYLESWLQLMLRWDPRQR 270
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
167-477 2.53e-12

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: 67.38  E-value: 2.53e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECiDHKAGGRHVAVK------IVKnvdRYCEA-ARSEIQVLEHLNttdpnSTFrCVQMLEWFEHHGHICI 239
Cdd:cd05605   8 LGKGGFGEVCAC-QVRATGKMYACKklekkrIKK---RKGEAmALNEKQILEKVN-----SRF-VVSLAYAYETKDALCL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 240 VFELLGLSTYDF----IKENGFLPFRldhIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqSDYTEaynpkikrdert 315
Cdd:cd05605  78 VLTIMNGGDLKFhiynMGNPGFEEER---AVFYAAEITCGLEHLHSERIVYRDLKPENILL--DDHGH------------ 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 316 linpdIKVVDFGSATYDDEHHST--LVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFpthdskehlammer 393
Cdd:cd05605 141 -----VRISDLGLAVEIPEGETIrgRVGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPF-------------- 201
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 394 ilgplpkhmiqktRKRKyfhhDRLDWDEhssagryVSRRCKPLKEFMLSQDVEHERlfDLIQKMLEYDPAKRITLREA-- 471
Cdd:cd05605 202 -------------RARK----EKVKREE-------VDRRVKEDQEEYSEKFSEEAK--SICSQLLQKDPKTRLGCRGEga 255

                ....*....
gi 67551261 472 ---LKHPFF 477
Cdd:cd05605 256 edvKSHPFF 264
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
159-408 3.13e-12

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: 66.97  E-value: 3.13e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 159 ARYEIVDTLGEGAFGKVVECIDHkAGGRHVAVKIVKNVDRYCEAARS----EIQVLEHLNttDPNstfrCVQMLEWFEHH 234
Cdd:cd08228   2 ANFQIEKKIGRGQFSEVYRATCL-LDRKPVALKKVQIFEMMDAKARQdcvkEIDLLKQLN--HPN----VIKYLDSFIED 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 235 GHICIVFEL-----LGLSTYDFIKENGFLPFRLdhIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYTEAynpki 309
Cdd:cd08228  75 NELNIVLELadagdLSQMIKYFKKQKRLIPERT--VWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKL----- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 310 krdertlinPDIKVVDFGSATYDDEHhsTLVSTRHYRAPEVILALGWSQPCDVWSIGCILieYYLGFTVFPTHDSKEHL- 388
Cdd:cd08228 148 ---------GDLGLGRFFSSKTTAAH--SLVGTPYYMSPERIHENGYNFKSDIWSLGCLL--YEMAALQSPFYGDKMNLf 214
                       250       260
                ....*....|....*....|....*
gi 67551261 389 AMMERI----LGPLPK-HMIQKTRK 408
Cdd:cd08228 215 SLCQKIeqcdYPPLPTeHYSEKLRE 239
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
160-475 3.47e-12

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: 66.29  E-value: 3.47e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIdHKAGGRHVAVKIVKnVDRYC----EAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHG 235
Cdd:cd08220   1 KYEKIRVVGRGAYGTVYLCR-RKDDNKLVIIKQIP-VEQMTkeerQAALNEVKVLSMLH--HPN----IIEYYESFLEDK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 236 HICIVFELL-GLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteaynpkikrDER 314
Cdd:cd08220  73 ALMIVMEYApGGTLFEYIQQRKGSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILL---------------NKK 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 315 TLInpdIKVVDFGSATY--DDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEyylgftvfpthdskehLAMME 392
Cdd:cd08220 138 RTV---VKIGDFGISKIlsSKSKAYTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYE----------------LASLK 198
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 393 RIL--GPLPKhMIQKTRKRKYfhhdrldwdehssagryvsrrcKPLKEfMLSQDVEHerlfdLIQKMLEYDPAKRITLRE 470
Cdd:cd08220 199 RAFeaANLPA-LVLKIMRGTF----------------------APISD-RYSEELRH-----LILSMLHLDPNKRPTLSE 249

                ....*
gi 67551261 471 ALKHP 475
Cdd:cd08220 250 IMAQP 254
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
164-476 3.59e-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: 66.62  E-value: 3.59e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 164 VDTLGEGAFGKVVECIDHKAGgRHVAVKIV--KNVDRYCEAARSEIQVLEHLNTTDPNSTFRCvqmlewFEHHGHICIVF 241
Cdd:cd06642   9 LERIGKGSFGEVYKGIDNRTK-EVVAIKIIdlEEAEDEIEDIQQEITVLSQCDSPYITRYYGS------YLKGTKLWIIM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 242 ELLGL-STYDFIKENgflPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDyteaynpkikrdertlinpD 320
Cdd:cd06642  82 EYLGGgSALDLLKPG---PLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQG-------------------D 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 321 IKVVDFGSA---TYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTvfPTHDskehLAMMeRILGP 397
Cdd:cd06642 140 VKLADFGVAgqlTDTQIKRNTFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEP--PNSD----LHPM-RVLFL 212
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 67551261 398 LPKHmiqktrkrkyfhhdrldwDEHSSAGRYvsrrCKPLKEFmlsqdveherlfdlIQKMLEYDPAKRITLREALKHPF 476
Cdd:cd06642 213 IPKN------------------SPPTLEGQH----SKPFKEF--------------VEACLNKDPRFRPTAKELLKHKF 255
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
164-476 4.14e-12

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: 66.61  E-value: 4.14e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 164 VDTLGEGAFGKVVECIDHKAGgRHVAVKIV--KNVDRYCEAARSEIQVLEHLNTTDPNSTFRCvqmlewFEHHGHICIVF 241
Cdd:cd06640   9 LERIGKGSFGEVFKGIDNRTQ-QVVAIKIIdlEEAEDEIEDIQQEITVLSQCDSPYVTKYYGS------YLKGTKLWIIM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 242 ELLGL-STYDFIKENGFLPFRldhIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDyteaynpkikrdertlinpD 320
Cdd:cd06640  82 EYLGGgSALDLLRAGPFDEFQ---IATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQG-------------------D 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 321 IKVVDFGSA---TYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTvfPTHDSKEHlammeRILGP 397
Cdd:cd06640 140 VKLADFGVAgqlTDTQIKRNTFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEP--PNSDMHPM-----RVLFL 212
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 67551261 398 LPKHmiqktrkrkyfhhdrldwdehsSAGRYVSRRCKPLKEFmlsqdveherlfdlIQKMLEYDPAKRITLREALKHPF 476
Cdd:cd06640 213 IPKN----------------------NPPTLVGDFSKPFKEF--------------IDACLNKDPSFRPTAKELLKHKF 255
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
160-476 4.17e-12

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: 66.33  E-value: 4.17e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGkVVECIDHKAGGRHVAVKIVKNVDRYCEAARSEIqvLEHLNTTDPNstfrCVQMLEWFEHHGHICI 239
Cdd:cd14662   1 RYELVKDIGSGNFG-VARLMRNKETKELVAVKYIERGLKIDENVQREI--INHRSLRHPN----IIRFKEVVLTPTHLAI 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 240 VFELL-GLSTYDFIKENGflPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsDYTEAynpkikrdertlin 318
Cdd:cd14662  74 VMEYAaGGELFERICNAG--RFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLL---DGSPA-------------- 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 319 PDIKVVDFG---SATYDDEHHSTlVSTRHYRAPEVILALGWS-QPCDVWSIGCILieYYLGFTVFPTHDSKEhlammeri 394
Cdd:cd14662 135 PRLKICDFGyskSSVLHSQPKST-VGTPAYIAPEVLSRKEYDgKVADVWSCGVTL--YVMLVGAYPFEDPDD-------- 203
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 395 lgplPKHM---IQKTRKRKYFHHDrldwdehssagrYVSrrckplkefmLSQDVEHerlfdLIQKMLEYDPAKRITLREA 471
Cdd:cd14662 204 ----PKNFrktIQRIMSVQYKIPD------------YVR----------VSQDCRH-----LLSRIFVANPAKRITIPEI 252

                ....*
gi 67551261 472 LKHPF 476
Cdd:cd14662 253 KNHPW 257
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
167-380 4.78e-12

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: 66.02  E-value: 4.78e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIdHKAGGRHVAVKIV-------KNVDRY---CEAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHGH 236
Cdd:cd06628   8 IGSGSFGSVYLGM-NASSGELMAVKQVelpsvsaENKDRKksmLDALQREIALLRELQ--HEN----IVQYLGSSSDANH 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELL-GLSTYDFIKENGFLPFRLdhIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteaynpkikrDERT 315
Cdd:cd06628  81 LNIFLEYVpGGSVATLLNNYGAFEESL--VRNFVRQILKGLNYLHNRGIIHRDIKGANILV---------------DNKG 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 67551261 316 linpDIKVVDFGsATYDDEHHSTLVSTRHYR----------APEVILALGWSQPCDVWSIGCILIEYYLGFTVFP 380
Cdd:cd06628 144 ----GIKISDFG-ISKKLEANSLSTKNNGARpslqgsvfwmAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFP 213
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
162-393 5.56e-12

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: 65.77  E-value: 5.56e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 162 EIVDTLGEGAFGKVVeCIDHKagGRHVAVKIVKNvDRYCEAARSEIQVLEHLNTTDpnstfrCVQMLEWF-EHHGHICIV 240
Cdd:cd05082   9 KLLQTIGKGEFGDVM-LGDYR--GNKVAVKCIKN-DATAQAFLAEASVMTQLRHSN------LVQLLGVIvEEKGGLYIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 241 FELLGL-STYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYTeaynpkikrdertlinp 319
Cdd:cd05082  79 TEYMAKgSLVDYLRSRGRSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVA----------------- 141
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 67551261 320 diKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYY-LGFTVFPTHDSKEHLAMMER 393
Cdd:cd05082 142 --KVSDFGLTKEASSTQDTGKLPVKWTAPEALREKKFSTKSDVWSFGILLWEIYsFGRVPYPRIPLKDVVPRVEK 214
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
161-477 5.58e-12

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: 65.74  E-value: 5.58e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKV--VECIDHKA--------GGRHVAVKIVKNVDRyceaarsEIQVLEHLNttdpnSTFrCVQMLEW 230
Cdd:cd05578   2 FQILRVIGKGSFGKVciVQKKDTKKmfamkymnKQKCIEKDSVRNVLN-------ELEILQELE-----HPF-LVNLWYS 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 231 FEHHGHICIVFELL--GLSTYDFIKEngfLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpk 308
Cdd:cd05578  69 FQDEEDMYMVVDLLlgGDLRYHLQQK---VKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGH------- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 309 ikrdertlinpdIKVVDFGSATY--DDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKe 386
Cdd:cd05578 139 ------------VHITDFNIATKltDGTLATSTSGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEIHSRT- 205
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 387 hlaMMERILgplpkHMIQKtrkrkyfhHDRLDWDEHSSAGRyvsrrckplkefmlsqdveherlfDLIQKMLEYDPAKRI 466
Cdd:cd05578 206 ---SIEEIR-----AKFET--------ASVLYPAGWSEEAI------------------------DLINKLLERDPQKRL 245
                       330
                ....*....|..
gi 67551261 467 -TLREALKHPFF 477
Cdd:cd05578 246 gDLSDLKNHPYF 257
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
161-477 5.74e-12

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: 66.03  E-value: 5.74e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVEcIDHKAGGRHVAVKIVkNVDRYCEAAR----SEIQVLEHLNttDPNstfrCVQMLEWF--EHH 234
Cdd:cd08217   2 YEVLETIGKGSFGTVRK-VRRKSDGKILVWKEI-DYGKMSEKEKqqlvSEVNILRELK--HPN----IVRYYDRIvdRAN 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 235 GHICIVFELLG---LSTY--DFIKENGFLPfrLDHIRKMAYQICKSVNFLH-----SNKLTHTDLKPENIlFVQSDYTea 304
Cdd:cd08217  74 TTLYIVMEYCEggdLAQLikKCKKENQYIP--EEFIWKIFTQLLLALYECHnrsvgGGKILHRDLKPANI-FLDSDNN-- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 305 ynpkikrdertlinpdIKVVDFGSATYDDEHHS---TLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFpt 381
Cdd:cd08217 149 ----------------VKLGDFGLARVLSHDSSfakTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPF-- 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 382 hDSKEHLAMMERI-LGPLPkhmiqktrkrkyfhhdrlDWDEHSSagryvsrrckplkefmlsqdvehERLFDLIQKMLEY 460
Cdd:cd08217 211 -QAANQLELAKKIkEGKFP------------------RIPSRYS-----------------------SELNEVIKSMLNV 248
                       330
                ....*....|....*..
gi 67551261 461 DPAKRITLREALKHPFF 477
Cdd:cd08217 249 DPDKRPSVEELLQLPLI 265
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
160-476 6.30e-12

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: 66.04  E-value: 6.30e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDhKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTdpnstfRCVQMLEWFEHHGHICI 239
Cdd:cd14104   1 KYMIAEELGRGQFGIVHRCVE-TSSKKTYMAKFVKVKGADQVLVKKEISILNIARHR------NILRLHESFESHEELVM 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 240 VFELLglSTYDFIKENGFLPFRLDHIRKMAY--QICKSVNFLHSNKLTHTDLKPENILFVqsdyteaynpkikrderTLI 317
Cdd:cd14104  74 IFEFI--SGVDIFERITTARFELNEREIVSYvrQVCEALEFLHSKNIGHFDIRPENIIYC-----------------TRR 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 318 NPDIKVVDFGSATY--DDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFpthdskehlammeriL 395
Cdd:cd14104 135 GSYIKIIEFGQSRQlkPGDKFRLQYTSAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPF---------------E 199
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 396 GPLPKHMIQKTRKrkyfhhdrLDWDEHSSAGRYVSRRCkplkefmlsqdveherlFDLIQKMLEYDPAKRITLREALKHP 475
Cdd:cd14104 200 AETNQQTIENIRN--------AEYAFDDEAFKNISIEA-----------------LDFVDRLLVKERKSRMTAQEALNHP 254

                .
gi 67551261 476 F 476
Cdd:cd14104 255 W 255
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
167-477 7.01e-12

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: 65.54  E-value: 7.01e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVveCIDH-KAGGRHVAVK---IVKNVDRycEAARSEIQVL---EHLNTTDPNSTFRCVQMLeWfehhghicI 239
Cdd:cd06648  15 IGEGSTGIV--CIATdKSTGRQVAVKkmdLRKQQRR--ELLFNEVVIMrdyQHPNIVEMYSSYLVGDEL-W--------V 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 240 VFELL-GLSTYDFIKENgflpfRLD--HIRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqsdyteaynpkIKRDERtl 316
Cdd:cd06648  82 VMEFLeGGALTDIVTHT-----RMNeeQIATVCRAVLKALSFLHSQGVIHRDIKSDSIL-------------LTSDGR-- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 317 inpdIKVVDFG---SATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGftvFPTHDSKEHLAMMER 393
Cdd:cd06648 142 ----VKLSDFGfcaQVSKEVPRRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDG---EPPYFNEPPLQAMKR 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 394 ILGPLPKHMiqktrkrKYFHHdrldwdehssagryVSrrckplkefmlsqdvehERLFDLIQKMLEYDPAKRITLREALK 473
Cdd:cd06648 215 IRDNEPPKL-------KNLHK--------------VS-----------------PRLRSFLDRMLVRDPAQRATAAELLN 256

                ....
gi 67551261 474 HPFF 477
Cdd:cd06648 257 HPFL 260
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
161-477 8.39e-12

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: 65.30  E-value: 8.39e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGkVVECIDHKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLnttdpnSTFRCVQMLEWFEHHGHICIV 240
Cdd:cd14107   4 YEVKEEIGRGTFG-FVKRVTHKGNGECCAAKFIPLRSSTRARAFQERDILARL------SHRRLTCLLDQFETRKTLILI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 241 FELLGL-STYDFIKENGFLPFRldHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSdyteaynpkikrdERTlinp 319
Cdd:cd14107  77 LELCSSeELLDRLFLKGVVTEA--EVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSP-------------TRE---- 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 320 DIKVVDFGSATYDD--EHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILieyYLGFTVFPTHDSKEHLAMMERILgp 397
Cdd:cd14107 138 DIKICDFGFAQEITpsEHQFSKYGSPEFVAPEIVHQEPVSAATDIWALGVIA---YLSLTCHSPFAGENDRATLLNVA-- 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 398 lpkhmiqktrkrkyfhHDRLDWDEHSSAGRyvsrrckplkefmlSQDVEherlfDLIQKMLEYDPAKRITLREALKHPFF 477
Cdd:cd14107 213 ----------------EGVVSWDTPEITHL--------------SEDAK-----DFIKRVLQPDPEKRPSASECLSHEWF 257
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
238-479 9.51e-12

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: 65.73  E-value: 9.51e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 238 CIVFELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDytEAYnpkikrdertli 317
Cdd:cd14020  85 CLLLELLDVSVSELLLRSSNQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAED--ECF------------ 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 318 npdiKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQ-----------PCDVWSIGCILIEYYLGFTVFPTHDSKE 386
Cdd:cd14020 151 ----KLIDFGLSFKEGNQDVKYIQTDGYRAPEAELQNCLAQaglqsetectsAVDLWSLGIVLLEMFSGMKLKHTVRSQE 226
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 387 hlammerilgplpkhmiqktrkrkyfhhdrldWDEHSSA--GRYVSrrckplKEFMLSQDVEHERLFDLIQKMLEYDPAK 464
Cdd:cd14020 227 --------------------------------WKDNSSAiiDHIFA------SNAVVNPAIPAYHLRDLIKSMLHNDPGK 268
                       250
                ....*....|....*
gi 67551261 465 RITLREALKHPFFDL 479
Cdd:cd14020 269 RATAEAALCSPFFSI 283
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
167-476 9.87e-12

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: 64.98  E-value: 9.87e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIdHKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTdpnstfRCVQMLEWFEHHGHICIVFELLgl 246
Cdd:cd14115   1 IGRGRFSIVKKCL-HKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHP------QYITLHDTYESPTSYILVLELM-- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 247 stydfikENG-FLPFRLDHIR----KMAY---QICKSVNFLHSNKLTHTDLKPENILfvqsdyteaynpkikRDERTLIn 318
Cdd:cd14115  72 -------DDGrLLDYLMNHDElmeeKVAFyirDIMEALQYLHNCRVAHLDIKPENLL---------------IDLRIPV- 128
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 319 PDIKVVDFGSATYDDEHHST--LVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMMERILG 396
Cdd:cd14115 129 PRVKLIDLEDAVQISGHRHVhhLLGNPEFAAPEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDF 208
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 397 PLPKhmiqktrkrKYFhhdrldwDEHSSAGRyvsrrckplkefmlsqdveherlfDLIQKMLEYDPAKRITLREALKHPF 476
Cdd:cd14115 209 SFPD---------EYF-------GDVSQAAR------------------------DFINVILQEDPRRRPTAATCLQHPW 248
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
167-477 9.97e-12

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: 64.97  E-value: 9.97e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIDHKAGGRhVAVKIVK------------NVdryceaaRSEIQVLEHLNttDPNstfrCVQMLEWFEHH 234
Cdd:cd14119   1 LGEGSYGKVKEVLDTETLCR-RAVKILKkrklrripngeaNV-------KREIQILRRLN--HRN----VIKLVDVLYNE 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 235 --GHICIVFELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteaynpkiKRD 312
Cdd:cd14119  67 ekQKLYMVMEYCVGGLQEMLDSAPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLL-------------TTD 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 313 ERtlinpdIKVVDFGSATY-----DDEHHSTLVSTRHYRAPEVILALG-WSQP-CDVWSIGCILieYYLGFTVFPthdsk 385
Cdd:cd14119 134 GT------LKISDFGVAEAldlfaEDDTCTTSQGSPAFQPPEIANGQDsFSGFkVDIWSAGVTL--YNMTTGKYP----- 200
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 386 ehlammerilgplpkhmiqktrkrkyFHHDRLdWDEHSSAGRyvsrrckplKEFMLSQDVEhERLFDLIQKMLEYDPAKR 465
Cdd:cd14119 201 --------------------------FEGDNI-YKLFENIGK---------GEYTIPDDVD-PDLQDLLRGMLEKDPEKR 243
                       330
                ....*....|..
gi 67551261 466 ITLREALKHPFF 477
Cdd:cd14119 244 FTIEQIRQHPWF 255
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
167-476 2.00e-11

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: 64.38  E-value: 2.00e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVveCIDHKAGGRHVAVKIVKNVDRYCEAARSEIQVLEhlnttdpnstfRCVQMLEWFEHH-----------G 235
Cdd:cd06631   9 LGKGAYGTV--YCGLTSTGQLIAVKQVELDTSDKEKAEKEYEKLQ-----------EEVDLLKTLKHVnivgylgtcleD 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 236 HICIVF-ELL-GLSTYDFIKENGFLPFRLdhIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQsdyteaynpkikrde 313
Cdd:cd06631  76 NVVSIFmEFVpGGSIASILARFGALEEPV--FCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMP--------------- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 314 rtliNPDIKVVDFGSA---TYDDEH--HSTLVSTRH----YRAPEVILALGWSQPCDVWSIGCilieyylgfTVFPTHDS 384
Cdd:cd06631 139 ----NGVIKLIDFGCAkrlCINLSSgsQSQLLKSMRgtpyWMAPEVINETGHGRKSDIWSIGC---------TVFEMATG 205
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 385 KEHLAMMERIlgplpkhmiqktrkrkyfhhdrldwdehsSAGRYVSRRCKPLKEfmLSQDVEHERLfDLIQKMLEYDPAK 464
Cdd:cd06631 206 KPPWADMNPM-----------------------------AAIFAIGSGRKPVPR--LPDKFSPEAR-DFVHACLTRDQDE 253
                       330
                ....*....|..
gi 67551261 465 RITLREALKHPF 476
Cdd:cd06631 254 RPSAEQLLKHPF 265
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
161-409 2.16e-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: 65.05  E-value: 2.16e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVeCIDHKAGGRHVAVKIVKnvdRYCEAARSEIQVLEHLNTTDPNSTFRCVQMLEW-FEHHGHICI 239
Cdd:cd05594  27 FEYLKLLGKGTFGKVI-LVKEKATGRYYAMKILK---KEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYsFQTHDRLCF 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 240 VFELL--GLSTYDFIKENgflPFRLDHIRKMAYQICKSVNFLHSNK-LTHTDLKPENILFVQSDYteaynpkikrdertl 316
Cdd:cd05594 103 VMEYAngGELFFHLSRER---VFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGH--------------- 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 317 inpdIKVVDFG---SATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKE--HLAMM 391
Cdd:cd05594 165 ----IKITDFGlckEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKlfELILM 240
                       250       260
                ....*....|....*....|...
gi 67551261 392 E-----RILGPLPKHMIQKTRKR 409
Cdd:cd05594 241 EeirfpRTLSPEAKSLLSGLLKK 263
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
167-398 2.34e-11

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: 64.17  E-value: 2.34e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECidhKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTDPNSTFRCV-QMLEWFEHHGHICIVF---- 241
Cdd:cd14000   2 LGDGGFGSVYRA---SYKGEPVAVKIFNKHTSSNFANVPADTMLRHLRATDAMKNFRLLrQELTVLSHLHHPSIVYllgi 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 242 ---------ELLGLSTYD-FIKENGFLPFRLDHI--RKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYTEAYNpki 309
Cdd:cd14000  79 gihplmlvlELAPLGSLDhLLQQDSRSFASLGRTlqQRIALQVADGLRYLHSAMIIYRDLKSHNVLVWTLYPNSAII--- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 310 krdertlinpdIKVVDFGSATYD-DEHHSTLVSTRHYRAPEVI-LALGWSQPCDVWSIGCILIEYYLGFTVFPTHDS-KE 386
Cdd:cd14000 156 -----------IKIADYGISRQCcRMGAKGSEGTPGFRAPEIArGNVIYNEKVDVFSFGMLLYEILSGGAPMVGHLKfPN 224
                       250
                ....*....|..
gi 67551261 387 HLAMMERILGPL 398
Cdd:cd14000 225 EFDIHGGLRPPL 236
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
261-476 2.69e-11

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: 63.82  E-value: 2.69e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 261 RLDHIRKMAY--QICKSVNFLHSNKLTHTDLKPENILFVQsdyteaynpkikrdertliNPDIKVVDFG-SATYDDEHHS 337
Cdd:cd14116 101 KFDEQRTATYitELANALSYCHSKRVIHRDIKPENLLLGS-------------------AGELKIADFGwSVHAPSSRRT 161
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 338 TLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMMERILGPLPKHMIQKTRkrkyfhhdrl 417
Cdd:cd14116 162 TLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGAR---------- 231
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 67551261 418 dwdehssagryvsrrckplkefmlsqdveherlfDLIQKMLEYDPAKRITLREALKHPF 476
Cdd:cd14116 232 ----------------------------------DLISRLLKHNPSQRPMLREVLEHPW 256
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
160-477 2.77e-11

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: 63.79  E-value: 2.77e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDhKAGGRHVAVKIVKNVDR-YCEAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHGHIC 238
Cdd:cd06647   8 KYTRFEKIGQGASGTVYTAID-VATGQEVAIKQMNLQQQpKKELIINEILVMRENK--NPN----IVNYLDSYLVGDELW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 239 IVFELL-GLSTYDFIKENgflpfRLD--HIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVqsdyteaynpkikrdert 315
Cdd:cd06647  81 VVMEYLaGGSLTDVVTET-----CMDegQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLG------------------ 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 316 lINPDIKVVDFG---SATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGftvfpthdskEHLAMME 392
Cdd:cd06647 138 -MDGSVKLTDFGfcaQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEG----------EPPYLNE 206
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 393 RILGPLpkHMIQKTRKRKYFHHDRLdwdehSSAGRyvsrrckplkefmlsqdveherlfDLIQKMLEYDPAKRITLREAL 472
Cdd:cd06647 207 NPLRAL--YLIATNGTPELQNPEKL-----SAIFR------------------------DFLNRCLEMDVEKRGSAKELL 255

                ....*
gi 67551261 473 KHPFF 477
Cdd:cd06647 256 QHPFL 260
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
161-454 2.89e-11

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: 64.38  E-value: 2.89e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECiDHKAGGRHVAVKIVKNVD----RYCEAARSEIQVLEHLNttdpnSTFrcVQMLEWFEH-HG 235
Cdd:cd05612   3 FERIKTIGTGTFGRVHLV-RDRISEHYYALKVMAIPEvirlKQEQHVHNEKRVLKEVS-----HPF--IIRLFWTEHdQR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 236 HICIVFELL-GLSTYDFIKENGflPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqsdyteaynpkIKRDER 314
Cdd:cd05612  75 FLYMLMEYVpGGELFSYLRNSG--RFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENIL-------------LDKEGH 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 315 tlinpdIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGftvFPTHDSKEHLAMMERI 394
Cdd:cd05612 140 ------IKLTDFGFAKKLRDRTWTLCGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVG---YPPFFDDNPFGIYEKI 210
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 67551261 395 L-GPL--PKHM--IQKTRKRKYFHHDRldwdehssagryvSRRCKPLKEFmlSQDVEHERLFDLI 454
Cdd:cd05612 211 LaGKLefPRHLdlYAKDLIKKLLVVDR-------------TRRLGNMKNG--ADDVKNHRWFKSV 260
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
160-380 3.16e-11

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


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 64.05  E-value: 3.16e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVEC----IDHKAGGRHVAVKIVKNVDRYCE--AARSEIQVL----EHLNTTdpNSTFRCVQmle 229
Cdd:cd05054   8 RLKLGKPLGRGAFGKVIQAsafgIDKSATCRTVAVKMLKEGATASEhkALMTELKILihigHHLNVV--NLLGACTK--- 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 230 wfeHHGHICIVFELL---GLSTYDFIKENGFLPFR----------------------LDHIRKMAYQICKSVNFLHSNKL 284
Cdd:cd05054  83 ---PGGPLMVIVEFCkfgNLSNYLRSKREEFVPYRdkgardveeeedddelykepltLEDLICYSFQVARGMEFLASRKC 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 285 THTDLKPENILFVQsdyteaynpkikrdertliNPDIKVVDFGSA--TYDDEHHSTLVSTR---HYRAPEVILALGWSQP 359
Cdd:cd05054 160 IHRDLAARNILLSE-------------------NNVVKICDFGLArdIYKDPDYVRKGDARlplKWMAPESIFDKVYTTQ 220
                       250       260
                ....*....|....*....|..
gi 67551261 360 CDVWSIGCILIEYY-LGFTVFP 380
Cdd:cd05054 221 SDVWSFGVLLWEIFsLGASPYP 242
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
160-371 3.34e-11

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: 63.58  E-value: 3.34e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDT-----LGEGAFGKVVECIDHKAGGRhVAVK-IVKNVDRYCEAARSEIQV---LEHLNTtdpnstfrcVQMLEW 230
Cdd:cd06624   4 EYEYDESgervvLGKGTFGVVYAARDLSTQVR-IAIKeIPERDSREVQPLHEEIALhsrLSHKNI---------VQYLGS 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 231 FEHHGHICIVFELL-GLSTYDFIKEN-GFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqSDYTEAynpk 308
Cdd:cd06624  74 VSEDGFFKIFMEQVpGGSLSALLRSKwGPLKDNENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLV--NTYSGV---- 147
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 67551261 309 ikrdertlinpdIKVVDFGSA---------TyddehhSTLVSTRHYRAPEVILA--LGWSQPCDVWSIGCILIE 371
Cdd:cd06624 148 ------------VKISDFGTSkrlaginpcT------ETFTGTLQYMAPEVIDKgqRGYGPPADIWSLGCTIIE 203
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
154-371 3.40e-11

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 65.20  E-value: 3.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  154 GDVLSARYEIVDTLGEGAFGKVvecidHKAG----GRHVAVKIVKN--------VDRY-CEA---ARseiqvLEHlnttd 217
Cdd:NF033483   2 GKLLGGRYEIGERIGRGGMAEV-----YLAKdtrlDRDVAVKVLRPdlardpefVARFrREAqsaAS-----LSH----- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  218 PNstfrCVQMLEWFEHHGHICIVFELL-GLSTYDFIKENGFLPFRlDHIRKMAyQICKSVNFLHSNKLTHTDLKPENIlf 296
Cdd:NF033483  67 PN----IVSVYDVGEDGGIPYIVMEYVdGRTLKDYIREHGPLSPE-EAVEIMI-QILSALEHAHRNGIVHRDIKPQNI-- 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  297 vqsdyteaynpkikrdertLINPD--IKVVDFG------SATYDdeHHSTLVSTRHYRAPEvilalgwsQ----PC---- 360
Cdd:NF033483 139 -------------------LITKDgrVKVTDFGiaralsSTTMT--QTNSVLGTVHYLSPE--------QarggTVdars 189
                        250
                 ....*....|.
gi 67551261  361 DVWSIGCILIE 371
Cdd:NF033483 190 DIYSLGIVLYE 200
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
161-385 4.01e-11

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: 63.28  E-value: 4.01e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVEcIDHKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLN-------------------TTDPNST 221
Cdd:cd14047   8 FKEIELIGSGGFGQVFK-AKHRIDGKTYAIKRVKLNNEKAEREVKALAKLDHPNivryngcwdgfdydpetssSNSSRSK 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 222 FRC--VQMlEWFEhhghicivfellGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQS 299
Cdd:cd14047  87 TKClfIQM-EFCE------------KGTLESWIEKRNGEKLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDT 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 300 DyteaynpkikrdertlinpDIKVVDFG--SATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYylgFT 377
Cdd:cd14047 154 G-------------------KVKIGDFGlvTSLKNDGKRTKSKGTLSYMSPEQISSQDYGKEVDIYALGLILFEL---LH 211

                ....*...
gi 67551261 378 VFPTHDSK 385
Cdd:cd14047 212 VCDSAFEK 219
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
167-371 4.09e-11

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: 63.18  E-value: 4.09e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVvecidHKA--GGRHVAVKIVKnVDRYCEAARSEIQV---------LEHLNTTdpnsTFR--CVQmlewfeh 233
Cdd:cd14061   2 IGVGGFGKV-----YRGiwRGEEVAVKAAR-QDPDEDISVTLENVrqearlfwmLRHPNII----ALRgvCLQ------- 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 234 HGHICIVFELLGLSTYDFIKENGFLPfrLDHIRKMAYQICKSVNFLHSNK---LTHTDLKPENILFVqsdytEAYNpkik 310
Cdd:cd14061  65 PPNLCLVMEYARGGALNRVLAGRKIP--PHVLVDWAIQIARGMNYLHNEApvpIIHRDLKSSNILIL-----EAIE---- 133
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 67551261 311 rdERTLINPDIKVVDFGSATydDEHHSTLVS---TRHYRAPEVILALGWSQPCDVWSIGCILIE 371
Cdd:cd14061 134 --NEDLENKTLKITDFGLAR--EWHKTTRMSaagTYAWMAPEVIKSSTFSKASDVWSYGVLLWE 193
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
160-481 4.11e-11

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: 63.97  E-value: 4.11e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDhKAGGRHVAVKIVkNVDRYCEAARSEIQVLEHLNTTDPNstfrCVQMLEWFEHHGHICI 239
Cdd:cd06656  20 KYTRFEKIGQGASGTVYTAID-IATGQEVAIKQM-NLQQQPKKELIINEILVMRENKNPN----IVNYLDSYLVGDELWV 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 240 VFELL-GLSTYDFIKENGFlpfRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVqsdyteaynpkikrdertlIN 318
Cdd:cd06656  94 VMEYLaGGSLTDVVTETCM---DEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLG-------------------MD 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 319 PDIKVVDFG---SATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGftvfpthdskEHLAMMERIL 395
Cdd:cd06656 152 GSVKLTDFGfcaQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEG----------EPPYLNENPL 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 396 GPLpkHMIQKTRKRKYFHHDRLdwdehSSAGRyvsrrckplkefmlsqdveherlfDLIQKMLEYDPAKRITLREALKHP 475
Cdd:cd06656 222 RAL--YLIATNGTPELQNPERL-----SAVFR------------------------DFLNRCLEMDVDRRGSAKELLQHP 270

                ....*.
gi 67551261 476 FFDLLK 481
Cdd:cd06656 271 FLKLAK 276
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
162-476 4.68e-11

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 64.07  E-value: 4.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  162 EIVDTLGEGAFGKVVECIdHKAGGRHVAVKIV-KNVDrycEAARSEI-QVLEHLNTTDPNSTFRCVQMlewFEHHGHICI 239
Cdd:PLN00034  77 ERVNRIGSGAGGTVYKVI-HRPTGRLYALKVIyGNHE---DTVRRQIcREIEILRDVNHPNVVKCHDM---FDHNGEIQV 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  240 VFELLGLSTYD--FIKENGFLPfrldhirKMAYQICKSVNFLHSNKLTHTDLKPENIlfvqsdyteaynpkikrdertLI 317
Cdd:PLN00034 150 LLEFMDGGSLEgtHIADEQFLA-------DVARQILSGIAYLHRRHIVHRDIKPSNL---------------------LI 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  318 NP--DIKVVDFG-----SATYDDEHHStlVSTRHYRAPEVI---LALGWSQPC--DVWSIGCILIEYYLGFTVFPTHDSK 385
Cdd:PLN00034 202 NSakNVKIADFGvsrilAQTMDPCNSS--VGTIAYMSPERIntdLNHGAYDGYagDIWSLGVSILEFYLGRFPFGVGRQG 279
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  386 EHLAMMERILGPLPkhmiqktrkrkyfhhdrldwdehSSAGRYVSRrckplkEFMlsqdveherlfDLIQKMLEYDPAKR 465
Cdd:PLN00034 280 DWASLMCAICMSQP-----------------------PEAPATASR------EFR-----------HFISCCLQREPAKR 319
                        330
                 ....*....|.
gi 67551261  466 ITLREALKHPF 476
Cdd:PLN00034 320 WSAMQLLQHPF 330
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
167-477 4.81e-11

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: 63.47  E-value: 4.81e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVveCI-DHKAGGRHVAVKIV---KNVDRycEAARSEIQVL---EHLNTtdpnstfrcVQMLEWFEHHGHICI 239
Cdd:cd06659  29 IGEGSTGVV--CIaREKHSGRQVAVKMMdlrKQQRR--ELLFNEVVIMrdyQHPNV---------VEMYKSYLVGEELWV 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 240 VFELL-GLSTYDFIKENgflpfRL--DHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVqsdyteaynpkikrdertl 316
Cdd:cd06659  96 LMEYLqGGALTDIVSQT-----RLneEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLT------------------- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 317 INPDIKVVDFG---SATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGftvFPTHDSKEHLAMMER 393
Cdd:cd06659 152 LDGRVKLSDFGfcaQISKDVPKRKSLVGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDG---EPPYFSDSPVQAMKR 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 394 ILGPLPKhmiqktrKRKYFHhdrldwdehssagryvsrRCKPLkefmlsqdveherLFDLIQKMLEYDPAKRITLREALK 473
Cdd:cd06659 229 LRDSPPP-------KLKNSH------------------KASPV-------------LRDFLERMLVRDPQERATAQELLD 270

                ....
gi 67551261 474 HPFF 477
Cdd:cd06659 271 HPFL 274
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
160-476 5.04e-11

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: 62.84  E-value: 5.04e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECiDHKAGGRHVAVK---IVKNVDRYCEAARSEIQVLEHLNttDPNstfrCVQMLEWFE-HHG 235
Cdd:cd08223   1 EYQFLRVIGKGSYGEVWLV-RHKRDRKQYVIKklnLKNASKRERKAAEQEAKLLSKLK--HPN----IVSYKESFEgEDG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 236 HICIVFELL-GLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrder 314
Cdd:cd08223  74 FLYIVMGFCeGGDLYTRLKEQKGVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNI------------- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 315 tlinpdIKVVDFGSATYDDEHH---STLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYlgfTVFPTHDSKEHLAMM 391
Cdd:cd08223 141 ------IKVGDLGIARVLESSSdmaTTLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMA---TLKHAFNAKDMNSLV 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 392 ERIL-GPLPKhmiqktRKRKYfhhdrldwdehssagryvsrrckplkefmlsqdveHERLFDLIQKMLEYDPAKRITLRE 470
Cdd:cd08223 212 YKILeGKLPP------MPKQY-----------------------------------SPELGELIKAMLHQDPEKRPSVKR 250

                ....*.
gi 67551261 471 ALKHPF 476
Cdd:cd08223 251 ILRQPY 256
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
161-376 5.17e-11

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: 63.30  E-value: 5.17e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVEcIDHKAGGRHVAVK---IVKNVDRYCEAARSEIQVL---EHLNTTDPNSTfrcvqmleWFEH- 233
Cdd:cd14049   8 FEEIARLGKGGYGKVYK-VRNKLDGQYYAIKkilIKKVTKRDCMKVLREVKVLaglQHPNIVGYHTA--------WMEHv 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 234 HGHICIVFELLGLSTYDFI------------KENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDY 301
Cdd:cd14049  79 QLMLYIQMQLCELSLWDWIvernkrpceeefKSAPYTPVDVDVTTKILQQLLEGVTYIHSMGIVHRDLKPRNIFLHGSDI 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 67551261 302 teaynpKIKRDERTLINPDIKVVDFGSATYDDE---HHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGF 376
Cdd:cd14049 159 ------HVRIGDFGLACPDILQDGNDSTTMSRLnglTHTSGVGTCLYAAPEQLEGSHYDFKSDMYSIGVILLELFQPF 230
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
166-385 5.64e-11

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: 63.38  E-value: 5.64e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 166 TLGEGAFGKVVeCIDHKAGGRHVAVKIV--KNVDRYC--EAARSEIQVLEHLNttdpnSTFrCVQMLEWFEHHGHICIVF 241
Cdd:cd05607   9 VLGKGGFGEVC-AVQVKNTGQMYACKKLdkKRLKKKSgeKMALLEKEILEKVN-----SPF-IVSLAYAFETKTHLCLVM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 242 ELLGLSTYDF-IKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteaynpkikrDErtliNPD 320
Cdd:cd05607  82 SLMNGGDLKYhIYNVGERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLL---------------DD----NGN 142
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 67551261 321 IKVVDFGSATYDDEHHSTL--VSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSK 385
Cdd:cd05607 143 CRLSDLGLAVEVKEGKPITqrAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRDHKEK 209
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
167-380 5.83e-11

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: 63.15  E-value: 5.83e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIdHKAGGRHVAVK-IVKNVDRyceaaRSEIQVLEHLNTTDPNStfRCVQMLEWFE---HHGHICIVFE 242
Cdd:cd06616  14 IGRGAFGTVNKML-HKPSGTIMAVKrIRSTVDE-----KEQKRLLMDLDVVMRSS--DCPYIVKFYGalfREGDCWICME 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 243 LLGLST---YDFI--KENGFLPFRLdhIRKMAYQICKSVNFLHSN-KLTHTDLKPENILfvqsdyteaynpkIKRdertl 316
Cdd:cd06616  86 LMDISLdkfYKYVyeVLDSVIPEEI--LGKIAVATVKALNYLKEElKIIHRDVKPSNIL-------------LDR----- 145
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 317 iNPDIKVVDFGSATY--DDEHHSTLVSTRHYRAPEVILALGWSQP----CDVWSIGCILIEYYLGftVFP 380
Cdd:cd06616 146 -NGNIKLCDFGISGQlvDSIAKTRDAGCRPYMAPERIDPSASRDGydvrSDVWSLGITLYEVATG--KFP 212
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
165-373 6.14e-11

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: 62.75  E-value: 6.14e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 165 DTLGEGAFGKVVECiDHKagGRHVAVKIVKNVDRYCEAARSEIQV---LEHLNTtdpnstfrcVQMLEWFEHHGHICIVF 241
Cdd:cd05039  12 ELIGKGEFGDVMLG-DYR--GQKVAVKCLKDDSTAAQAFLAEASVmttLRHPNL---------VQLLGVVLEGNGLYIVT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 242 ELLGL-STYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENIlfvqsdyteaynpkikrdertLINPD 320
Cdd:cd05039  80 EYMAKgSLVDYLRSRGRAVITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNV---------------------LVSED 138
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 67551261 321 I--KVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYY 373
Cdd:cd05039 139 NvaKVSDFGLAKEASSNQDGGKLPIKWTAPEALREKKFSTKSDVWSFGILLWEIY 193
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
160-481 8.09e-11

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: 62.82  E-value: 8.09e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDhKAGGRHVAVKIVkNVDRYC--EAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHGHI 237
Cdd:cd06655  20 KYTRYEKIGQGASGTVFTAID-VATGQEVAIKQI-NLQKQPkkELIINEILVMKELK--NPN----IVNFLDSFLVGDEL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 238 CIVFELL-GLSTYDFIKENGflpfrLD--HIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVqsdyteaynpkikrder 314
Cdd:cd06655  92 FVVMEYLaGGSLTDVVTETC-----MDeaQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLG----------------- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 315 tlINPDIKVVDFG---SATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMM 391
Cdd:cd06655 150 --MDGSVKLTDFGfcaQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 392 ERILGPlpkhMIQKTRKRKYFHHDRLDwdehssagryvsrRCkplkefmlsqdveherlfdliqkmLEYDPAKRITLREA 471
Cdd:cd06655 228 ATNGTP----ELQNPEKLSPIFRDFLN-------------RC------------------------LEMDVEKRGSAKEL 266
                       330
                ....*....|
gi 67551261 472 LKHPFFDLLK 481
Cdd:cd06655 267 LQHPFLKLAK 276
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
161-397 1.27e-10

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: 62.79  E-value: 1.27e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVeCIDHKAGGRHVAVKIVKN--VDRYCEAARS--EIQVLEhlNTTDPNSTfrcvQMLEWFEHHGH 236
Cdd:cd05593  17 FDYLKLLGKGTFGKVI-LVREKASGKYYAMKILKKevIIAKDEVAHTltESRVLK--NTRHPFLT----SLKYSFQTKDR 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELL--GLSTYDFIKENgflPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrder 314
Cdd:cd05593  90 LCFVMEYVngGELFFHLSRER---VFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGH------------- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 315 tlinpdIKVVDFG---SATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKE--HLA 389
Cdd:cd05593 154 ------IKITDFGlckEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKlfELI 227

                ....*...
gi 67551261 390 MMERILGP 397
Cdd:cd05593 228 LMEDIKFP 235
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
161-395 1.31e-10

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 62.69  E-value: 1.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  161 YEIVDTLGEGAFGKVVECIDHKAGGRHVAVK------IVKNvdRYCEAARSEIQVLEHLNTTdpnstfRCVQMLEWFEHH 234
Cdd:PTZ00426  32 FNFIRTLGTGSFGRVILATYKNEDFPPVAIKrfekskIIKQ--KQVDHVFSERKILNYINHP------FCVNLYGSFKDE 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  235 GHICIVFE-LLGLSTYDFIKENGFLPFRLDHIrkMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrde 313
Cdd:PTZ00426 104 SYLYLVLEfVIGGEFFTFLRRNKRFPNDVGCF--YAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGF------------ 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  314 rtlinpdIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGftvFPTHDSKEHLAMMER 393
Cdd:PTZ00426 170 -------IKMTDFGFAKVVDTRTYTLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVG---CPPFYANEPLLIYQK 239

                 ..
gi 67551261  394 IL 395
Cdd:PTZ00426 240 IL 241
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
158-390 1.39e-10

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: 61.92  E-value: 1.39e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 158 SARYEIVDTLGEGAFGKVVECIDHKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLnTTDPNstfrCVQMLEwfEHHGHI 237
Cdd:cd14037   2 SHHVTIEKYLAEGGFAHVYLVKTSNGGNRAALKRVYVNDEHDLNVCKREIEIMKRL-SGHKN----IVGYID--SSANRS 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 238 -CIVFELLGLstYDFIKENGFLPF---RLDH------IRKMAYQICKSVNFLHSNK--LTHTDLKPENILFVQSdyteay 305
Cdd:cd14037  75 gNGVYEVLLL--MEYCKGGGVIDLmnqRLQTglteseILKIFCDVCEAVAAMHYLKppLIHRDLKVENVLISDS------ 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 306 npkikrdertlinPDIKVVDFGSATY----------------DDEHHSTLvstrHYRAPEVI---LALGWSQPCDVWSIG 366
Cdd:cd14037 147 -------------GNYKLCDFGSATTkilppqtkqgvtyveeDIKKYTTL----QYRAPEMIdlyRGKPITEKSDIWALG 209
                       250       260
                ....*....|....*....|....
gi 67551261 367 CILieYYLGFTVFPTHDSKEhLAM 390
Cdd:cd14037 210 CLL--YKLCFYTTPFEESGQ-LAI 230
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
160-375 1.88e-10

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: 61.66  E-value: 1.88e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDhKAGGRHVAVKIVkNVDRYCEAARSEIQVLEHLNTTDPNstfrCVQMLEWFEHHGHICI 239
Cdd:cd06654  21 KYTRFEKIGQGASGTVYTAMD-VATGQEVAIRQM-NLQQQPKKELIINEILVMRENKNPN----IVNYLDSYLVGDELWV 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 240 VFELL-GLSTYDFIKENGFlpfRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVqsdyteaynpkikrdertlIN 318
Cdd:cd06654  95 VMEYLaGGSLTDVVTETCM---DEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLG-------------------MD 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 319 PDIKVVDFG---SATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLG 375
Cdd:cd06654 153 GSVKLTDFGfcaQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEG 212
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
161-476 1.96e-10

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3). PIM3 can inhibit apoptosis and promote cell survival and protein translation, therefore, it can enhance the proliferation of normal and cancer cells. Mice deficient with PIM3 show minimal effects, suggesting that PIM3 msy not be essential. Since its expression is enhanced in several cancers, it may make a good molecular target for cancer drugs. The PIM3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 61.12  E-value: 1.96e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECiDHKAGGRHVAVKIVKNvDRYCE-AARSEIQV-LEHLNTTDPNSTFRCV-QMLEWFEHHGHI 237
Cdd:cd14102   2 YQVGSVLGSGGFGTVYAG-SRIADGLPVAVKHVVK-ERVTEwGTLNGVMVpLEIVLLKKVGSGFRGViKLLDWYERPDGF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 238 CIVFEL--LGLSTYDFIKENGflPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteaynpkikrDERT 315
Cdd:cd14102  80 LIVMERpePVKDLFDFITEKG--ALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLV---------------DLRT 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 316 linPDIKVVDFGS-ATYDDEHHSTLVSTRHYRAPEVILALGW-SQPCDVWSIGCILIEYYLGFTVFPTHdskehlammER 393
Cdd:cd14102 143 ---GELKLIDFGSgALLKDTVYTDFDGTRVYSPPEWIRYHRYhGRSATVWSLGVLLYDMVCGDIPFEQD---------EE 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 394 ILgplpkhmiqktRKRKYFHhdrldwdehssagRYVSRRCKplkefmlsqdveherlfDLIQKMLEYDPAKRITLREALK 473
Cdd:cd14102 211 IL-----------RGRLYFR-------------RRVSPECQ-----------------QLIKWCLSLRPSDRPTLEQIFD 249

                ...
gi 67551261 474 HPF 476
Cdd:cd14102 250 HPW 252
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
161-474 2.01e-10

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: 61.43  E-value: 2.01e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVEcidhkaggrhvavkiVKNVDRYCEAARSEIQVLEhlNTTDPNSTFRCVQMLEWFEHHG----- 235
Cdd:cd14048   8 FEPIQCLGRGGFGVVFE---------------AKNKVDDCNYAVKRIRLPN--NELAREKVLREVRALAKLDHPGivryf 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 236 ------------------HICIVFELLGLSTY-DFIKENGFLPFRLDHIRKMAY-QICKSVNFLHSNKLTHTDLKPENIL 295
Cdd:cd14048  71 nawlerppegwqekmdevYLYIQMQLCRKENLkDWMNRRCTMESRELFVCLNIFkQIASAVEYLHSKGLIHRDLKPSNVF 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 296 FVQSDYteaynpkikrdertlinpdIKVVDFGSATYDDE---------------HHSTLVSTRHYRAPEVILALGWSQPC 360
Cdd:cd14048 151 FSLDDV-------------------VKVGDFGLVTAMDQgepeqtvltpmpayaKHTGQVGTRLYMSPEQIHGNQYSEKV 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 361 DVWSIGCILIEYYLGFTvfpthdskehlAMMERIlgplpkHMIQKTRKRKYfhhdrldwdehssagryvsrrckPLkefM 440
Cdd:cd14048 212 DIFALGLILFELIYSFS-----------TQMERI------RTLTDVRKLKF-----------------------PA---L 248
                       330       340       350
                ....*....|....*....|....*....|....
gi 67551261 441 LSQDVEHERlfDLIQKMLEYDPAKRITLREALKH 474
Cdd:cd14048 249 FTNKYPEER--DMVQQMLSPSPSERPEAHEVIEH 280
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
160-391 2.02e-10

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: 61.34  E-value: 2.02e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVdtlGEGAFGKVVECIdHKAGGRHVAVKIVkNVDR---YCEAARSEIQVLEHLNTTDPNSTFRcvqmlewfeHHG- 235
Cdd:cd06917   5 RLELV---GRGSYGAVYRGY-HVKTGRVVALKVL-NLDTdddDVSDIQKEVALLSQLKLGQPKNIIK---------YYGs 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 236 -----HICIVFELL-GLSTYDFIKENgflPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDyteaynpki 309
Cdd:cd06917  71 ylkgpSLWIIMDYCeGGSIRTLMRAG---PIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTG--------- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 310 krdertlinpDIKVVDFGSAT---YDDEHHSTLVSTRHYRAPEVIL-ALGWSQPCDVWSIGCILIEYYLGFTvfPTHDSK 385
Cdd:cd06917 139 ----------NVKLCDFGVAAslnQNSSKRSTFVGTPYWMAPEVITeGKYYDTKADIWSLGITTYEMATGNP--PYSDVD 206

                ....*.
gi 67551261 386 EHLAMM 391
Cdd:cd06917 207 ALRAVM 212
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
167-375 2.51e-10

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: 60.59  E-value: 2.51e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIDHkagGRHVAVKIVKnvdrycEAARSEIQVLEHLNttDPNS-TFR--CVQMLEWfehhghiCIVFEL 243
Cdd:cd14059   1 LGSGAQGAVFLGKFR---GEEVAVKKVR------DEKETDIKHLRKLN--HPNIiKFKgvCTQAPCY-------CILMEY 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 244 LGLST-YDFIKENGFLPFRLdhIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrdertlinpdIK 322
Cdd:cd14059  63 CPYGQlYEVLRAGREITPSL--LVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDV-------------------LK 121
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 67551261 323 VVDFGSATYDDEHHS--TLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLG 375
Cdd:cd14059 122 ISDFGTSKELSEKSTkmSFAGTVAWMAPEVIRNEPCSEKVDIWSFGVVLWELLTG 176
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
161-371 3.06e-10

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: 61.18  E-value: 3.06e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVEcidhkagGRHV------AVKIVKNVDRYCEAARSEIQVLEHLNTTDPNSTFRCVQMLEWFE-H 233
Cdd:cd06636  18 FELVEVVGNGTYGQVYK-------GRHVktgqlaAIKVMDVTEDEEEEIKLEINMLKKYSHHRNIATYYGAFIKKSPPgH 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 234 HGHICIVFELLGL-STYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQsdyteaynpkikrd 312
Cdd:cd06636  91 DDQLWLVMEFCGAgSVTDLVKNTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTE-------------- 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 67551261 313 ertliNPDIKVVDFG-SATYDDE--HHSTLVSTRHYRAPEVILA-----LGWSQPCDVWSIGCILIE 371
Cdd:cd06636 157 -----NAEVKLVDFGvSAQLDRTvgRRNTFIGTPYWMAPEVIACdenpdATYDYRSDIWSLGITAIE 218
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
161-375 3.06e-10

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: 60.86  E-value: 3.06e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIDHKAGgRHVAVKIV--KNVDRYCEAARSEIQVLEHLNTtdPNSTfrcvQMLEWFEHHGHIC 238
Cdd:cd06641   6 FTKLEKIGKGSFGEVFKGIDNRTQ-KVVAIKIIdlEEAEDEIEDIQQEITVLSQCDS--PYVT----KYYGSYLKDTKLW 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 239 IVFELLGLSTYDFIKENGflPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqSDYTEaynpkikrdertlin 318
Cdd:cd06641  79 IIMEYLGGGSALDLLEPG--PLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLL--SEHGE--------------- 139
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 319 pdIKVVDFGSA---TYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLG 375
Cdd:cd06641 140 --VKLADFGVAgqlTDTQIKRN*FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARG 197
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
167-484 3.24e-10

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: 61.22  E-value: 3.24e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECiDHKAGGRHVAVKIVKN---VDRYcEAARS--EIQVLEhlNTTDPNSTfrcvQMLEWFEHHGHICIVF 241
Cdd:cd05571   3 LGKGTFGKVILC-REKATGELYAIKILKKeviIAKD-EVAHTltENRVLQ--NTRHPFLT----SLKYSFQTNDRLCFVM 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 242 ELLglstydfikENGFLPFRL--------DHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqsdyteaynpkIKRDE 313
Cdd:cd05571  75 EYV---------NGGELFFHLsrervfseDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLL-------------LDKDG 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 314 RtlinpdIKVVDFG----SATYDDEHhSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDskeHLA 389
Cdd:cd05571 133 H------IKITDFGlckeEISYGATT-KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRD---HEV 202
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 390 MMERILGP---LPKHMIQKTRkrkyfhhdrldwdehssagryvsrrckplkefmlsqdveherlfDLIQKMLEYDPAKRI 466
Cdd:cd05571 203 LFELILMEevrFPSTLSPEAK--------------------------------------------SLLAGLLKKDPKKRL 238
                       330       340
                ....*....|....*....|....*....
gi 67551261 467 -----TLREALKHPFF------DLLKKSI 484
Cdd:cd05571 239 gggprDAKEIMEHPFFasinwdDLYQKKI 267
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
167-375 3.25e-10

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: 60.77  E-value: 3.25e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIDHkagGRHVAVKIV-----KNVDRYCEAARSEIQV---LEHLNTTdpnsTFRCVQMLEwfehhGHIC 238
Cdd:cd14148   2 IGVGGFGKVYKGLWR---GEEVAVKAArqdpdEDIAVTAENVRQEARLfwmLQHPNII----ALRGVCLNP-----PHLC 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 239 IVFELLGLSTYDFIKENGFLPFRLdhIRKMAYQICKSVNFLHSNK---LTHTDLKPENILFVQsdyteaynpKIKRDErt 315
Cdd:cd14148  70 LVMEYARGGALNRALAGKKVPPHV--LVNWAVQIARGMNYLHNEAivpIIHRDLKSSNILILE---------PIENDD-- 136
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 67551261 316 LINPDIKVVDFGSATydDEHHSTLVS---TRHYRAPEVILALGWSQPCDVWSIGCILIEYYLG 375
Cdd:cd14148 137 LSGKTLKITDFGLAR--EWHKTTKMSaagTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTG 197
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
161-395 3.44e-10

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: 61.57  E-value: 3.44e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVeCIDHKAGGRHVAVKIVKNvdRYCEAARSEIQVLEHLNTTDPNSTFRCVQMLEW-FEHHGHICI 239
Cdd:cd05602   9 FHFLKVIGKGSFGKVL-LARHKSDEKFYAVKVLQK--KAILKKKEEKHIMSERNVLLKNVKHPFLVGLHFsFQTTDKLYF 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 240 VFELL--GLSTYDFIKENGFLPFRldhIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrdertli 317
Cdd:cd05602  86 VLDYIngGELFYHLQRERCFLEPR---ARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGH---------------- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 318 npdIKVVDFGSATYDDEHH---STLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEhlaMMERI 394
Cdd:cd05602 147 ---IVLTDFGLCKENIEPNgttSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAE---MYDNI 220

                .
gi 67551261 395 L 395
Cdd:cd05602 221 L 221
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
161-379 4.21e-10

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: 61.55  E-value: 4.21e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVvECIDHKAGGRHVAVKIVKnvdRYCEAARSEIQVL-EHLNTTDPNSTFRCVQMLEWFEHHGHICI 239
Cdd:cd05621  54 YDVVKVIGRGAFGEV-QLVRHKASQKVYAMKLLS---KFEMIKRSDSAFFwEERDIMAFANSPWVVQLFCAFQDDKYLYM 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 240 VFELLG-------LSTYDFIKENGflpfrldhiRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrd 312
Cdd:cd05621 130 VMEYMPggdlvnlMSNYDVPEKWA---------KFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGH----------- 189
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 67551261 313 ertlinpdIKVVDFGSATYDDE----HHSTLVSTRHYRAPEVILALG----WSQPCDVWSIGCILIEYYLGFTVF 379
Cdd:cd05621 190 --------LKLADFGTCMKMDEtgmvHCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLFEMLVGDTPF 256
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
167-375 4.51e-10

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: 60.44  E-value: 4.51e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVvecidHKAG--GRHVAVKIVK-----NVDRYCEAARSEIQV---LEHLNTTDPNSTfrCVQmlewfehHGH 236
Cdd:cd14146   2 IGVGGFGKV-----YRATwkGQEVAVKAARqdpdeDIKATAESVRQEAKLfsmLRHPNIIKLEGV--CLE-------EPN 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELL--GLSTYDFIKENGFLPFRLD-----HIR-KMAYQICKSVNFLHSNKLT---HTDLKPENILFVQsdyteay 305
Cdd:cd14146  68 LCLVMEFArgGTLNRALAAANAAPGPRRArrippHILvNWAVQIARGMLYLHEEAVVpilHRDLKSSNILLLE------- 140
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 67551261 306 npKIKRDErtLINPDIKVVDFGSATydDEHHSTLVS---TRHYRAPEVILALGWSQPCDVWSIGCILIEYYLG 375
Cdd:cd14146 141 --KIEHDD--ICNKTLKITDFGLAR--EWHRTTKMSaagTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTG 207
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
276-386 4.54e-10

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: 60.71  E-value: 4.54e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 276 VNFLHSNKLTHTDLKPENILFvqsdyteaynpkikrDERTlinpDIKVVDFGSATYDDEHH---STlVSTRHYRAPEVIL 352
Cdd:cd05599 114 IESIHKLGYIHRDIKPDNLLL---------------DARG----HIKLSDFGLCTGLKKSHlayST-VGTPDYIAPEVFL 173
                        90       100       110
                ....*....|....*....|....*....|....
gi 67551261 353 ALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKE 386
Cdd:cd05599 174 QKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQE 207
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
161-476 5.72e-10

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: 59.66  E-value: 5.72e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIdHKAGGRHVAVKIVKNVDRYCEAAR---SEIQVLEHLNttDPNstfrCVQMLEWFEHHGHI 237
Cdd:cd14075   4 YRIRGELGSGNFSQVKLGI-HQLTKEKVAIKILDKTKLDQKTQRllsREISSMEKLH--HPN----IIRLYEVVETLSKL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 238 CIVFELL-GLSTYDFIKENGflPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrdertl 316
Cdd:cd14075  77 HLVMEYAsGGELYTKISTEG--KLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNC--------------- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 317 inpdIKVVDFGSATY--DDEHHSTLVSTRHYRAPEVILALGW-SQPCDVWSIGCILIEYYLGFTVFpthdSKEHLAMMER 393
Cdd:cd14075 140 ----VKVGDFGFSTHakRGETLNTFCGSPPYAAPELFKDEHYiGIYVDIWALGVLLYFMVTGVMPF----RAETVAKLKK 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 394 -ILgplpkhmiqktrkrkyfhhdrldwDEHSSAGRYVSRRCKplkefmlsqdveherlfDLIQKMLEYDPAKRITLREAL 472
Cdd:cd14075 212 cIL------------------------EGTYTIPSYVSEPCQ-----------------ELIRGILQPVPSDRYSIDEIK 250

                ....
gi 67551261 473 KHPF 476
Cdd:cd14075 251 NSEW 254
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
165-375 7.21e-10

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: 59.64  E-value: 7.21e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 165 DTLGEGAFGKVVECIDHKAGGRhVAVKIVKnVDRYcEAARSEIQV-LEHLNTTDPNSTFRCVQMLEWFEHHGHicivfel 243
Cdd:cd13995  10 DFIPRGAFGKVYLAQDTKTKKR-MACKLIP-VEQF-KPSDVEIQAcFRHENIAELYGALLWEETVHLFMEAGE------- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 244 lGLSTYDFIKENGflPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYTeaynpkikrdertlinpdikV 323
Cdd:cd13995  80 -GGSVLEKLESCG--PMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAV--------------------L 136
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 67551261 324 VDFG---SATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLG 375
Cdd:cd13995 137 VDFGlsvQMTEDVYVPKDLRGTEIYMSPEVILCRGHNTKADIYSLGATIIHMQTG 191
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
138-477 1.01e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 59.89  E-value: 1.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  138 TRSVEDDEEGHLICQSGD---VLSARYEIVDTLGEGAFGKVVecIDHKAG-GRHVAVKIVKNVDRYCEAARseIQVLEHL 213
Cdd:PHA03209  42 SESDDDDDDGLIPTKQKArevVASLGYTVIKTLTPGSEGRVF--VATKPGqPDPVVLKIGQKGTTLIEAML--LQNVNHP 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  214 NTtdpnstfrcVQMLEWFEHHGHICIVFELLGLSTYDFIKENGfLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPEN 293
Cdd:PHA03209 118 SV---------IRMKDTLVSGAITCMVLPHYSSDLYTYLTKRS-RPLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTEN 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  294 ILFVQSDyteaynpkikrdertlinpDIKVVDFGSATYD--DEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIE 371
Cdd:PHA03209 188 IFINDVD-------------------QVCIGDLGAAQFPvvAPAFLGLAGTVETNAPEVLARDKYNSKADIWSAGIVLFE 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  372 yYLGF--TVF---------PTHDSKEHLAMMERILGPLPKHMIQKTRKRKyfhhdRLDWDEHSSAGRYVSRRCKPLKEFM 440
Cdd:PHA03209 249 -MLAYpsTIFedppstpeeYVKSCHSHLLKIISTLKVHPEEFPRDPGSRL-----VRGFIEYASLERQPYTRYPCFQRVN 322
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 67551261  441 LSQDVEHerlfdLIQKMLEYDPAKRITLREALKHPFF 477
Cdd:PHA03209 323 LPIDGEF-----LVHKMLTFDAAMRPSAEEILNYPMF 354
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
152-477 1.05e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 60.48  E-value: 1.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  152 QSGDVLSARYEIVDTLGEGAFGKVVECIDHKAGG-------------------RHVAvKIVKNVDRYCEAARSEIQVLEH 212
Cdd:PHA03210 141 KHDDEFLAHFRVIDDLPAGAFGKIFICALRASTEeaearrgvnstnqgkpkceRLIA-KRVKAGSRAAIQLENEILALGR 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  213 LNTTDpnstfrCVQMLEWFEHHGHICIVFELLGLSTYDFIKENGF----LPFrLDHIRKMAYQICKSVNFLHSNKLTHTD 288
Cdd:PHA03210 220 LNHEN------ILKIEEILRSEANTYMITQKYDFDLYSFMYDEAFdwkdRPL-LKQTRAIMKQLLCAVEYIHDKKLIHRD 292
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  289 LKPENIlfvqsdyteaynpkikrdertLINPDIKVV--DFGSAT-YDDEHHS---TLVSTRHYRAPEVILALGWSQPCDV 362
Cdd:PHA03210 293 IKLENI---------------------FLNCDGKIVlgDFGTAMpFEKEREAfdyGWVGTVATNSPEILAGDGYCEITDI 351
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  363 WSIGCILIEyYLGFTVFPTHD-SKEHLAMMERILGPL----------PKHMiqktrkrkyfhHDRLDWDEHSSAGRYVSr 431
Cdd:PHA03210 352 WSCGLILLD-MLSHDFCPIGDgGGKPGKQLLKIIDSLsvcdeefpdpPCKL-----------FDYIDSAEIDHAGHSVP- 418
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 67551261  432 rckPL-KEFMLSQDVEHErlfdlIQKMLEYDPAKRITLREALKHPFF 477
Cdd:PHA03210 419 ---PLiRNLGLPADFEYP-----LVKMLTFDWHLRPGAAELLALPLF 457
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
167-366 1.28e-09

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: 58.93  E-value: 1.28e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIDHkagGRHVAVKIVKNVDRYCEAARS---EIQV--LEHLNTTDpnstfrcVQMLEWFEHHGHI-CIV 240
Cdd:cd13979  11 LGSGGFGSVYKATYK---GETVAVKIVRRRRKNRASRQSfwaELNAarLRHENIVR-------VLAAETGTDFASLgLII 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 241 FELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyTEAYNPKIkrdertlinpd 320
Cdd:cd13979  81 MEYCGNGTLQQLIYEGSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILI-----SEQGVCKL----------- 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 67551261 321 ikvVDFGSATYDDE------HHSTLVSTRHYRAPEVILALGWSQPCDVWSIG 366
Cdd:cd13979 145 ---CDFGCSVKLGEgnevgtPRSHIGGTYTYRAPELLKGERVTPKADIYSFG 193
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
167-477 1.44e-09

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


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 59.08  E-value: 1.44e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECiDHKAGGRHVAVKIV--KNVD-RYCEA-ARSEIQVLEHLNttdpnSTFrCVQMLEWFEHHGHICIVFE 242
Cdd:cd05577   1 LGRGGFGEVCAC-QVKATGKMYACKKLdkKRIKkKKGETmALNEKIILEKVS-----SPF-IVSLAYAFETKDKLCLVLT 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 243 LLGLSTYDF-IKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteaynpkikrDErtliNPDI 321
Cdd:cd05577  74 LMNGGDLKYhIYNVGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILL---------------DD----HGHV 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 322 KVVDFGSATYDDEHHST--LVSTRHYRAPEVIL-ALGWSQPCDVWSIGCILIEYYLGFTVFpthdskehlammerilgpl 398
Cdd:cd05577 135 RISDLGLAVEFKGGKKIkgRVGTHGYMAPEVLQkEVAYDFSVDWFALGCMLYEMIAGRSPF------------------- 195
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 399 pkhmiqKTRKRKYFHHDrldwdehssagryvsrrckpLKEFMLSQDVEHERLF-----DLIQKMLEYDPAKRITLR---- 469
Cdd:cd05577 196 ------RQRKEKVDKEE--------------------LKRRTLEMAVEYPDSFspearSLCEGLLQKDPERRLGCRggsa 249

                ....*....
gi 67551261 470 -EALKHPFF 477
Cdd:cd05577 250 dEVKEHPFF 258
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
161-393 1.50e-09

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: 59.29  E-value: 1.50e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAfGKVVECIDHKAGGRHVAVKIVKNVDRycEAARS----EIQVLEHLNTTdpnstfRCVQMLEWFEHHGH 236
Cdd:cd06649   7 FERISELGAGN-GGVVTKVQHKPSGLIMARKLIHLEIK--PAIRNqiirELQVLHECNSP------YIVGFYGAFYSDGE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELL-GLSTYDFIKENGFLPFRLdhIRKMAYQICKSVNFL-HSNKLTHTDLKPENILfVQSdyteaynpkikRDEr 314
Cdd:cd06649  78 ISICMEHMdGGSLDQVLKEAKRIPEEI--LGKVSIAVLRGLAYLrEKHQIMHRDVKPSNIL-VNS-----------RGE- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 315 tlinpdIKVVDFG-SATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMMER 393
Cdd:cd06649 143 ------IKLCDFGvSGQLIDSMANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYPIPPPDAKELEAIFGR 216
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
286-375 1.65e-09

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: 59.25  E-value: 1.65e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 286 HTDLKPENILfvqsdyteaynpkIKRDERtlinpdIKVVDFGSAT-----YDDEH---HStLVSTRHYRAPEVILALGWS 357
Cdd:cd05598 124 HRDIKPDNIL-------------IDRDGH------IKLTDFGLCTgfrwtHDSKYylaHS-LVGTPNYIAPEVLLRTGYT 183
                        90
                ....*....|....*...
gi 67551261 358 QPCDVWSIGCILIEYYLG 375
Cdd:cd05598 184 QLCDWWSVGVILYEMLVG 201
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
222-476 1.71e-09

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: 58.53  E-value: 1.71e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 222 FRCVQMLEWFEHHghICIVFE-LLGLSTYDFIKENGFLPfrLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSD 300
Cdd:cd14012  66 FSIERRGRSDGWK--VYLLTEyAPGGSLSELLDSVGSVP--LDTARRWTLQLLEALEYLHRNGVVHKSLHAGNVLLDRDA 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 301 YTeaYNPKIKrD---ERTLINPDikvvdfgSATYDDEHHSTlvstrHYRAPEVIL-ALGWSQPCDVWSIGCILIEyylgf 376
Cdd:cd14012 142 GT--GIVKLT-DyslGKTLLDMC-------SRGSLDEFKQT-----YWLPPELAQgSKSPTRKTDVWDLGLLFLQ----- 201
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 377 tvfpthdskehlammerilgplpkhMIQktrkrkyfhhdrldwdehssaGRYVSRRCKPLKEFMLSQDVeHERLFDLIQK 456
Cdd:cd14012 202 -------------------------MLF---------------------GLDVLEKYTSPNPVLVSLDL-SASLQDFLSK 234
                       250       260
                ....*....|....*....|
gi 67551261 457 MLEYDPAKRITLREALKHPF 476
Cdd:cd14012 235 CLSLDPKKRPTALELLPHEF 254
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
265-421 1.87e-09

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: 58.40  E-value: 1.87e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 265 IRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQsdyteaynpkikrdertliNPDIKVVDFGSATY---DDEHHSTLVS 341
Cdd:cd14189 103 VRYYLKQIISGLKYLHLKGILHRDLKLGNFFINE-------------------NMELKVGDFGLAARlepPEQRKKTICG 163
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 342 TRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMMERILGPLP-------KHMIQKTRKRKyfHH 414
Cdd:cd14189 164 TPNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQVKYTLPaslslpaRHLLAGILKRN--PG 241

                ....*..
gi 67551261 415 DRLDWDE 421
Cdd:cd14189 242 DRLTLDQ 248
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
167-484 1.94e-09

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: 58.77  E-value: 1.94e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKV--VEcidHKAGGRHVAVKIVKNV----DRYCEAARSEIQVLEHLNttdpnstfRC---VQMLEWFEHHGHI 237
Cdd:cd05570   3 LGKGSFGKVmlAE---RKKTDELYAIKVLKKEviieDDDVECTMTEKRVLALAN--------RHpflTGLHACFQTEDRL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 238 CIVFELLglSTYDF---IKENGflPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVqsdyTEAYnpkikrder 314
Cdd:cd05570  72 YFVMEYV--NGGDLmfhIQRAR--RFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLD----AEGH--------- 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 315 tlinpdIKVVDFG---SATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEhlaMM 391
Cdd:cd05570 135 ------IKIADFGmckEGIWGGNTTSTFCGTPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDE---LF 205
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 392 ERILG---PLPKHMiqktrkrkyfhhdrldwdehssagryvSRRCKplkefmlsqdveherlfDLIQKMLEYDPAKRI-- 466
Cdd:cd05570 206 EAILNdevLYPRWL---------------------------SREAV-----------------SILKGLLTKDPARRLgc 241
                       330       340
                ....*....|....*....|....*..
gi 67551261 467 --TLREALK-HPFF------DLLKKSI 484
Cdd:cd05570 242 gpKGEADIKaHPFFrnidwdKLEKKEV 268
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
167-477 2.08e-09

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: 58.78  E-value: 2.08e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVeCIDHKAGGRHVAVKIVKN----VDRYCEAARSEIQVL----EHLNTTDPNSTFRCVQmlewfehhgHIC 238
Cdd:cd05619  13 LGKGSFGKVF-LAELKGTNQFFAIKALKKdvvlMDDDVECTMVEKRVLslawEHPFLTHLFCTFQTKE---------NLF 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 239 IVFELLglstydfikENGFLPFRLDHIRKM--------AYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkik 310
Cdd:cd05619  83 FVMEYL---------NGGDLMFHIQSCHKFdlpratfyAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGH--------- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 311 rdertlinpdIKVVDFG---SATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEh 387
Cdd:cd05619 145 ----------IKIADFGmckENMLGDAKTSTFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEE- 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 388 lammerilgplpkhmiqktrkrkYFHHDRLDwdehssagryvsrrcKPLKEFMLSQDVEherlfDLIQKMLEYDPAKRIT 467
Cdd:cd05619 214 -----------------------LFQSIRMD---------------NPFYPRWLEKEAK-----DILVKLFVREPERRLG 250
                       330
                ....*....|.
gi 67551261 468 LREALK-HPFF 477
Cdd:cd05619 251 VRGDIRqHPFF 261
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
161-368 2.33e-09

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: 57.99  E-value: 2.33e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFgKVVECIDHKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTdpnstfRCVQMLEWFEHHGHICIV 240
Cdd:cd14108   4 YDIHKEIGRGAF-SYLRRVKEKSSDLSFAAKFIPVRAKKKTSARRELALLAELDHK------SIVRFHDAFEKRRVVIIV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 241 FELlglSTYDFIKENGFLPFRLD-HIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYTEaynpkikrdertlinp 319
Cdd:cd14108  77 TEL---CHEELLERITKRPTVCEsEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKTDQ---------------- 137
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 67551261 320 dIKVVDFGSA--TYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCI 368
Cdd:cd14108 138 -VRICDFGNAqeLTPNEPQYCKYGTPEFVAPEIVNQSPVSKVTDIWPVGVI 187
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
167-375 2.55e-09

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: 58.05  E-value: 2.55e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVecIDHKAGGRHVAVKI--VKNVDRYCEAARSEIqvLEHLNTTDPNSTF----RCVQMLEWFEH------- 233
Cdd:cd14067   1 LGQGGSGTVI--YRARYQGQPVAVKRfhIKKCKKRTDGSADTM--LKHLRAADAMKNFsefrQEASMLHSLQHpcivyli 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 234 ----HGhICIVFELLGLSTYDFI-----KENGFLPfrLDHI--RKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYT 302
Cdd:cd14067  77 gisiHP-LCFALELAPLGSLNTVleenhKGSSFMP--LGHMltFKIAYQIAAGLAYLHKKNIIFCDLKSDNILVWSLDVQ 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 67551261 303 EAYNpkikrdertlinpdIKVVDFGsATYDDEHHSTL--VSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLG 375
Cdd:cd14067 154 EHIN--------------IKLSDYG-ISRQSFHEGALgvEGTPGYQAPEIRPRIVYDEKVDMFSYGMVLYELLSG 213
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
162-371 2.57e-09

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: 58.12  E-value: 2.57e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 162 EIVDTLGEGAFGKVVE-----CIDHKAGGRhVAVKIVKnvdrycEAARSEiQVLEHLNTTDPNSTFRC---VQMLEWFEH 233
Cdd:cd05032   9 TLIRELGQGSFGMVYEglakgVVKGEPETR-VAIKTVN------ENASMR-ERIEFLNEASVMKEFNChhvVRLLGVVST 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 234 HGHICIVFELLG---LSTY------DFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfVQSDYTea 304
Cdd:cd05032  81 GQPTLVVMELMAkgdLKSYlrsrrpEAENNPGLGPPTLQKFIQMAAEIADGMAYLAAKKFVHRDLAARNCM-VAEDLT-- 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 67551261 305 ynpkikrdertlinpdIKVVDFGSAtyddehhSTLVSTRHYR------------APEVILALGWSQPCDVWSIGCILIE 371
Cdd:cd05032 158 ----------------VKIGDFGMT-------RDIYETDYYRkggkgllpvrwmAPESLKDGVFTTKSDVWSFGVVLWE 213
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
162-375 2.61e-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: 58.13  E-value: 2.61e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 162 EIVDTLGEGAFGKVvecidHKaGGRH--VAVKIVkNVDRYCE----AARSEIQVLE---HLNTT-------DPNstfrcv 225
Cdd:cd14063   3 EIKEVIGKGRFGRV-----HR-GRWHgdVAIKLL-NIDYLNEeqleAFKEEVAAYKntrHDNLVlfmgacmDPP------ 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 226 qmlewfehhgHICIVFELL-GLSTYDFIKEnGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqsdytea 304
Cdd:cd14063  70 ----------HLAIVTSLCkGRTLYSLIHE-RKEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIF--------- 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 305 ynpkikrdertLINPDIKVVDFG-----SATYDDEHHSTLVSTRH---YRAPEVILALG----------WSQPCDVWSIG 366
Cdd:cd14063 130 -----------LENGRVVITDFGlfslsGLLQPGRREDTLVIPNGwlcYLAPEIIRALSpdldfeeslpFTKASDVYAFG 198

                ....*....
gi 67551261 367 CILIEYYLG 375
Cdd:cd14063 199 TVWYELLAG 207
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
206-475 2.69e-09

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: 58.14  E-value: 2.69e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 206 EIQVLEHLNttDPNstfrCVQMLEWFE--HHGHICIVFELLGLStyDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNK 283
Cdd:cd14118  64 EIAILKKLD--HPN----VVKLVEVLDdpNEDNLYMVFELVDKG--AVMEVPTDNPLSEETARSYFRDIVLGIEYLHYQK 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 284 LTHTDLKPENILFVQSDYteaynpkikrdertlinpdIKVVDFGSA---TYDDEHHSTLVSTRHYRAPEVILALGWSQ-- 358
Cdd:cd14118 136 IIHRDIKPSNLLLGDDGH-------------------VKIADFGVSnefEGDDALLSSTAGTPAFMAPEALSESRKKFsg 196
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 359 -PCDVWSIGCILieYYLGFTVFPTHDskEH-LAMMERIlgplpkhmiqktrkrkyfhhdrldwdehssagryvsrRCKPL 436
Cdd:cd14118 197 kALDIWAMGVTL--YCFVFGRCPFED--DHiLGLHEKI-------------------------------------KTDPV 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 67551261 437 K---EFMLSQDVEherlfDLIQKMLEYDPAKRITLREALKHP 475
Cdd:cd14118 236 VfpdDPVVSEQLK-----DLILRMLDKNPSERITLPEIKEHP 272
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
161-477 8.02e-09

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: 57.24  E-value: 8.02e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKV--VECIDHKAGGRHVAVKIVKNV-----DRYCEAARSEIQVLEHLNttdpNSTFrCVQMLEWFEH 233
Cdd:cd05614   2 FELLKVLGTGAYGKVflVRKVSGHDANKLYAMKVLRKAalvqkAKTVEHTRTERNVLEHVR----QSPF-LVTLHYAFQT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 234 HGHICIVFELLG---LSTYDFIKENgflpFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkik 310
Cdd:cd05614  77 DAKLHLILDYVSggeLFTHLYQRDH----FSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGH--------- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 311 rdertlinpdIKVVDFGSA----TYDDEHHSTLVSTRHYRAPEVILA-LGWSQPCDVWSIGCILIEYYLGFTVFPTHDSK 385
Cdd:cd05614 144 ----------VVLTDFGLSkeflTEEKERTYSFCGTIEYMAPEIIRGkSGHGKAVDWWSLGILMFELLTGASPFTLEGEK 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 386 EHLA-MMERILgplpkhmiqktrkrkyfhhdrldwdehssagryvsrRCKPLKEFMLSQDVEherlfDLIQKMLEYDPAK 464
Cdd:cd05614 214 NTQSeVSRRIL------------------------------------KCDPPFPSFIGPVAR-----DLLQKLLCKDPKK 252
                       330
                ....*....|....*...
gi 67551261 465 RI-----TLREALKHPFF 477
Cdd:cd05614 253 RLgagpqGAQEIKEHPFF 270
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
164-373 8.05e-09

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: 56.50  E-value: 8.05e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 164 VDTLGEGAFGKVvecidHKA---GGRHVAVKIVKnvdrycEAARSEIQVLEHLNTTDPNSTFRCVQMLEWFEHHGHICIV 240
Cdd:cd05112   9 VQEIGSGQFGLV-----HLGywlNKDKVAIKTIR------EGAMSEEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 241 FELLglstydfikENGFLP---------FRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQsdyteaynpkikr 311
Cdd:cd05112  78 FEFM---------EHGCLSdylrtqrglFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGE------------- 135
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 67551261 312 dertliNPDIKVVDFGSATY--DDEHHSTLVSTRHYR--APEVILALGWSQPCDVWSIGCILIEYY 373
Cdd:cd05112 136 ------NQVVKVSDFGMTRFvlDDQYTSSTGTKFPVKwsSPEVFSFSRYSSKSDVWSFGVLMWEVF 195
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
270-477 8.21e-09

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: 56.28  E-value: 8.21e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 270 YQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrdertlinpdIKVVDFGSATYDDEHHS---TLVSTRHYR 346
Cdd:cd08221 108 YQIVSAVSHIHKAGILHRDIKTLNIFLTKADL-------------------VKLGDFGISKVLDSESSmaeSIVGTPYYM 168
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 347 APEVILALGWSQPCDVWSIGCILIEYylgFTVFPTHDSKEHLAMMERILgplpkhmiqktrkrkyfhhdRLDWDEHSsag 426
Cdd:cd08221 169 SPELVQGVKYNFKSDIWAVGCVLYEL---LTLKRTFDATNPLRLAVKIV--------------------QGEYEDID--- 222
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 67551261 427 ryvsrrckplkefmlsqDVEHERLFDLIQKMLEYDPAKRITLREALKHPFF 477
Cdd:cd08221 223 -----------------EQYSEEIIQLVHDCLHQDPEDRPTAEELLERPLL 256
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
263-477 9.75e-09

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: 56.96  E-value: 9.75e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 263 DHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQS------DY---TEAYNP-KIKRDERTLINPDIKVVDFGSATY- 331
Cdd:cd05600 111 EHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSghikltDFglaSGTLSPkKIESMKIRLEEVKNTAFLELTAKEr 190
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 332 ---------DDEHHS-TLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMMERIlgplpKH 401
Cdd:cd05600 191 rniyramrkEDQNYAnSVVGSPDYMAPEVLRGEGYDLTVDYWSLGCILFECLVGFPPFSGSTPNETWANLYHW-----KK 265
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 67551261 402 MIQKTRKRkyfhhdrldwdehssagryvsrrcKPLKEFMLSqdvehERLFDLIQKMLEyDPAKRI-TLREALKHPFF 477
Cdd:cd05600 266 TLQRPVYT------------------------DPDLEFNLS-----DEAWDLITKLIT-DPQDRLqSPEQIKNHPFF 312
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
160-388 9.89e-09

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: 56.80  E-value: 9.89e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDHKAGGRhVAVKIVK-NVDRYCEAARSEIQVLEHLNTTDPNSTF--RCV----QMLEWFE 232
Cdd:cd13977   1 KYSLIREVGRGSYGVVYEAVVRRTGAR-VAVKKIRcNAPENVELALREFWALSSIQRQHPNVIQleECVlqrdGLAQRMS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 233 HHGHICIVFELL------GLSTYDFiKENGFLPFRLDHI-------------------RKMAYQICKSVNFLHSNKLTHT 287
Cdd:cd13977  80 HGSSKSDLYLLLvetslkGERCFDP-RSACYLWFVMEFCdggdmneyllsrrpdrqtnTSFMLQLSSALAFLHRNQIVHR 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 288 DLKPENILFVQsdyteaynpkiKRDErtlinPDIKVVDFG--------------SATYDDEHHSTLVSTRHYRAPEVila 353
Cdd:cd13977 159 DLKPDNILISH-----------KRGE-----PILKVADFGlskvcsgsglnpeePANVNKHFLSSACGSDFYMAPEV--- 219
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 67551261 354 lgW----SQPCDVWSIGCILIEYYLGFTVFPTHDSKEHL 388
Cdd:cd13977 220 --WeghyTAKADIFALGIIIWAMVERITFRDGETKKELL 256
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
253-484 9.98e-09

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: 56.56  E-value: 9.98e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 253 KENGFLPFRldhIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrdertlinpdIKVVDFGSATYD 332
Cdd:cd05575  89 RERHFPEPR---ARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGH-------------------VVLTDFGLCKEG 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 333 DEHH---STLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEhlaMMERILgplpkhmiqktrkr 409
Cdd:cd05575 147 IEPSdttSTFCGTPEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRDTAE---MYDNIL-------------- 209
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 410 kyfhHDRLDWDEH-SSAGRyvsrrckplkefmlsqdveherlfDLIQKMLEYDPAKRI----TLREALKHPFF------D 478
Cdd:cd05575 210 ----HKPLRLRTNvSPSAR------------------------DLLEGLLQKDRTKRLgsgnDFLEIKNHSFFrpinwdD 261

                ....*.
gi 67551261 479 LLKKSI 484
Cdd:cd05575 262 LEAKKI 267
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
160-380 1.03e-08

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


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 56.91  E-value: 1.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVEC----IDHKAGGRHVAVKIVKNVDRYCE--AARSEIQVL----EHLNTTdpNSTFRCVQmle 229
Cdd:cd05102   8 RLRLGKVLGHGAFGKVVEAsafgIDKSSSCETVAVKMLKEGATASEhkALMSELKILihigNHLNVV--NLLGACTK--- 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 230 wfeHHGHICIVFELL---GLSTYDFIKENGFLPFR------LDHIRKM-------------------------------- 268
Cdd:cd05102  83 ---PNGPLMVIVEFCkygNLSNFLRAKREGFSPYRersprtRSQVRSMveavradrrsrqgsdrvasftestsstnqprq 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 269 ------------------AYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrdertlinpdIKVVDFGSA- 329
Cdd:cd05102 160 evddlwqspltmedlicySFQVARGMEFLASRKCIHRDLAARNILLSENNV-------------------VKICDFGLAr 220
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 67551261 330 -TYDDEHHSTLVSTR---HYRAPEVILALGWSQPCDVWSIGCILIEYY-LGFTVFP 380
Cdd:cd05102 221 dIYKDPDYVRKGSARlplKWMAPESIFDKVYTTQSDVWSFGVLLWEIFsLGASPYP 276
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
161-435 1.06e-08

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: 56.54  E-value: 1.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVeCIDHKAGGRHVAVKIVKNVD----RYCEAARSEIQVLEHLNTTdpNSTFrCVQMLEWFEHHGH 236
Cdd:cd05589   1 FRCIAVLGRGHFGKVL-LAEYKPTGELFAIKALKKGDiiarDEVESLMCEKRIFETVNSA--RHPF-LVNLFACFQTPEH 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELL-GLSTYDFIKENGFlpfrlDHIRKMAYQICK--SVNFLHSNKLTHTDLKPENILFvqsDyTEAYnpkikrde 313
Cdd:cd05589  77 VCFVMEYAaGGDLMMHIHEDVF-----SEPRAVFYAACVvlGLQFLHEHKIVYRDLKLDNLLL---D-TEGY-------- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 314 rtlinpdIKVVDFG----SATYDDEHhSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHD------ 383
Cdd:cd05589 140 -------VKIADFGlckeGMGFGDRT-STFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDeeevfd 211
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 67551261 384 -------------SKEHLAMMERILGPLPKHMI-------QKTRKRKYFHHdrLDWDEhssagrYVSRRCKP 435
Cdd:cd05589 212 sivndevryprflSTEAISIMRRLLRKNPERRLgaserdaEDVKKQPFFRN--IDWEA------LLARKIKP 275
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
201-476 1.21e-08

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: 56.13  E-value: 1.21e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 201 EAARSEIQVLEHLNttDPNstfrCVQMLEWFE--HHGHICIVFELLGLSTYDFIKENGflPFRLDHIRKMAYQICKSVNF 278
Cdd:cd14199  70 ERVYQEIAILKKLD--HPN----VVKLVEVLDdpSEDHLYMVFELVKQGPVMEVPTLK--PLSEDQARFYFQDLIKGIEY 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 279 LHSNKLTHTDLKPENILFVQSDYteaynpkikrdertlinpdIKVVDFG-SATYD--DEHHSTLVSTRHYRAPEVI---L 352
Cdd:cd14199 142 LHYQKIIHRDVKPSNLLVGEDGH-------------------IKIADFGvSNEFEgsDALLTNTVGTPAFMAPETLsetR 202
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 353 ALGWSQPCDVWSIGCILIEYYLGFTVFpthdskehlaMMERILGplpkhmiqktrkrkyfHHDRLdwdehssagryvsrR 432
Cdd:cd14199 203 KIFSGKALDVWAMGVTLYCFVFGQCPF----------MDERILS----------------LHSKI--------------K 242
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 67551261 433 CKPLkEFMLSQDVEhERLFDLIQKMLEYDPAKRITLREALKHPF 476
Cdd:cd14199 243 TQPL-EFPDQPDIS-DDLKDLLFRMLDKNPESRISVPEIKLHPW 284
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
167-379 1.32e-08

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: 56.13  E-value: 1.32e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIDHKAGGRHVAVKIVKN--VDRYCEA-ARSEIQVLEHLNttdpnSTFrCVQMLEWFEHHGHICIVFEL 243
Cdd:cd05632  10 LGKGGFGEVCACQVRATGKMYACKRLEKKriKKRKGESmALNEKQILEKVN-----SQF-VVNLAYAYETKDALCLVLTI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 244 LGLSTYDF-IKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqSDYTEaynpkikrdertlinpdIK 322
Cdd:cd05632  84 MNGGDLKFhIYNMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILL--DDYGH-----------------IR 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 67551261 323 VVDFGSATYDDEHHST--LVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVF 379
Cdd:cd05632 145 ISDLGLAVKIPEGESIrgRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPF 203
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
188-371 1.33e-08

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 56.95  E-value: 1.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  188 VAVKIVKNVDRYCEAARSEIQVLEHLNTtdpnstFRCVQMLEWFEHHGHICIVFEL-----LGLSTYDFIKENgfLPFRL 262
Cdd:PTZ00267  97 VAKFVMLNDERQAAYARSELHCLAACDH------FGIVKHFDDFKSDDKLLLIMEYgsggdLNKQIKQRLKEH--LPFQE 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  263 DHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrdertlinpdIKVVDFG-SATYDD----EHHS 337
Cdd:PTZ00267 169 YEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGI-------------------IKLGDFGfSKQYSDsvslDVAS 229
                        170       180       190
                 ....*....|....*....|....*....|....
gi 67551261  338 TLVSTRHYRAPEVILALGWSQPCDVWSIGCILIE 371
Cdd:PTZ00267 230 SFCGTPYYLAPELWERKRYSKKADMWSLGVILYE 263
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
167-473 1.73e-08

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: 55.71  E-value: 1.73e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIDHKAG---GRHVAVKIVKNVDRYCEAA--RSEIQVLE---HLNTTDPNSTfrCVQmlewfEHHGHIC 238
Cdd:cd05079  12 LGEGHFGKVELCRYDPEGdntGEQVAVKSLKPESGGNHIAdlKKEIEILRnlyHENIVKYKGI--CTE-----DGGNGIK 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 239 IVFELLGLSTydfIKEngFLPFRLDHIR-----KMAYQICKSVNFLHSNKLTHTDLKPENILfVQSDYTeaynpkikrde 313
Cdd:cd05079  85 LIMEFLPSGS---LKE--YLPRNKNKINlkqqlKYAVQICKGMDYLGSRQYVHRDLAARNVL-VESEHQ----------- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 314 rtlinpdIKVVDFG--SATYDDEHHST----LVSTRHYRAPEVILALGWSQPCDVWSIGCILIEyylgFTVFPTHDSKEh 387
Cdd:cd05079 148 -------VKIGDFGltKAIETDKEYYTvkddLDSPVFWYAPECLIQSKFYIASDVWSFGVTLYE----LLTYCDSESSP- 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 388 LAMMERILGPLPKHMIqktrkrkyfhhdrldwdehssagryVSRRCKPLKE--FMLSQDVEHERLFDLIQKMLEYDPAKR 465
Cdd:cd05079 216 MTLFLKMIGPTHGQMT-------------------------VTRLVRVLEEgkRLPRPPNCPEEVYQLMRKCWEFQPSKR 270

                ....*...
gi 67551261 466 ITLREALK 473
Cdd:cd05079 271 TTFQNLIE 278
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
165-477 1.87e-08

Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNT7 is a plant thylakoid-associated kinase that is essential in short- and long-term acclimation responses to cope with various light conditions in order to maintain photosynthetic redox poise for optimal photosynthetic performance. Short-term response involves state transitions over periods of minutes while the long-term response (LTR) occurs over hours to days and involves changing the relative amounts of photosystems I and II. SNT7 acts as a redox sensor and a signal transducer for both responses, which are triggered by the redox state of the plastoquinone (PQ) pool. It is positioned at the top of a phosphorylation cascade that induces state transitions by phosphorylating light-harvesting complex II (LHCII), and triggers the LTR through the phosphorylation of chloroplast proteins. The SNT7 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270915 [Multi-domain]  Cd Length: 318  Bit Score: 55.91  E-value: 1.87e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 165 DTLGEGAFGKV--VECIDHKAGGRHVAVkIVKNVDRYCEAarsEIQVLEHLNTTDPNStfrCVQMLEWFEH-------HG 235
Cdd:cd14013   1 KKLGEGGFGTVykGSLLQKDPGGEKRRV-VLKKAKEYGEV---EIWMNERVRRACPSS---CAEFVGAFLDttskkftKP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 236 HICIVFELLGLST-YDFIKENGFlPFRLDH-------------------IRKMAYQICKSVNFLHSNKLTHTDLKPENIL 295
Cdd:cd14013  74 SLWLVWKYEGDATlADLMQGKEF-PYNLEPiifgrvlipprgpkrenviIKSIMRQILVALRKLHSTGIVHRDVKPQNII 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 296 FVQSDYTeaynpkikrdertlinpdIKVVDFGSA-------------TYDDEHHST----LVSTRHYRAPEVILALGWSq 358
Cdd:cd14013 153 VSEGDGQ------------------FKIIDLGAAadlriginyipkeFLLDPRYAPpeqyIMSTQTPSAPPAPVAAALS- 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 359 PC----------DVWSIGCILIEyylgfTVFPTHDSKEHLAMMERILgplpkhmiqktrkrkyfhhDRLDWDE---HSSA 425
Cdd:cd14013 214 PVlwqmnlpdrfDMYSAGVILLQ-----MAFPNLRSDSNLIAFNRQL-------------------KQCDYDLnawRMLV 269
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 67551261 426 GRYVSRRCKPLKEFMlsqDVEHERLFDLIQKMLEYDPAKRITLREALKHPFF 477
Cdd:cd14013 270 EPRASADLREGFEIL---DLDDGAGWDLVTKLIRYKPRGRLSASAALAHPYF 318
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
160-380 2.07e-08

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


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 55.76  E-value: 2.07e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVEC----IDHKAGGRHVAVKIVKNVDRYCE--AARSEIQVL----EHLNTTdpNSTFRCVQmle 229
Cdd:cd05103   8 RLKLGKPLGRGAFGQVIEAdafgIDKTATCRTVAVKMLKEGATHSEhrALMSELKILihigHHLNVV--NLLGACTK--- 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 230 wfeHHGHICIVFELL---GLSTYDFIKENGFLPF-----------------------RLDHIRK---------------- 267
Cdd:cd05103  83 ---PGGPLMVIVEFCkfgNLSAYLRSKRSEFVPYktkgarfrqgkdyvgdisvdlkrRLDSITSsqssassgfveeksls 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 268 ------------------------MAYQICKSVNFLHSNKLTHTDLKPENILFVQsdyteaynpkikrdertliNPDIKV 323
Cdd:cd05103 160 dveeeeagqedlykdfltledlicYSFQVAKGMEFLASRKCIHRDLAARNILLSE-------------------NNVVKI 220
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 67551261 324 VDFGSA--TYDDEHHSTLVSTR---HYRAPEVILALGWSQPCDVWSIGCILIEYY-LGFTVFP 380
Cdd:cd05103 221 CDFGLArdIYKDPDYVRKGDARlplKWMAPETIFDRVYTIQSDVWSFGVLLWEIFsLGASPYP 283
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
261-478 2.27e-08

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: 55.65  E-value: 2.27e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 261 RLDHIRKMAY--QICKSVNFLHSNKLTHTDLKPENILFvqsDYTEaynpkikrdertlinpDIKVVDFGSATY---DDEH 335
Cdd:cd05585  90 RFDLSRARFYtaELLCALECLHKFNVIYRDLKPENILL---DYTG----------------HIALCDFGLCKLnmkDDDK 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 336 HSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEhlaMMERIlgplpkhmiqktrkrkyfhhd 415
Cdd:cd05585 151 TNTFCGTPEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENTNE---MYRKI--------------------- 206
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 67551261 416 rldwdehssagryvsrrckpLKEFMLSQDVEHERLFDLIQKMLEYDPAKRITL---REALKHPFFD 478
Cdd:cd05585 207 --------------------LQEPLRFPDGFDRDAKDLLIGLLNRDPTKRLGYngaQEIKNHPFFD 252
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
159-477 2.44e-08

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 55.77  E-value: 2.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  159 ARYEIVDTLGEGAFGKVVECIDHKAGgRHVAVKIVKNvdrycEAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHGHIC 238
Cdd:PHA03212  92 AGFSILETFTPGAEGFAFACIDNKTC-EHVVIKAGQR-----GGTATEAHILRAIN--HPS----IIQLKGTFTYNKFTC 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  239 IVFELLGLSTYDFIKENGFLPfrLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENIlfvqsdyteaynpkikrdertLIN 318
Cdd:PHA03212 160 LILPRYKTDLYCYLAAKRNIA--ICDILAIERSVLRAIQYLHENRIIHRDIKAENI---------------------FIN 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  319 --PDIKVVDFGSATYDDEhhstLVSTRHY--------RAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHL 388
Cdd:PHA03212 217 hpGDVCLGDFGAACFPVD----INANKYYgwagtiatNAPELLARDPYGPAVDIWSAGIVLFEMATCHDSLFEKDGLDGD 292
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  389 AMMERilgplpkhMIQKTRKRKYFHHDRLDWDEHSSAGRYVSRRCK---------PL--KEFMLSQDVEHerlfdLIQKM 457
Cdd:PHA03212 293 CDSDR--------QIKLIIRRSGTHPNEFPIDAQANLDEIYIGLAKkssrkpgsrPLwtNLYELPIDLEY-----LICKM 359
                        330       340
                 ....*....|....*....|
gi 67551261  458 LEYDPAKRITLREALKHPFF 477
Cdd:PHA03212 360 LAFDAHHRPSAEALLDFAAF 379
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
167-393 2.45e-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: 54.97  E-value: 2.45e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECI-DHKAGGRHVAVKIVKNvDRYCEAARSEI----QVLEHLNttDPnstfRCVQMLEWFEHHGHIcIVF 241
Cdd:cd05116   3 LGSGNFGTVKKGYyQMKKVVKTVAVKILKN-EANDPALKDELlreaNVMQQLD--NP----YIVRMIGICEAESWM-LVM 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 242 ELLGLSTYD-FIKENGFLPFRldHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYTeaynpkikrdertlinpd 320
Cdd:cd05116  75 EMAELGPLNkFLQKNRHVTEK--NITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYA------------------ 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 321 iKVVDFG--SATYDDEHHSTLVST----RHYRAPEVILALGWSQPCDVWSIGCILIE-YYLGFTVFPTHDSKEHLAMMER 393
Cdd:cd05116 135 -KISDFGlsKALRADENYYKAQTHgkwpVKWYAPECMNYYKFSSKSDVWSFGVLMWEaFSYGQKPYKGMKGNEVTQMIEK 213
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
167-386 2.49e-08

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: 54.88  E-value: 2.49e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVEcidHKAGGRHVAVKIVKnVDRYCEAARSEIQVLEHLNTTDpnstfrCVQMLEWFEHHGhICIVFELLGL 246
Cdd:cd05083  14 IGEGEFGAVLQ---GEYMGQKVAVKNIK-CDVTAQAFLEETAVMTKLQHKN------LVRLLGVILHNG-LYIVMELMSK 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 247 STY-DFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqSDYTEAynpkikrdertlinpdiKVVD 325
Cdd:cd05083  83 GNLvNFLRSRGRALVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILV--SEDGVA-----------------KISD 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 67551261 326 FGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYY-LGFTVFPTHDSKE 386
Cdd:cd05083 144 FGLAKVGSMGVDNSRLPVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFsYGRAPYPKMSVKE 205
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
167-395 2.77e-08

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


Pssm-ID: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 55.35  E-value: 2.77e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVeCIDHKAGGRHVAVKIV-KNV--DRyceaaRSEIQVLEHLNTTDPNSTFRCVQMLEW-FEHHGHICIVFe 242
Cdd:cd05604   4 IGKGSFGKVL-LAKRKRDGKYYAVKVLqKKVilNR-----KEQKHIMAERNVLLKNVKHPFLVGLHYsFQTTDKLYFVL- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 243 llglstyDFIKeNGFLPFRLDHIRKM--------AYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrder 314
Cdd:cd05604  77 -------DFVN-GGELFFHLQRERSFpeprarfyAAEIASALGYLHSINIVYRDLKPENILLDSQGH------------- 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 315 tlinpdIKVVDFG---SATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEhlaMM 391
Cdd:cd05604 136 ------IVLTDFGlckEGISNSDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAE---MY 206

                ....
gi 67551261 392 ERIL 395
Cdd:cd05604 207 ENIL 210
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
167-397 2.98e-08

Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow kinase on the X chromosome; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Btk and Bmx (also named Etk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Btk contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Btk is expressed in B-cells, and a variety of myeloid cells including mast cells, platelets, neutrophils, and dendrictic cells. It interacts with a variety of partners, from cytosolic proteins to nuclear transcription factors, suggesting a diversity of functions. Stimulation of a diverse array of cell surface receptors, including antigen engagement of the B-cell receptor, leads to PH-mediated membrane translocation of Btk and subsequent phosphorylation by Src kinase and activation. Btk plays an important role in the life cycle of B-cells including their development, differentiation, proliferation, survival, and apoptosis. Mutations in Btk cause the primary immunodeficiency disease, X-linked agammaglobulinaemia (XLA) in humans. Bmx is primarily expressed in bone marrow and the arterial endothelium, and plays an important role in ischemia-induced angiogenesis. It facilitates arterial growth, capillary formation, vessel maturation, and bone marrow-derived endothelial progenitor cell mobilization. The Btk/Bmx subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 54.50  E-value: 2.98e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGkVVECidHKAGGRH-VAVKIVKnvdrycEAARSEIQVLEHLNTTDPNSTFRCVQMLEWFEHHGHICIVFELLG 245
Cdd:cd05113  12 LGTGQFG-VVKY--GKWRGQYdVAIKMIK------EGSMSEDEFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMA 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 246 ---LSTYDFIKENGFLPFRLdhiRKMAYQICKSVNFLHSNKLTHTDLKPENILfVQSDYTeaynpkikrdertlinpdIK 322
Cdd:cd05113  83 ngcLLNYLREMRKRFQTQQL---LEMCKDVCEAMEYLESKQFLHRDLAARNCL-VNDQGV------------------VK 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 323 VVDFGSATY--DDEHHSTLVSTRHYR--APEVILALGWSQPCDVWSIGCILIEYY-LG---FTVFPTHDSKEHLAMMERI 394
Cdd:cd05113 141 VSDFGLSRYvlDDEYTSSVGSKFPVRwsPPEVLMYSKFSSKSDVWAFGVLMWEVYsLGkmpYERFTNSETVEHVSQGLRL 220

                ...
gi 67551261 395 LGP 397
Cdd:cd05113 221 YRP 223
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
167-369 3.00e-08

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: 54.64  E-value: 3.00e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIdHKAGGRHVAVKIV-KNVDRYCEAARsEIQVLEHLnttdpnSTFRC-VQMLE-WFEHHGHICIVFEL 243
Cdd:cd13987   1 LGEGTYGKVLLAV-HKGSGTKMALKFVpKPSTKLKDFLR-EYNISLEL------SVHPHiIKTYDvAFETEDYYVFAQEY 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 244 -LGLSTYDFIKENGFLPfrLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYTEaynpkikrdertlinpdIK 322
Cdd:cd13987  73 aPYGDLFSIIPPQVGLP--EERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDCRR-----------------VK 133
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 67551261 323 VVDFGSATYDDehhsTLVSTRH----YRAPEVI-------LALGWSQpcDVWSIGCIL 369
Cdd:cd13987 134 LCDFGLTRRVG----STVKRVSgtipYTAPEVCeakknegFVVDPSI--DVWAFGVLL 185
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
167-433 3.03e-08

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: 54.81  E-value: 3.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVEcidHKAGGRHVAVK-IVKNVDRYCEAAR----SEIQVL---EHLNTtdpnstfrcVQMLEWFEHHGHIC 238
Cdd:cd14158  23 LGEGGFGVVFK---GYINDKNVAVKkLAAMVDISTEDLTkqfeQEIQVMakcQHENL---------VELLGYSCDGPQLC 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 239 IVFELLglstydfikENGFLPFRLD----------HIR-KMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyTEAYNP 307
Cdd:cd14158  91 LVYTYM---------PNGSLLDRLAclndtpplswHMRcKIAQGTANGINYLHENNHIHRDIKSANILL-----DETFVP 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 308 KIKrdertlinpdikvvDFGSATYDDEHHSTL-----VSTRHYRAPEViLALGWSQPCDVWSIGCILIEYYLGFTVFPTH 382
Cdd:cd14158 157 KIS--------------DFGLARASEKFSQTImteriVGTTAYMAPEA-LRGEITPKSDIFSFGVVLLEIITGLPPVDEN 221
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 67551261 383 DSKEHLAMMerilgplpKHMIQKTRKRKYFHHDRL--DWDEHSSAGRY-VSRRC 433
Cdd:cd14158 222 RDPQLLLDI--------KEEIEDEEKTIEDYVDKKmgDWDSTSIEAMYsVASQC 267
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
161-420 3.30e-08

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: 55.46  E-value: 3.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVvECIDHKAGGRHVAVKIVKNVD--RYCEAA--RSEIQVLEHLNTTdpnstfRCVQMLEWFEHHGH 236
Cdd:cd05596  28 FDVIKVIGRGAFGEV-QLVRHKSTKKVYAMKLLSKFEmiKRSDSAffWEERDIMAHANSE------WIVQLHYAFQDDKY 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELLG-------LSTYDFIKengflpfrlDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpki 309
Cdd:cd05596 101 LYMVMDYMPggdlvnlMSNYDVPE---------KWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGH-------- 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 310 krdertlinpdIKVVDFGSATYDDE----HHSTLVSTRHYRAPEVILALG----WSQPCDVWSIGCILIEYYLGFTVFpT 381
Cdd:cd05596 164 -----------LKLADFGTCMKMDKdglvRSDTAVGTPDYISPEVLKSQGgdgvYGRECDWWSVGVFLYEMLVGDTPF-Y 231
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 67551261 382 HDS-----------KEHLAMMERILGP-----------------LPKHMIQKTRKRKYFHHDRLDWD 420
Cdd:cd05596 232 ADSlvgtygkimnhKNSLQFPDDVEISkdakslicafltdrevrLGRNGIEEIKAHPFFKNDQWTWD 298
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
167-408 4.00e-08

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: 54.80  E-value: 4.00e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIdHKAGGRHVAVKIVKNVD--RYCEAARSEIQVLEHLNTTDPNSTFRCVQMLEwfehHGHICIVFELL 244
Cdd:cd13988   1 LGQGATANVFRGR-HKKTGDLYAVKVFNNLSfmRPLDVQMREFEVLKKLNHKNIVKLFAIEEELT----TRHKVLVMELC 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 245 -GLSTYDFIKE--NGF-LPFRLDHIrkMAYQICKSVNFLHSNKLTHTDLKPENIL-FVQSDYTEAYnpkikrdertlinp 319
Cdd:cd13988  76 pCGSLYTVLEEpsNAYgLPESEFLI--VLRDVVAGMNHLRENGIVHRDIKPGNIMrVIGEDGQSVY-------------- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 320 diKVVDFGSAT--YDDEHHSTLVSTRHYRAPEVI--------LALGWSQPCDVWSIGCILIEYYLGFTVF-PTHDSKEHL 388
Cdd:cd13988 140 --KLTDFGAARelEDDEQFVSLYGTEEYLHPDMYeravlrkdHQKKYGATVDLWSIGVTFYHAATGSLPFrPFEGPRRNK 217
                       250       260
                ....*....|....*....|
gi 67551261 389 AMMERILGPLPKHMIQKTRK 408
Cdd:cd13988 218 EVMYKIITGKPSGAISGVQK 237
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
161-371 4.03e-08

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: 54.24  E-value: 4.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIDhKAGGRHVAVKIVK-----NVDR---YCEAARSEiQVLEHlnttdPNstfrCVQMLEWFE 232
Cdd:cd14050   3 FTILSKLGEGSFGEVFKVRS-REDGKLYAVKRSRsrfrgEKDRkrkLEEVERHE-KLGEH-----PN----CVRFIKAWE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 233 HHGHICIVFELLGLSTYDFIKENGFLPFRldHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrd 312
Cdd:cd14050  72 EKGILYIQTELCDTSLQQYCEETHSLPES--EVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGV----------- 138
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 67551261 313 ertlinpdIKVVDFG---SATYDDEHHSTLVSTRhYRAPEVILALgWSQPCDVWSIGCILIE 371
Cdd:cd14050 139 --------CKLGDFGlvvELDKEDIHDAQEGDPR-YMAPELLQGS-FTKAADIFSLGITILE 190
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
161-420 4.27e-08

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: 55.40  E-value: 4.27e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVeCIDHKAGGRHVAVKIVknvDRYCEAARSEIQVLEHLNTTDPNSTFRCVQMLEW-FEHHGHICI 239
Cdd:cd05624  74 FEIIKVIGRGAFGEVA-VVKMKNTERIYAMKIL---NKWEMLKRAETACFREERNVLVNGDCQWITTLHYaFQDENYLYL 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 240 VFE------LLGLSTydfiKENGFLPfrLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVqsdyteaynpkikrde 313
Cdd:cd05624 150 VMDyyvggdLLTLLS----KFEDKLP--EDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLD---------------- 207
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 314 rtlINPDIKVVDFGSATYDDE----HHSTLVSTRHYRAPEVILAL-----GWSQPCDVWSIGCILIEYYLGFT------- 377
Cdd:cd05624 208 ---MNGHIRLADFGSCLKMNDdgtvQSSVAVGTPDYISPEILQAMedgmgKYGPECDWWSLGVCMYEMLYGETpfyaesl 284
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 67551261 378 --------------VFPTH------DSKEHLAMM----ERILGplpKHMIQKTRKRKYFhhDRLDWD 420
Cdd:cd05624 285 vetygkimnheerfQFPSHvtdvseEAKDLIQRLicsrERRLG---QNGIEDFKKHAFF--EGLNWE 346
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
161-366 4.43e-08

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: 54.15  E-value: 4.43e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIDhKAGGRHVAVKIVKNVDRYCEAARSEIQVLE---HLNTTDPNSTF---RCVQMLEwfehh 234
Cdd:cd14110   5 YAFQTEINRGRFSVVRQCEE-KRSGQMLAAKIIPYKPEDKQLVLREYQVLRrlsHPRIAQLHSAYlspRHLVLIE----- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 235 gHICIVFELLglstYDFIKENGFLPfrlDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrder 314
Cdd:cd14110  79 -ELCSGPELL----YNLAERNSYSE---AEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNL------------- 137
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 67551261 315 tlinpdIKVVDFGSATYDDEHHSTLVSTRHY----RAPEVILALGWSQPCDVWSIG 366
Cdd:cd14110 138 ------LKIVDLGNAQPFNQGKVLMTDKKGDyvetMAPELLEGQGAGPQTDIWAIG 187
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
161-379 4.55e-08

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: 55.01  E-value: 4.55e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVvECIDHKAGGRHVAVKIVKNVDRYceaARSEIQVL-EHLNTTDPNSTFRCVQMLEWFEHHGHICI 239
Cdd:cd05622  75 YEVVKVIGRGAFGEV-QLVRHKSTRKVYAMKLLSKFEMI---KRSDSAFFwEERDIMAFANSPWVVQLFYAFQDDRYLYM 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 240 VFELLGLSTYDFIKENGFLPFRLdhIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrdertlinp 319
Cdd:cd05622 151 VMEYMPGGDLVNLMSNYDVPEKW--ARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGH------------------ 210
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 67551261 320 dIKVVDFGSATYDDEHH----STLVSTRHYRAPEVILALG----WSQPCDVWSIGCILIEYYLGFTVF 379
Cdd:cd05622 211 -LKLADFGTCMKMNKEGmvrcDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPF 277
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
259-371 5.14e-08

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: 53.99  E-value: 5.14e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 259 PFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyTEaynpkikrdertliNPDIKVVDFGSATYDDEHHSt 338
Cdd:cd06607  97 PLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILL-----TE--------------PGTVKLADFGSASLVCPANS- 156
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 67551261 339 LVSTRHYRAPEVILALGWSQ---PCDVWSIGCILIE 371
Cdd:cd06607 157 FVGTPYWMAPEVILAMDEGQydgKVDVWSLGITCIE 192
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
161-478 6.14e-08

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: 54.24  E-value: 6.14e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVvECIDHKAGGRHVAVKIVKNVDRYCEAARS----EIQVLEHLNTtdpnstfrcvqmlEW------ 230
Cdd:cd05601   3 FEVKNVIGRGHFGEV-QVVKEKATGDIYAMKVLKKSETLAQEEVSffeeERDIMAKANS-------------PWitklqy 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 231 -FEHHGHICIVFE------LLGL-STYDFIkengflpFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyt 302
Cdd:cd05601  69 aFQDSENLYLVMEyhpggdLLSLlSRYDDI-------FEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILI------ 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 303 eaynpkikrdERTlinPDIKVVDFGSA---TYDDEHHSTL-VSTRHYRAPEVILALG------WSQPCDVWSIGCILIEY 372
Cdd:cd05601 136 ----------DRT---GHIKLADFGSAaklSSDKTVTSKMpVGTPDYIAPEVLTSMNggskgtYGVECDWWSLGIVAYEM 202
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 373 YLGFTVFpTHDSkehlammerilgplpkhmIQKTRKRKYFHHDRLDWDEHSSagryvsrrckplkefmLSQDveherLFD 452
Cdd:cd05601 203 LYGKTPF-TEDT------------------VIKTYSNIMNFKKFLKFPEDPK----------------VSES-----AVD 242
                       330       340
                ....*....|....*....|....*.
gi 67551261 453 LIQKMLEyDPAKRITLREALKHPFFD 478
Cdd:cd05601 243 LIKGLLT-DAKERLGYEGLCCHPFFS 267
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
161-414 6.80e-08

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: 53.88  E-value: 6.80e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIDHKAGgRHVAVKIVK--NVDRYCEAARSEIQVLE--HLNTTDPNSTFRCVQMLeWfehhgh 236
Cdd:cd06646  11 YELIQRVGSGTYGDVYKARNLHTG-ELAAVKIIKlePGDDFSLIQQEIFMVKEckHCNIVAYFGSYLSREKL-W------ 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFeLLGLSTYDFIKENGflPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQsdyteaynpkikrdertl 316
Cdd:cd06646  83 ICMEY-CGGGSLQDIYHVTG--PLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTD------------------ 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 317 iNPDIKVVDFGSA---TYDDEHHSTLVSTRHYRAPEVILAL---GWSQPCDVWSIGCILIEY-YLGFTVFPTHDSKEHLA 389
Cdd:cd06646 142 -NGDVKLADFGVAakiTATIAKRKSFIGTPYWMAPEVAAVEkngGYNQLCDIWAVGITAIELaELQPPMFDLHPMRALFL 220
                       250       260
                ....*....|....*....|....*
gi 67551261 390 MMERILGPlPKhMIQKTRKRKYFHH 414
Cdd:cd06646 221 MSKSNFQP-PK-LKDKTKWSSTFHN 243
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
161-371 8.99e-08

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: 53.57  E-value: 8.99e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVEcidhkagGRHVAVKIVKNVDRYCEAARSEIQVLEHLNttdpnstfrcvqMLEWFEHHGHIC-- 238
Cdd:cd06637   8 FELVELVGNGTYGQVYK-------GRHVKTGQLAAIKVMDVTGDEEEEIKQEIN------------MLKKYSHHRNIAty 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 239 -----------------IVFELLGL-STYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQsd 300
Cdd:cd06637  69 ygafikknppgmddqlwLVMEFCGAgSVTDLIKNTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTE-- 146
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 67551261 301 yteaynpkikrdertliNPDIKVVDFGSATYDDE---HHSTLVSTRHYRAPEVILA-----LGWSQPCDVWSIGCILIE 371
Cdd:cd06637 147 -----------------NAEVKLVDFGVSAQLDRtvgRRNTFIGTPYWMAPEVIACdenpdATYDFKSDLWSLGITAIE 208
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
167-371 9.93e-08

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: 53.43  E-value: 9.93e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVvecidHKA---GGRHVAVKIVKNvdRYCEA----ARSEIQVLEHLNttDPNstfrCVQMLEWFEHHGHICI 239
Cdd:cd14066   1 IGSGGFGTV-----YKGvleNGTVVAVKRLNE--MNCAAskkeFLTELEMLGRLR--HPN----LVRLLGYCLESDEKLL 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 240 VFELL-GLSTYDFIKENGFL-PFRLDHIRKMAYQICKSVNFLHS---NKLTHTDLKPENILFVQSdyteaYNPkikrder 314
Cdd:cd14066  68 VYEYMpNGSLEDRLHCHKGSpPLPWPQRLKIAKGIARGLEYLHEecpPPIIHGDIKSSNILLDED-----FEP------- 135
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 67551261 315 tlinpdiKVVDFGSA---TYDDEHHST--LVSTRHYRAPEVILALGWSQPCDVWSIGCILIE 371
Cdd:cd14066 136 -------KLTDFGLArliPPSESVSKTsaVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLE 190
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
159-371 1.01e-07

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


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 53.50  E-value: 1.01e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 159 ARYEIVDTLGEGAFGKVVEC---IDHKAggrhVAVKIVKNVDRYCEAARS----EIQVLEHLNttDPNstfrCVQMLEWF 231
Cdd:cd08229  24 ANFRIEKKIGRGQFSEVYRAtclLDGVP----VALKKVQIFDLMDAKARAdcikEIDLLKQLN--HPN----VIKYYASF 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 232 EHHGHICIVFEL-----LGLSTYDFIKENGFLPFRLdhIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYTEAyn 306
Cdd:cd08229  94 IEDNELNIVLELadagdLSRMIKHFKKQKRLIPEKT--VWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKL-- 169
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 67551261 307 pkikrdertlinPDIKVVDFGSATYDDEHhsTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIE 371
Cdd:cd08229 170 ------------GDLGLGRFFSSKTTAAH--SLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYE 220
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
167-395 1.38e-07

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: 53.05  E-value: 1.38e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVeCIDHKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTDPNSTFrCVQMLEWFEHHGHICIVFELL-- 244
Cdd:cd05603   3 IGKGSFGKVL-LAKRKCDGKFYAVKVLQKKTILKKKEQNHIMAERNVLLKNLKHPF-LVGLHYSFQTSEKLYFVLDYVng 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 245 GLSTYDFIKENGFLPFRldhIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsDYteaynpkikrdertliNPDIKVV 324
Cdd:cd05603  81 GELFFHLQRERCFLEPR---ARFYAAEVASAIGYLHSLNIIYRDLKPENILL---DC----------------QGHVVLT 138
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 67551261 325 DFG---SATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEhlaMMERIL 395
Cdd:cd05603 139 DFGlckEGMEPEETTSTFCGTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQ---MYDNIL 209
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
167-369 1.47e-07

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: 52.65  E-value: 1.47e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIDHkagGRHVAVKIVKNVDRYcEAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHGhiCIVFELLGL 246
Cdd:cd14068   2 LGDGGFGSVYRAVYR---GEDVAVKIFNKHTSF-RLLRQELVVLSHLH--HPS----LVALLAAGTAPR--MLVMELAPK 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 247 STYD--FIKENGFLPFRLDHirKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdYTEAYNPKIKrdertlinpdIKVV 324
Cdd:cd14068  70 GSLDalLQQDNASLTRTLQH--RIALHVADGLRYLHSAMIIYRDLKPHNVLL----FTLYPNCAII----------AKIA 133
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 67551261 325 DFGSATYDDEHH-STLVSTRHYRAPEVILA-LGWSQPCDVWSIGCIL 369
Cdd:cd14068 134 DYGIAQYCCRMGiKTSEGTPGFRAPEVARGnVIYNQQADVYSFGLLL 180
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
259-371 1.48e-07

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: 53.12  E-value: 1.48e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 259 PFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDyteaynpkikrdertlinpDIKVVDFGSATYDDEHHSt 338
Cdd:cd06633 117 PLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPG-------------------QVKLADFGSASIASPANS- 176
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 67551261 339 LVSTRHYRAPEVILALGWSQ---PCDVWSIGCILIE 371
Cdd:cd06633 177 FVGTPYWMAPEVILAMDEGQydgKVDIWSLGITCIE 212
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
275-391 1.69e-07

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: 52.79  E-value: 1.69e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 275 SVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrdertlinpdIKVVDFG---SATYDDEHHSTLVSTRHYRAPEVI 351
Cdd:cd05582 109 ALDHLHSLGIIYRDLKPENILLDEDGH-------------------IKLTDFGlskESIDHEKKAYSFCGTVEYMAPEVV 169
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 67551261 352 LALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMM 391
Cdd:cd05582 170 NRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMI 209
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
162-476 1.75e-07

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: 52.54  E-value: 1.75e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 162 EIVDTLGEGAFGKVVECIdHKAGGRHVAVKIVK-NVDrycEAARSeiQVLEHLNTTDPNSTFRCVQMLEWFEHHGHICIV 240
Cdd:cd06622   4 EVLDELGKGNYGSVYKVL-HRPTGVTMAMKEIRlELD---ESKFN--QIIMELDILHKAVSPYIVDFYGAFFIEGAVYMC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 241 FELLGLSTYDFIKENGFLPFRLDH--IRKMAYQICKSVNFL-HSNKLTHTDLKPENILfVQSdyteaynpkikrdertli 317
Cdd:cd06622  78 MEYMDAGSLDKLYAGGVATEGIPEdvLRRITYAVVKGLKFLkEEHNIIHRDVKPTNVL-VNG------------------ 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 318 NPDIKVVDFG-SATYDDEHHSTLVSTRHYRAPEVILALGWSQ------PCDVWSIGCILIEYYLGFTVFPTHDSKEHLAM 390
Cdd:cd06622 139 NGQVKLCDFGvSGNLVASLAKTNIGCQSYMAPERIKSGGPNQnptytvQSDVWSLGLSILEMALGRYPYPPETYANIFAQ 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 391 MERIL-GPLPkhmiqktrkrkyfhhdRLDwDEHSSAGRyvsrrckplkefmlsqdveherlfDLIQKMLEYDPAKRITLR 469
Cdd:cd06622 219 LSAIVdGDPP----------------TLP-SGYSDDAQ------------------------DFVAKCLNKIPNRRPTYA 257

                ....*..
gi 67551261 470 EALKHPF 476
Cdd:cd06622 258 QLLEHPW 264
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
161-402 1.81e-07

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: 52.69  E-value: 1.81e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVeCIDHKAGGRHVAVKIVKN----VDRYCEAARSEIQVLEhLNTTDPNSTfrcvQMLEWFEHHGH 236
Cdd:cd05616   2 FNFLMVLGKGSFGKVM-LAERKGTDELYAVKILKKdvviQDDDVECTMVEKRVLA-LSGKPPFLT----QLHSCFQTMDR 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELL-GLSTYDFIKENGflPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrdert 315
Cdd:cd05616  76 LYFVMEYVnGGDLMYHIQQVG--RFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGH-------------- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 316 linpdIKVVDFG---SATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHL-AMM 391
Cdd:cd05616 140 -----IKIADFGmckENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFqSIM 214
                       250
                ....*....|.
gi 67551261 392 ERILGpLPKHM 402
Cdd:cd05616 215 EHNVA-YPKSM 224
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
235-371 1.83e-07

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: 52.79  E-value: 1.83e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 235 GHICIVFELLGLSTYDFI---KENGFLPFRLDHIRKMAYQICKSVNFLHSNK-LTHTDLKPENILfVQSDYtEAynpkik 310
Cdd:cd14001  79 GSLCLAMEYGGKSLNDLIeerYEAGLGPFPAATILKVALSIARALEYLHNEKkILHGDIKSGNVL-IKGDF-ES------ 150
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 67551261 311 rdertlinpdIKVVDFGSATYDDEHHSTL-------VSTRHYRAPEVILALG-WSQPCDVWSIGCILIE 371
Cdd:cd14001 151 ----------VKLCDFGVSLPLTENLEVDsdpkaqyVGTEPWKAKEALEEGGvITDKADIFAYGLVLWE 209
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
161-477 1.95e-07

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


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 52.13  E-value: 1.95e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVD-TLGEGAFG---KVVEcidhKAGGRHVAVKIvknvdRYC-EAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHG 235
Cdd:cd14109   5 YEIGEeDEKRAAQGapfHVTE----RSTGRNFLAQL-----RYGdPFLMREVDIHNSLD--HPN----IVQMHDAYDDEK 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 236 HICIVFELLGlSTYDFIKENGFLP---FRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfVQSDYteaynpkikrd 312
Cdd:cd14109  70 LAVTVIDNLA-STIELVRDNLLPGkdyYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDIL-LQDDK----------- 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 313 ertlinpdIKVVDFGSA--TYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGciLIEYYL--GFTVFPTHDSKEHL 388
Cdd:cd14109 137 --------LKLADFGQSrrLLRGKLTTLIYGSPEFVSPEIVNSYPVTLATDMWSVG--VLTYVLlgGISPFLGDNDRETL 206
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 389 AmmerilgplpkhmiqKTRKRKYfHHDRLDWDEHSSAGRyvsrrckplkefmlsqdveherlfDLIQKMLEYDPAKRITL 468
Cdd:cd14109 207 T---------------NVRSGKW-SFDSSPLGNISDDAR------------------------DFIKKLLVYIPESRLTV 246

                ....*....
gi 67551261 469 REALKHPFF 477
Cdd:cd14109 247 DEALNHPWF 255
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
158-393 2.06e-07

Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Yes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 52.38  E-value: 2.06e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 158 SARYEIvdTLGEGAFGKVveCIDHKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTDPNSTFRCVQmlewfehHGHI 237
Cdd:cd05069  13 SLRLDV--KLGQGCFGEV--WMGTWNGTTKVAIKTLKPGTMMPEAFLQEAQIMKKLRHDKLVPLYAVVS-------EEPI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 238 CIVFELLGL-STYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQsdyteaynpkikrdertl 316
Cdd:cd05069  82 YIVTEFMGKgSLLDFLKEGDGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGD------------------ 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 317 iNPDIKVVDFGSATY-DDEHHSTLVSTR---HYRAPEVILALGWSQPCDVWSIGCILIEYYL-GFTVFPTHDSKEHLAMM 391
Cdd:cd05069 144 -NLVCKIADFGLARLiEDNEYTARQGAKfpiKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMVNREVLEQV 222

                ..
gi 67551261 392 ER 393
Cdd:cd05069 223 ER 224
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
271-368 2.09e-07

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


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 52.13  E-value: 2.09e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 271 QICKSVNFLHSNKLTHTDLKPENILfVQSDYTeaynpkikrdertlinpdIKVVDFGSA-TYDD---EHHSTLVSTRHYR 346
Cdd:cd14111 107 QILQGLEYLHGRRVLHLDIKPDNIM-VTNLNA------------------IKIVDFGSAqSFNPlslRQLGRRTGTLEYM 167
                        90       100
                ....*....|....*....|..
gi 67551261 347 APEVILALGWSQPCDVWSIGCI 368
Cdd:cd14111 168 APEMVKGEPVGPPADIWSIGVL 189
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
165-380 2.15e-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: 52.19  E-value: 2.15e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 165 DTLGEGAFGKVVECIdHKAGGRHVAVKIVKnVDRYCEAARSEIQVLEHLnttdpnstFRCVQ--MLEWF-----EHHGHI 237
Cdd:cd06619   7 EILGHGNGGTVYKAY-HLLTRRILAVKVIP-LDITVELQKQIMSELEIL--------YKCDSpyIIGFYgaffvENRISI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 238 CIVFELLG-LSTYDFIKENgflpfrldHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqsdyteaynpkikrdertl 316
Cdd:cd06619  77 CTEFMDGGsLDVYRKIPEH--------VLGRIAVAVVKGLTYLWSLKILHRDVKPSNML--------------------- 127
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 67551261 317 INP--DIKVVDFGSAT-YDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFP 380
Cdd:cd06619 128 VNTrgQVKLCDFGVSTqLVNSIAKTYVGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGRFPYP 194
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
160-480 2.17e-07

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: 52.30  E-value: 2.17e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDHKAGGRHVAVKIVKNVDRYCEAARSEIQVleHLNTTDPN---STFRCVQMLEWFEHHGH 236
Cdd:cd13986   1 RYRIQRLLGEGGFSFVYLVEDLSTGRLYALKKILCHSKEDVKEAMREIEN--YRLFNHPNilrLLDSQIVKEAGGKKEVY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELLGlSTYDFI----KENGFLPF-RLDHIRKmayQICKSVNFLHSNKL---THTDLKPENILFvqSDyteaynpk 308
Cdd:cd13986  79 LLLPYYKRG-SLQDEIerrlVKGTFFPEdRILHIFL---GICRGLKAMHEPELvpyAHRDIKPGNVLL--SE-------- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 309 ikrdertliNPDIKVVDFGSATYD----------------DEHHSTLVstrhYRAPE--------VIlalgwSQPCDVWS 364
Cdd:cd13986 145 ---------DDEPILMDLGSMNPArieiegrrealalqdwAAEHCTMP----YRAPElfdvkshcTI-----DEKTDIWS 206
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 365 IGCILieYYLGFTVFPthdskehlamMERILGplpkhmiqktrkrkyfHHDrldwdehSSAGRYVSRRCKPLKEFMLSQD 444
Cdd:cd13986 207 LGCTL--YALMYGESP----------FERIFQ----------------KGD-------SLALAVLSGNYSFPDNSRYSEE 251
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 67551261 445 veherLFDLIQKMLEYDPAKRITLREALKHpfFDLL 480
Cdd:cd13986 252 -----LHQLVKSMLVVNPAERPSIDDLLSR--VHDL 280
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
161-388 2.64e-07

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: 52.72  E-value: 2.64e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVeCIDHKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTDPNSTFrCVQMLEWFEHHGHICIV 240
Cdd:cd05617  17 FDLIRVIGRGSYAKVL-LVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPF-LVGLHSCFQTTSRLFLV 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 241 FELLGLSTYDF-IKENGFLPfrLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrdertlinp 319
Cdd:cd05617  95 IEYVNGGDLMFhMQRQRKLP--EEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGH------------------ 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 67551261 320 dIKVVDFG---SATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVF------PTHDSKEHL 388
Cdd:cd05617 155 -IKLTDYGmckEGLGPGDTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFdiitdnPDMNTEDYL 231
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
259-476 2.96e-07

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK1, also called CaMKK alpha, is involved in the regulation of glucose uptake in skeletal muscles, independently of AMPK and PKB activation. It also play roles in learning and memory. Studies on CaMKK1 knockout mice reveal deficits in fear conditioning. The CaMKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 51.87  E-value: 2.96e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 259 PFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrdertlinpdIKVVDFGSATY---DDEH 335
Cdd:cd14200 120 PFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDDGH-------------------VKIADFGVSNQfegNDAL 180
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 336 HSTLVSTRHYRAPEVILALGWS---QPCDVWSIGCILIEYYLGFTVFpthdskehlaMMERILGplpkhmiqktrkrkyf 412
Cdd:cd14200 181 LSSTAGTPAFMAPETLSDSGQSfsgKALDVWAMGVTLYCFVYGKCPF----------IDEFILA---------------- 234
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 67551261 413 HHDRLdwdehssagryvsrRCKPLkEFMLSQDVEHErLFDLIQKMLEYDPAKRITLREALKHPF 476
Cdd:cd14200 235 LHNKI--------------KNKPV-EFPEEPEISEE-LKDLILKMLDKNPETRITVPEIKVHPW 282
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
160-381 3.45e-07

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: 51.65  E-value: 3.45e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVV-----ECIDHKAGGRHVAVKIVKN--VDRYCEAARSEIQVL----EHLNTTdpNSTFRCVQ-- 226
Cdd:cd05053  13 RLTLGKPLGEGAFGQVVkaeavGLDNKPNEVVTVAVKMLKDdaTEKDLSDLVSEMEMMkmigKHKNII--NLLGACTQdg 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 227 ----MLEwFEHHGHIcivfellglstYDFIK-------ENGFLPFR-------LDHIRKMAYQICKSVNFLHSNKLTHTD 288
Cdd:cd05053  91 plyvVVE-YASKGNL-----------REFLRarrppgeEASPDDPRvpeeqltQKDLVSFAYQVARGMEYLASKKCIHRD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 289 LKPENILfVQSDYTeaynpkikrdertlinpdIKVVDFGSATydDEHHSTlvstrHYR------------APEVILALGW 356
Cdd:cd05053 159 LAARNVL-VTEDNV------------------MKIADFGLAR--DIHHID-----YYRkttngrlpvkwmAPEALFDRVY 212
                       250       260
                ....*....|....*....|....*.
gi 67551261 357 SQPCDVWSIGCILIEYY-LGFTVFPT 381
Cdd:cd05053 213 THQSDVWSFGVLLWEIFtLGGSPYPG 238
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
263-477 4.05e-07

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: 51.56  E-value: 4.05e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 263 DHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQsdyteaynpkikrDERtlinpdIKVVDFG---SATYDDEHHSTL 339
Cdd:cd06657 116 EQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTH-------------DGR------VKLSDFGfcaQVSKEVPRRKSL 176
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 340 VSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGftvFPTHDSKEHLAMMERILGPLPKhmiqktrKRKYFHhdrldw 419
Cdd:cd06657 177 VGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDG---EPPYFNEPPLKAMKMIRDNLPP-------KLKNLH------ 240
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 67551261 420 dehssagryvsrRCKPLkefmlsqdveherLFDLIQKMLEYDPAKRITLREALKHPFF 477
Cdd:cd06657 241 ------------KVSPS-------------LKGFLDRLLVRDPAQRATAAELLKHPFL 273
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
167-479 4.34e-07

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: 51.58  E-value: 4.34e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVveCI-DHKAGGRHVAVK---IVKNVDRycEAARSEIQVLE---HLNTTDPNSTFRCVQMLeWfehhghicI 239
Cdd:cd06658  30 IGEGSTGIV--CIaTEKHTGKQVAVKkmdLRKQQRR--ELLFNEVVIMRdyhHENVVDMYNSYLVGDEL-W--------V 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 240 VFELLglstydfikENGFLPFRLDHIRKMAYQIC-------KSVNFLHSNKLTHTDLKPENILFVQsdyteaynpkikrD 312
Cdd:cd06658  97 VMEFL---------EGGALTDIVTHTRMNEEQIAtvclsvlRALSYLHNQGVIHRDIKSDSILLTS-------------D 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 313 ERtlinpdIKVVDFG---SATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGftvFPTHDSKEHLA 389
Cdd:cd06658 155 GR------IKLSDFGfcaQVSKEVPKRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDG---EPPYFNEPPLQ 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 390 MMERILGPLPKHMiqktrkrKYFHhdrldwdehssagryvsRRCKPLKEFMlsqdveherlfDLiqkMLEYDPAKRITLR 469
Cdd:cd06658 226 AMRRIRDNLPPRV-------KDSH-----------------KVSSVLRGFL-----------DL---MLVREPSQRATAQ 267
                       330
                ....*....|
gi 67551261 470 EALKHPFFDL 479
Cdd:cd06658 268 ELLQHPFLKL 277
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
167-371 4.52e-07

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: 51.23  E-value: 4.52e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVEC---IDHKAGGRHVAVKIVK--NVDRYCEAARSEIQVLEHLNTtdPNstfrCVQMLEWFEHHGH--ICI 239
Cdd:cd05038  12 LGEGHFGSVELCrydPLGDNTGEQVAVKSLQpsGEEQHMSDFKREIEILRTLDH--EY----IVKYKGVCESPGRrsLRL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 240 VFELLGLSTYDfikenGFLPF---RLDHIR--KMAYQICKSVNFLHSNKLTHTDLKPENILfVQSDYTeaynpkikrder 314
Cdd:cd05038  86 IMEYLPSGSLR-----DYLQRhrdQIDLKRllLFASQICKGMEYLGSQRYIHRDLAARNIL-VESEDL------------ 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 67551261 315 tlinpdIKVVDFGSATYDDEHHSTLVSTR------HYRAPEVILALGWSQPCDVWSIGCILIE 371
Cdd:cd05038 148 ------VKISDFGLAKVLPEDKEYYYVKEpgespiFWYAPECLRESRFSSASDVWSFGVTLYE 204
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
167-477 4.57e-07

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: 51.24  E-value: 4.57e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVecIDHKAGGRHV----AVKIVKNVD-----RYCEAARSEIQVLEHLNttdpNSTFrCVQMLEWFEHHGHI 237
Cdd:cd05583   2 LGTGAYGKVF--LVRKVGGHDAgklyAMKVLKKATivqkaKTAEHTMTERQVLEAVR----QSPF-LVTLHYAFQTDAKL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 238 CIVFELLG---LSTYDFIKEngflPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrder 314
Cdd:cd05583  75 HLILDYVNggeLFTHLYQRE----HFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGH------------- 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 315 tlinpdIKVVDFG-SATY----DDEHHStLVSTRHYRAPEVILA--LGWSQPCDVWSIGCILIEYYLGFTVFPTHDSK-E 386
Cdd:cd05583 138 ------VVLTDFGlSKEFlpgeNDRAYS-FCGTIEYMAPEVVRGgsDGHDKAVDWWSLGVLTYELLTGASPFTVDGERnS 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 387 HLAMMERILG---PLPKHMiqktrkrkyfhhdrldwdehssagryvSRRCKplkefmlsqdveherlfDLIQKMLEYDPA 463
Cdd:cd05583 211 QSEISKRILKshpPIPKTF---------------------------SAEAK-----------------DFILKLLEKDPK 246
                       330
                ....*....|....*....
gi 67551261 464 KRI-----TLREALKHPFF 477
Cdd:cd05583 247 KRLgagprGAHEIKEHPFF 265
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
250-380 5.86e-07

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: 51.56  E-value: 5.86e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 250 DFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSdyteaynpKIkrdertlinpdIKVVDFGSA 329
Cdd:cd05105 224 NLLSDDGSEGLTTLDLLSFTYQVARGMEFLASKNCVHRDLAARNVLLAQG--------KI-----------VKICDFGLA 284
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 67551261 330 TyDDEHHSTLVSTR------HYRAPEVILALGWSQPCDVWSIGCILIEYY-LGFTVFP 380
Cdd:cd05105 285 R-DIMHDSNYVSKGstflpvKWMAPESIFDNLYTTLSDVWSYGILLWEIFsLGGTPYP 341
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
269-375 6.23e-07

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: 50.80  E-value: 6.23e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 269 AYQICKSVNFLHSNKLT---HTDLKPENILFVQSDYTEAYnpkikrDERTLinpdiKVVDFGSATydDEHHSTLVS---T 342
Cdd:cd14147 107 AVQIARGMHYLHCEALVpviHRDLKSNNILLLQPIENDDM------EHKTL-----KITDFGLAR--EWHKTTQMSaagT 173
                        90       100       110
                ....*....|....*....|....*....|...
gi 67551261 343 RHYRAPEVILALGWSQPCDVWSIGCILIEYYLG 375
Cdd:cd14147 174 YAWMAPEVIKASTFSKGSDVWSFGVLLWELLTG 206
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
167-407 6.83e-07

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: 51.25  E-value: 6.83e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKV--VECIDHKAGGRHVAVKIVKN---VDRYCEAA--RSEIQVLEHLNttdpnSTFrCVQMLEWFEHHGHICI 239
Cdd:cd05584   4 LGKGGYGKVfqVRKTTGSDKGKIFAMKVLKKasiVRNQKDTAhtKAERNILEAVK-----HPF-IVDLHYAFQTGGKLYL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 240 VFELL-GLSTYDFIKENGFLP-----FRLDhirkmayQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrde 313
Cdd:cd05584  78 ILEYLsGGELFMHLEREGIFMedtacFYLA-------EITLALGHLHSLGIIYRDLKPENILLDAQGH------------ 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 314 rtlinpdIKVVDFG---SATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAM 390
Cdd:cd05584 139 -------VKLTDFGlckESIHDGTVTHTFCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDK 211
                       250
                ....*....|....*..
gi 67551261 391 MERILGPLPKHMIQKTR 407
Cdd:cd05584 212 ILKGKLNLPPYLTNEAR 228
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
167-393 6.92e-07

Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes a subset of Src-like PTKs including Src, Fyn, Yrk, and Yes, which are all widely expressed. Yrk has been detected only in chickens. It is primarily found in neuronal and epithelial cells and in macrophages. It may play a role in inflammation and in response to injury. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. They are also implicated in acute inflammatory responses and osteoclast function. The Src/Fyn-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 50.30  E-value: 6.92e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVveCIDHKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTdpnstfRCVQMLEWFEHHGhICIVFELLGL 246
Cdd:cd14203   3 LGQGCFGEV--WMGTWNGTTKVAIKTLKPGTMSPEAFLEEAQIMKKLRHD------KLVQLYAVVSEEP-IYIVTEFMSK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 247 -STYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQsdyteaynpkikrdertliNPDIKVVD 325
Cdd:cd14203  74 gSLLDFLKDGEGKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGD-------------------NLVCKIAD 134
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 67551261 326 FGSATY--DDEHHSTLVSTR--HYRAPEVILALGWSQPCDVWSIGCILIEYYL-GFTVFPTHDSKEHLAMMER 393
Cdd:cd14203 135 FGLARLieDNEYTARQGAKFpiKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQVER 207
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
161-476 8.41e-07

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


Pssm-ID: 271019 [Multi-domain]  Cd Length: 270  Bit Score: 50.25  E-value: 8.41e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVeCIDHKAGGRHVAVKIVKNVDRYCEAA----RSEIQVLEHLNttDPNstfrCVQMLEWFEHHGH 236
Cdd:cd14117   8 FDIGRPLGKGKFGNVY-LAREKQSKFIVALKVLFKSQIEKEGVehqlRREIEIQSHLR--HPN----ILRLYNYFHDRKR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELLGLST-YDFIKENGflpfRLDHIRKMAY--QICKSVNFLHSNKLTHTDLKPENILFVqsdyteaynpkikrde 313
Cdd:cd14117  81 IYLILEYAPRGElYKELQKHG----RFDEQRTATFmeELADALHYCHEKKVIHRDIKPENLLMG---------------- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 314 rtlINPDIKVVDFG-SATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGftvFPTHDSKEHLAMME 392
Cdd:cd14117 141 ---YKGELKIADFGwSVHAPSLRRRTMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVG---MPPFESASHTETYR 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 393 RILG---PLPKHMIQKTRkrkyfhhdrldwdehssagryvsrrckplkefmlsqdveherlfDLIQKMLEYDPAKRITLR 469
Cdd:cd14117 215 RIVKvdlKFPPFLSDGSR--------------------------------------------DLISKLLRYHPSERLPLK 250

                ....*..
gi 67551261 470 EALKHPF 476
Cdd:cd14117 251 GVMEHPW 257
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
142-477 9.61e-07

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 51.00  E-value: 9.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  142 EDDEEGHLICQSGDVLSA---RYEIVDTLGEGAFGKVVECIDH-KAGGRHVAVKIV---KNVDRyceaarsEIQVLEHLN 214
Cdd:PHA03207  72 DVCQEPCETTSSSDPASVvrmQYNILSSLTPGSEGEVFVCTKHgDEQRKKVIVKAVtggKTPGR-------EIDILKTIS 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  215 TTDpnstfrCVQMLEWFEHHGHICIVFELLGLSTYDFIKENGFLPfrLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENI 294
Cdd:PHA03207 145 HRA------IINLIHAYRWKSTVCMVMPKYKCDLFTYVDRSGPLP--LEQAITIQRRLLEALAYLHGRGIIHRDVKTENI 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  295 LfvqsdyteaynpkikrdertLINPDIKVV-DFGSATYDDEHHST-----LVSTRHYRAPEvILALG-WSQPCDVWSIGC 367
Cdd:PHA03207 217 F--------------------LDEPENAVLgDFGAACKLDAHPDTpqcygWSGTLETNSPE-LLALDpYCAKTDIWSAGL 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  368 ILIEYYLGFTVFPTHDSKEHLAMMERILGPLPKHMIQ-----KTRKRKYFhhdrldwdehssaGRYVSRRCKP------L 436
Cdd:PHA03207 276 VLFEMSVKNVTLFGKQVKSSSSQLRSIIRCMQVHPLEfpqngSTNLCKHF-------------KQYAIVLRPPytippvI 342
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 67551261  437 KEFMLSQDVEHerlfdLIQKMLEYDPAKRITLREALKHPFF 477
Cdd:PHA03207 343 RKYGMHMDVEY-----LIAKMLTFDQEFRPSAQDILSLPLF 378
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
167-393 1.10e-06

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: 49.97  E-value: 1.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVvecidHKA---GGRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTdpnstfRCVQMLEWFEHHGHICIVFEL 243
Cdd:cd05034   3 LGAGQFGEV-----WMGvwnGTTKVAVKTLKPGTMSPEAFLQEAQIMKKLRHD------KLVQLYAVCSDEEPIYIVTEL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 244 L--GlSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteaynpkikrDErtliNPDI 321
Cdd:cd05034  72 MskG-SLLDYLRTGEGRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILV---------------GE----NNVC 131
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 67551261 322 KVVDFGSATY--DDE---HHSTLVSTRhYRAPEVILALGWSQPCDVWSIGCILIEYY-LGFTVFPTHDSKEHLAMMER 393
Cdd:cd05034 132 KVADFGLARLieDDEytaREGAKFPIK-WTAPEAALYGRFTIKSDVWSFGILLYEIVtYGRVPYPGMTNREVLEQVER 208
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
166-380 1.38e-06

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: 49.96  E-value: 1.38e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 166 TLGEGAFGKVVEC----IDHKAGGRHVAVKIVKNVDRYCE--AARSEIQVLEHLN----------TTDPNSTFRCVQMLE 229
Cdd:cd05045   7 TLGEGEFGKVVKAtafrLKGRAGYTTVAVKMLKENASSSElrDLLSEFNLLKQVNhphviklygaCSQDGPLLLIVEYAK 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 230 WFEHHGHI-------CIVFELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDyt 302
Cdd:cd05045  87 YGSLRSFLresrkvgPSYLGSDGNRNSSYLDNPDERALTMGDLISFAWQISRGMQYLAEMKLVHRDLAARNVLVAEGR-- 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 303 eaynpkikrdertlinpDIKVVDFGSA--TYDDEHHSTLVSTR---HYRAPEVILALGWSQPCDVWSIGCILIEYY-LGF 376
Cdd:cd05045 165 -----------------KMKISDFGLSrdVYEEDSYVKRSKGRipvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVtLGG 227

                ....
gi 67551261 377 TVFP 380
Cdd:cd05045 228 NPYP 231
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
250-380 1.43e-06

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. 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: 50.00  E-value: 1.43e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 250 DFIKEngflPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQsdyteaynpkikrdertliNPDIKVVDFGSA 329
Cdd:cd14207 171 DFYKR----PLTMEDLISYSFQVARGMEFLSSRKCIHRDLAARNILLSE-------------------NNVVKICDFGLA 227
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 67551261 330 --TYDDEHHSTLVSTR---HYRAPEVILALGWSQPCDVWSIGCILIEYY-LGFTVFP 380
Cdd:cd14207 228 rdIYKNPDYVRKGDARlplKWMAPESIFDKIYSTKSDVWSYGVLLWEIFsLGASPYP 284
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
161-371 1.98e-06

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: 49.36  E-value: 1.98e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIdhKAGGRHVAVKIVKNVDRYC-EAARSEIQVLEHLnttdpnstfrcvqmlewfeHHGHICI 239
Cdd:cd05148   8 FTLERKLGSGYFGEVWEGL--WKNRVRVAIKILKSDDLLKqQDFQKEVQALKRL-------------------RHKHLIS 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 240 VFELLGLSTYDFI----KENGFL----------PFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfVQSDYTeay 305
Cdd:cd05148  67 LFAVCSVGEPVYIitelMEKGSLlaflrspegqVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNIL-VGEDLV--- 142
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 306 npkikrdertlinpdIKVVDFGSATYDDEH----HSTLVSTRhYRAPEVILALGWSQPCDVWSIGCILIE 371
Cdd:cd05148 143 ---------------CKVADFGLARLIKEDvylsSDKKIPYK-WTAPEAASHGTFSTKSDVWSFGILLYE 196
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
259-371 2.28e-06

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: 49.28  E-value: 2.28e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 259 PFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDyteaynpkikrdertlinpDIKVVDFGSATYDDEHHSt 338
Cdd:cd06635 121 PLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPG-------------------QVKLADFGSASIASPANS- 180
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 67551261 339 LVSTRHYRAPEVILALGWSQ---PCDVWSIGCILIE 371
Cdd:cd06635 181 FVGTPYWMAPEVILAMDEGQydgKVDVWSLGITCIE 216
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
167-295 2.71e-06

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 46.67  E-value: 2.71e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIdHKAGGRHVAVKIVKNVDR-YCEAARSEIQVLEHLNTTDPNStfrcVQMLEWFEHHGHICIVFELL- 244
Cdd:cd13968   1 MGEGASAKVFWAE-GECTTIGVAVKIGDDVNNeEGEDLESEMDILRRLKGLELNI----PKVLVTEDVDGPNILLMELVk 75
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 67551261 245 GLSTYDFIKENgfLPFRLDhIRKMAYQICKSVNFLHSNKLTHTDLKPENIL 295
Cdd:cd13968  76 GGTLIAYTQEE--ELDEKD-VESIMYQLAECMRLLHSFHLIHRDLNNDNIL 123
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
279-386 2.75e-06

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: 49.11  E-value: 2.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 279 LHSNKLTHTDLKPENILFvqsdytEAynpkikrdertliNPDIKVVDFGSAT---YDDEHHSTLVSTRHYRAPEVIL-AL 354
Cdd:cd05586 112 LHKNDIVYRDLKPENILL------DA-------------NGHIALCDFGLSKadlTDNKTTNTFCGTTEYLAPEVLLdEK 172
                        90       100       110
                ....*....|....*....|....*....|..
gi 67551261 355 GWSQPCDVWSIGCILIEYYLGFTVFPTHDSKE 386
Cdd:cd05586 173 GYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQ 204
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
158-393 3.48e-06

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


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 48.53  E-value: 3.48e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 158 SARYEIvdTLGEGAFGKVveCIDHKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTdpnstfRCVQMLEWFEHHGhI 237
Cdd:cd05071  10 SLRLEV--KLGQGCFGEV--WMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHE------KLVQLYAVVSEEP-I 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 238 CIVFELLGL-STYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQsdyteaynpkikrdertl 316
Cdd:cd05071  79 YIVTEYMSKgSLLDFLKGEMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGE------------------ 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 317 iNPDIKVVDFGSATY-DDEHHSTLVSTR---HYRAPEVILALGWSQPCDVWSIGCILIEYYL-GFTVFPTHDSKEHLAMM 391
Cdd:cd05071 141 -NLVCKVADFGLARLiEDNEYTARQGAKfpiKWTAPEAALYGRFTIKSDVWSFGILLTELTTkGRVPYPGMVNREVLDQV 219

                ..
gi 67551261 392 ER 393
Cdd:cd05071 220 ER 221
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
167-395 4.32e-06

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: 48.75  E-value: 4.32e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVeCIDHKAGGRHVAVKIVKN----VDRYCEAARSEIQVLEhLNTTDPNST--FRCVQMLEwfehhgHICIV 240
Cdd:cd05590   3 LGKGSFGKVM-LARLKESGRLYAVKVLKKdvilQDDDVECTMTEKRILS-LARNHPFLTqlYCCFQTPD------RLFFV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 241 FELLglstydfikENGFLPF------RLDHIRKMAY--QICKSVNFLHSNKLTHTDLKPENILFVQSDYTeaynpkikrd 312
Cdd:cd05590  75 MEFV---------NGGDLMFhiqksrRFDEARARFYaaEITSALMFLHDKGIIYRDLKLDNVLLDHEGHC---------- 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 313 ertlinpdiKVVDFG---SATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEhla 389
Cdd:cd05590 136 ---------KLADFGmckEGIFNGKTTSTFCGTPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDD--- 203

                ....*.
gi 67551261 390 MMERIL 395
Cdd:cd05590 204 LFEAIL 209
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
167-371 4.83e-06

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


Pssm-ID: 270964 [Multi-domain]  Cd Length: 253  Bit Score: 47.77  E-value: 4.83e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIDHKAggrhVAVKIVKNVDRYCE---AARSEIQVLE---HLN-------TTDPNSTFrcvqMLEWFE- 232
Cdd:cd14062   1 IGSGSFGTVYKGRWHGD----VAVKKLNVTDPTPSqlqAFKNEVAVLRktrHVNillfmgyMTKPQLAI----VTQWCEg 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 233 ----HHGHICIV-FELLGLstydfikengflpfrLDhirkMAYQICKSVNFLHSNKLTHTDLKPENIlFVQSDYTeaynp 307
Cdd:cd14062  73 sslyKHLHVLETkFEMLQL---------------ID----IARQTAQGMDYLHAKNIIHRDLKSNNI-FLHEDLT----- 127
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 67551261 308 kikrdertlinpdIKVVDFGSATYddehhSTLVSTRHYR----------APEVILALG---WSQPCDVWSIGCILIE 371
Cdd:cd14062 128 -------------VKIGDFGLATV-----KTRWSGSQQFeqptgsilwmAPEVIRMQDenpYSFQSDVYAFGIVLYE 186
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
161-327 5.90e-06

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: 48.12  E-value: 5.90e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIDHKAG--GRHVAVKIVKnvdrycEAARSEIQVLEHLNTTDPNSTFRcvqmlewfEHHGHIC 238
Cdd:cd13981   2 YVISKELGEGGYASVYLAKDDDEQsdGSLVALKVEK------PPSIWEFYICDQLHSRLKNSRLR--------ESISGAH 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 239 IVFELLGLSTY-DFIKENGFLpfrLDHIRKM----------------AYQICKSVNFLHSNKLTHTDLKPENILF----- 296
Cdd:cd13981  68 SAHLFQDESILvMDYSSQGTL---LDVVNKMknktgggmdeplamffTIELLKVVEALHEVGIIHGDIKPDNFLLrleic 144
                       170       180       190
                ....*....|....*....|....*....|.
gi 67551261 297 VQSDYTEAYNPKikrdertliNPDIKVVDFG 327
Cdd:cd13981 145 ADWPGEGENGWL---------SKGLKLIDFG 166
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
161-478 7.15e-06

Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like kinase (also called greatwall kinase); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MASTL kinases in this group carry only a catalytic domain, which contains a long insertion relative to MAST kinases. MASTL, also called greatwall kinase (Gwl), is involved in the regulation of mitotic entry, which is controlled by the coordinated activities of protein kinases and opposing protein phosphatases (PPs). The cyclin B/CDK1 complex induces entry into M-phase while PP2A-B55 shows anti-mitotic activity. MASTL/Gwl is activated downstream of cyclin B/CDK1 and indirectly inhibits PP2A-B55 by phosphorylating the small protein alpha-endosulfine (Ensa) or the cAMP-regulated phosphoprotein 19 (Arpp19), resulting in M-phase progression. Gwl kinase may also play roles in mRNA stabilization and DNA checkpoint recovery. The human MASTL gene has also been named FLJ14813; a missense mutation in FLJ14813 is associated with autosomal dominant thrombocytopenia. The MASTL kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 47.95  E-value: 7.15e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVeCIDHKAGGRHVAVKIVKNVDRYCEAARSEIQVlEHLNTTDPNSTFrCVQMLEWFEHHGHICIV 240
Cdd:cd05610   6 FVIVKPISRGAFGKVY-LGRKKNNSKLYAVKVVKKADMINKNMVHQVQA-ERDALALSKSPF-IVHLYYSLQSANNVYLV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 241 FE-LLGLSTYDFIKENGFlpFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDY---TEAYNPKIKRDeRTL 316
Cdd:cd05610  83 MEyLIGGDVKSLLHIYGY--FDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHiklTDFGLSKVTLN-REL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 317 INPDI--------------------------------------KVVDFGSATYDDEHhstLVSTRHYRAPEVILALGWSQ 358
Cdd:cd05610 160 NMMDIlttpsmakpkndysrtpgqvlslisslgfntptpyrtpKSVRRGAARVEGER---ILGTPDYLAPELLLGKPHGP 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 359 PCDVWSIGCILIEYYLGftVFPTHDSKehlammerilgplPKHMIQKTRKRKyfhhdrLDWdehssagryvsrrckPLKE 438
Cdd:cd05610 237 AVDWWALGVCLFEFLTG--IPPFNDET-------------PQQVFQNILNRD------IPW---------------PEGE 280
                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 67551261 439 FMLSQDVEherlfDLIQKMLEYDPAKRITLREALKHPFFD 478
Cdd:cd05610 281 EELSVNAQ-----NAIEILLTMDPTKRAGLKELKQHPLFH 315
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
167-373 7.33e-06

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: 47.70  E-value: 7.33e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVEC-ID--HKAGGRHVAVKIVKN-VDRYCEAARSEIQVLEHLNTtDPNSTFRCVQmleWFEHHGHICIVFE 242
Cdd:cd14205  12 LGKGNFGSVEMCrYDplQDNTGEVVAVKKLQHsTEEHLRDFEREIEILKSLQH-DNIVKYKGVC---YSAGRRNLRLIME 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 243 LLGL-STYDFIKENgflPFRLDHIRKMAY--QICKSVNFLHSNKLTHTDLKPENILfVQSDYTeaynpkikrdertlinp 319
Cdd:cd14205  88 YLPYgSLRDYLQKH---KERIDHIKLLQYtsQICKGMEYLGTKRYIHRDLATRNIL-VENENR----------------- 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 320 dIKVVDFGSATY---DDEHHSTL---VSTRHYRAPEVILALGWSQPCDVWSIGCILIEYY 373
Cdd:cd14205 147 -VKIGDFGLTKVlpqDKEYYKVKepgESPIFWYAPESLTESKFSVASDVWSFGVVLYELF 205
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
167-371 7.53e-06

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: 47.49  E-value: 7.53e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVEcIDHKAGGRHVAVKIVKNVDRYCEAARsEIQVLEHLntTDPNstfrCVQMLEWFEHHGHICIVFELLGL 246
Cdd:cd14065   1 LGKGFFGEVYK-VTHRETGKVMVMKELKRFDEQRSFLK-EVKLMRRL--SHPN----ILRFIGVCVKDNKLNFITEYVNG 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 247 STYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteaynpKIKRDERTLINPDI----K 322
Cdd:cd14065  73 GTLEELLKSMDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLV-----------REANRGRNAVVADFglarE 141
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 67551261 323 VVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIE 371
Cdd:cd14065 142 MPDEKTKKPDRKKRLTVVGSPYWMAPEMLRGESYDEKVDVFSFGIVLCE 190
pknD PRK13184
serine/threonine-protein kinase PknD;
271-369 8.96e-06

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 48.23  E-value: 8.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  271 QICKSVNFLHSNKLTHTDLKPENILF------VQSDYTEAYNPKIKRDERTLINPDIKVVDFGSATYDDEhhstLVSTRH 344
Cdd:PRK13184 121 KICATIEYVHSKGVLHRDLKPDNILLglfgevVILDWGAAIFKKLEEEDLLDIDVDERNICYSSMTIPGK----IVGTPD 196
                         90       100
                 ....*....|....*....|....*
gi 67551261  345 YRAPEVILALGWSQPCDVWSIGCIL 369
Cdd:PRK13184 197 YMAPERLLGVPASESTDIYALGVIL 221
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
167-371 1.10e-05

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: 46.95  E-value: 1.10e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIDHKAGGRH--VAVKIVKNvdryceaarseiqvlEHLNTTDPNSTFRC-VQMLEWFEHHGHI------ 237
Cdd:cd05040   3 LGDGSFGVVRRGEWTTPSGKViqVAVKCLKS---------------DVLSQPNAMDDFLKeVNAMHSLDHPNLIrlygvv 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 238 -----CIVFELLGL-STYDFIKENG--FLPFRLDHirkMAYQICKSVNFLHSNKLTHTDLKPENILfvqsdyteaynpki 309
Cdd:cd05040  68 lssplMMVTELAPLgSLLDRLRKDQghFLISTLCD---YAVQIANGMAYLESKRFIHRDLAARNIL-------------- 130
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 67551261 310 krdertLINPD-IKVVDFGSATYDDEHHSTLVSTRHYR------APEVILALGWSQPCDVWSIGCILIE 371
Cdd:cd05040 131 ------LASKDkVKIGDFGLMRALPQNEDHYVMQEHRKvpfawcAPESLKTRKFSHASDVWMFGVTLWE 193
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
167-404 1.26e-05

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: 46.74  E-value: 1.26e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVvECIDHKAGGRHVAVKIVKN-VDRycEAARSEIQVLEHLntTDPNstfrCVQMLEWFEHHGHICIVFELLG 245
Cdd:cd14156   1 IGSGFFSKV-YKVTHGATGKVMVVKIYKNdVDQ--HKIVREISLLQKL--SHPN----IVRYLGICVKDEKLHPILEYVS 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 246 LSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILF-VQSDYTEAYnpkikrdertlinpdikVV 324
Cdd:cd14156  72 GGCLEELLAREELPLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIrVTPRGREAV-----------------VT 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 325 DFGSA-------TYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFP-----THDSKEHLAMME 392
Cdd:cd14156 135 DFGLArevgempANDPERKLSLVGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEILARIPADPevlprTGDFGLDVQAFK 214
                       250
                ....*....|..
gi 67551261 393 RILGPLPKHMIQ 404
Cdd:cd14156 215 EMVPGCPEPFLD 226
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
269-433 1.34e-05

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: 47.31  E-value: 1.34e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 269 AYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrdertlinpdIKVVDFGSATyDDEHHSTLVST------ 342
Cdd:cd05107 245 SYQVANGMEFLASKNCVHRDLAARNVLICEGKL-------------------VKICDFGLAR-DIMRDSNYISKgstflp 304
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 343 RHYRAPEVILALGWSQPCDVWSIGCILIEYY-LGFTVFPthdskeHLAMMERILGPLpkhmiqktrKRKYfhhdRLDWDE 421
Cdd:cd05107 305 LKWMAPESIFNNLYTTLSDVWSFGILLWEIFtLGGTPYP------ELPMNEQFYNAI---------KRGY----RMAKPA 365
                       170
                ....*....|...
gi 67551261 422 HSSAGRY-VSRRC 433
Cdd:cd05107 366 HASDEIYeIMQKC 378
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
160-399 1.50e-05

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 47.56  E-value: 1.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  160 RYEIVDTLGEGAFGKVVeCIDHKAGGRHVAVKIVkNVDRYCEA----ARSEIQVL------------EHLNTTDPNSTfR 223
Cdd:PTZ00283  33 KYWISRVLGSGATGTVL-CAKRVSDGEPFAVKVV-DMEGMSEAdknrAQAEVCCLlncdffsivkchEDFAKKDPRNP-E 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  224 CVQMlewfehhghICIVFELLGLStyDFIKE-----NGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQ 298
Cdd:PTZ00283 110 NVLM---------IALVLDYANAG--DLRQEiksraKTNRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCS 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  299 sdyteaynpkikrdertliNPDIKVVDFG-----SATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYy 373
Cdd:PTZ00283 179 -------------------NGLVKLGDFGfskmyAATVSDDVGRTFCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYEL- 238
                        250       260       270
                 ....*....|....*....|....*....|
gi 67551261  374 lgFTVFPTHDSKEHLAMMERILG----PLP 399
Cdd:PTZ00283 239 --LTLKRPFDGENMEEVMHKTLAgrydPLP 266
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
259-477 1.66e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 47.19  E-value: 1.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  259 PFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqsdyteaynpkikrdertlIN--PDIKVVDFGSATYDDEHH 336
Cdd:PHA03211 256 PLGLAQVTAVARQLLSAIDYIHGEGIIHRDIKTENVL---------------------VNgpEDICLGDFGAACFARGSW 314
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  337 ST-----LVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYL-GFTVFPTHDSKEHLAMMERILgplpkHMIQKTRkrk 410
Cdd:PHA03211 315 STpfhygIAGTVDTNAPEVLAGDPYTPSVDIWSAGLVIFEAAVhTASLFSASRGDERRPYDAQIL-----RIIRQAQ--- 386
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261  411 yFHHDrlDWDEHSSA---GRYVSR----------RCKPLKEFMLSQDVEHerlfdLIQKMLEYDPAKRITLREALKHPFF 477
Cdd:PHA03211 387 -VHVD--EFPQHAGSrlvSQYRHRaarnrrpaytRPAWTRYYKLDLDVEY-----LVCRALTFDGARRPSAAELLRLPLF 458
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
162-393 2.01e-05

Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fyn and Yrk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Fyn/Yrk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase.


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 46.21  E-value: 2.01e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 162 EIVDTLGEGAFGKVveCIDHKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTdpnstfRCVQMLEWFEHHGhICIVF 241
Cdd:cd05070  12 QLIKRLGNGQFGEV--WMGTWNGNTKVAIKTLKPGTMSPESFLEEAQIMKKLKHD------KLVQLYAVVSEEP-IYIVT 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 242 ELLGL-STYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSdyteaynpkikrdertLInpd 320
Cdd:cd05070  83 EYMSKgSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNG----------------LI--- 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 67551261 321 IKVVDFGSATYDDEHHSTLVSTRHY----RAPEVILALGWSQPCDVWSIGCILIEYYL-GFTVFPTHDSKEHLAMMER 393
Cdd:cd05070 144 CKIADFGLARLIEDNEYTARQGAKFpikwTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQVER 221
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
162-399 2.26e-05

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: 46.21  E-value: 2.26e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 162 EIVDTLGEGAFGKVVECiDHKAGGRHVAVKIVKNVDRYCEAARseiqVLEHLNTTdpNSTFRC---VQMLEWFEHHGHIC 238
Cdd:cd06618  18 ENLGEIGSGTCGQVYKM-RHKKTGHVMAVKQMRRSGNKEENKR----ILMDLDVV--LKSHDCpyiVKCYGYFITDSDVF 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 239 IVFELLGLSTYDFIKE-NGFLPFRLdhIRKMAYQICKSVNFLHSNK-LTHTDLKPENILFvqsdyteaynpkikrDERTl 316
Cdd:cd06618  91 ICMELMSTCLDKLLKRiQGPIPEDI--LGKMTVSIVKALHYLKEKHgVIHRDVKPSNILL---------------DESG- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 317 inpDIKVVDFGSATY--DDEHHSTLVSTRHYRAPEVILALGWSQ---PCDVWSIGCILIEYYLGftVFPTHDSKEHLAMM 391
Cdd:cd06618 153 ---NVKLCDFGISGRlvDSKAKTRSAGCAAYMAPERIDPPDNPKydiRADVWSLGISLVELATG--QFPYRNCKTEFEVL 227

                ....*...
gi 67551261 392 ERILGPLP 399
Cdd:cd06618 228 TKILNEEP 235
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
164-400 2.31e-05

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: 46.16  E-value: 2.31e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 164 VDTLGEGAFGKVVECIDHKAGGRH---VAVKIVKNVD--RYCEAARSEIQVLEHLNttDPNstfrCVQMLEWFEHHGHIC 238
Cdd:cd05090  10 MEELGECAFGKIYKGHLYLPGMDHaqlVAIKTLKDYNnpQQWNEFQQEASLMTELH--HPN----IVCLLGVVTQEQPVC 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 239 IVFELLGLST-YDFI-------------KENGFLPFRLDH--IRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYT 302
Cdd:cd05090  84 MLFEFMNQGDlHEFLimrsphsdvgcssDEDGTVKSSLDHgdFLHIAIQIAAGMEYLSSHFFVHKDLAARNILVGEQLHV 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 303 EAYNPKIKRdertlinpdikvvDFGSATYDDEHHSTLVSTRhYRAPEVILALGWSQPCDVWSIGCILIEYY-LGFTVFPT 381
Cdd:cd05090 164 KISDLGLSR-------------EIYSSDYYRVQNKSLLPIR-WMPPEAIMYGKFSSDSDIWSFGVVLWEIFsFGLQPYYG 229
                       250       260
                ....*....|....*....|
gi 67551261 382 HDSKEHLAMM-ERILGPLPK 400
Cdd:cd05090 230 FSNQEVIEMVrKRQLLPCSE 249
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
167-373 2.38e-05

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: 45.80  E-value: 2.38e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIDHKAGGRH--VAVKIVKNVDRycEAARSEI----QVLEHLNttDPNstfrCVQMLEWFEHHGhICIV 240
Cdd:cd05060   3 LGHGNFGSVRKGVYLMKSGKEveVAVKTLKQEHE--KAGKKEFlreaSVMAQLD--HPC----IVRLIGVCKGEP-LMLV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 241 FELLGL-STYDFIKENGFLPfrLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrdertlinp 319
Cdd:cd05060  74 MELAPLgPLLKYLKKRREIP--VSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQ------------------ 133
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 67551261 320 dIKVVDFG---SATYDDEHHStlvSTRHYR------APEVILALGWSQPCDVWSIGCILIEYY 373
Cdd:cd05060 134 -AKISDFGmsrALGAGSDYYR---ATTAGRwplkwyAPECINYGKFSSKSDVWSYGVTLWEAF 192
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
166-349 2.73e-05

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: 46.54  E-value: 2.73e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 166 TLGEGAFGKVVEC----IDHKAGGRHVAVKIVKNVDRYCE--AARSEIQVLEHLNttdPNstFRCVQMLEWFEHHGHICI 239
Cdd:cd05107  44 TLGSGAFGRVVEAtahgLSHSQSTMKVAVKMLKSTARSSEkqALMSELKIMSHLG---PH--LNIVNLLGACTKGGPIYI 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 240 VFELL---GLSTYDFIKENGFLPFRLDHIRKMAYqicksvnfLHSNKLTHTDLKPENILF-VQSD--YTEaynpkIKRDE 313
Cdd:cd05107 119 ITEYCrygDLVDYLHRNKHTFLQYYLDKNRDDGS--------LISGGSTPLSQRKSHVSLgSESDggYMD-----MSKDE 185
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 67551261 314 RTLINP------DIKVVDFGSATYDDEHHSTLvstrhYRAPE 349
Cdd:cd05107 186 SADYVPmqdmkgTVKYADIESSNYESPYDQYL-----PSAPE 222
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
162-368 2.87e-05

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: 45.88  E-value: 2.87e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 162 EIVDTLGEGAFGKVVECIDHKAGGR--HVAVKIVKNVdryCEAARSEIQVLEHLnttdpnstfrcvqMLEWFEHhGHIC- 238
Cdd:cd05056   9 TLGRCIGEGQFGDVYQGVYMSPENEkiAVAVKTCKNC---TSPSVREKFLQEAY-------------IMRQFDH-PHIVk 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 239 -----------IVFELLGLSTY-DFIKENgflPFRLDHIR--KMAYQICKSVNFLHSNKLTHTDLKPENILFVqsdytea 304
Cdd:cd05056  72 ligvitenpvwIVMELAPLGELrSYLQVN---KYSLDLASliLYAYQLSTALAYLESKRFVHRDIAARNVLVS------- 141
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 305 ynpkikrdertliNPD-IKVVDFGSATY-DDEHHSTLVSTR---HYRAPEVILALGWSQPCDVWSIG-CI 368
Cdd:cd05056 142 -------------SPDcVKLGDFGLSRYmEDESYYKASKGKlpiKWMAPESINFRRFTSASDVWMFGvCM 198
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
167-371 2.91e-05

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


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 45.66  E-value: 2.91e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKV-VECID--HKAGGRHVAVKIVK--NVDRYCEAARSEIQVLEHLNTTDPNSTFRCVQmlewfEHHGHIC-IV 240
Cdd:cd05080  12 LGEGHFGKVsLYCYDptNDGTGEMVAVKALKadCGPQHRSGWKQEIDILKTLYHENIVKYKGCCS-----EQGGKSLqLI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 241 FELLGL-STYDFIKENGFlpfRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfvqsdyteaynpkIKRDERtlinp 319
Cdd:cd05080  87 MEYVPLgSLRDYLPKHSI---GLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVL-------------LDNDRL----- 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 67551261 320 dIKVVDFGSATYDDEHHstlvstRHYR------------APEVILALGWSQPCDVWSIGCILIE 371
Cdd:cd05080 146 -VKIGDFGLAKAVPEGH------EYYRvredgdspvfwyAPECLKEYKFYYASDVWSFGVTLYE 202
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
160-386 3.02e-05

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: 45.39  E-value: 3.02e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDhKAGGRHVAVKIV-----------KNVDRYCEAARseiqVLEHLNTtdpnstfrcVQML 228
Cdd:cd14188   2 RYCRGKVLGKGGFAKCYEMTD-LTTNKVYAAKIIphsrvskphqrEKIDKEIELHR----ILHHKHV---------VQFY 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 229 EWFEHHGHICIVFELLGL-STYDFIKENGFLPfrLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENiLFVQSdyteaynp 307
Cdd:cd14188  68 HYFEDKENIYILLEYCSRrSMAHILKARKVLT--EPEVRYYLRQIVSGLKYLHEQEILHRDLKLGN-FFINE-------- 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 308 kikrdertliNPDIKVVDFGSATY---DDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDS 384
Cdd:cd14188 137 ----------NMELKVGDFGLAARlepLEHRRRTICGTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNL 206

                ..
gi 67551261 385 KE 386
Cdd:cd14188 207 KE 208
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
161-386 3.50e-05

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: 45.80  E-value: 3.50e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVvECIDHKAGGRHVAVKIVKNVDRYCEAARSEIQVlEHLNTTDPNSTFrCVQMLEWFEHHGHICIV 240
Cdd:cd05628   3 FESLKVIGRGAFGEV-RLVQKKDTGHVYAMKILRKADMLEKEQVGHIRA-ERDILVEADSLW-VVKMFYSFQDKLNLYLI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 241 FELLglSTYDFIKengfLPFRLDHIRKMAYQI-----CKSVNFLHSNKLTHTDLKPENILFVQ------SDY------TE 303
Cdd:cd05628  80 MEFL--PGGDMMT----LLMKKDTLTEEETQFyiaetVLAIDSIHQLGFIHRDIKPDNLLLDSkghvklSDFglctglKK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 304 AYNPKIKRDERTLINPDIKVVDFGSA----TYDDEHHS---TLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGF 376
Cdd:cd05628 154 AHRTEFYRNLNHSLPSDFTFQNMNSKrkaeTWKRNRRQlafSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGY 233
                       250
                ....*....|
gi 67551261 377 TVFPTHDSKE 386
Cdd:cd05628 234 PPFCSETPQE 243
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
338-375 3.63e-05

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: 45.77  E-value: 3.63e-05
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 67551261 338 TLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLG 375
Cdd:cd05626 207 SLVGTPNYIAPEVLLRKGYTQLCDWWSVGVILFEMLVG 244
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
259-371 3.91e-05

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: 45.40  E-value: 3.91e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 259 PFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrdertlinpdIKVVDFGSATYDDEHHSt 338
Cdd:cd06634 111 PLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGL-------------------VKLGDFGSASIMAPANS- 170
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 67551261 339 LVSTRHYRAPEVILALGWSQ---PCDVWSIGCILIE 371
Cdd:cd06634 171 FVGTPYWMAPEVILAMDEGQydgKVDVWSLGITCIE 206
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
167-370 4.08e-05

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: 45.19  E-value: 4.08e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVvECIDHKAGGRHVAVKIVknvdryceaaRSEIQVLEHLNTTDPNSTFRCVQMLEWFEHHGHICIVFELL-G 245
Cdd:cd13991  14 IGRGSFGEV-HRMEDKQTGFQCAVKKV----------RLEVFRAEELMACAGLTSPRVVPLYGAVREGPWVNIFMDLKeG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 246 LSTYDFIKENGFLPfrldHIRKMAY--QICKSVNFLHSNKLTHTDLKPENILfVQSDYTEAYnpkikrdertlinpdikV 323
Cdd:cd13991  83 GSLGQLIKEQGCLP----EDRALHYlgQALEGLEYLHSRKILHGDVKADNVL-LSSDGSDAF-----------------L 140
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 67551261 324 VDFG-SATYDDEHHSTLVSTRHY-------RAPEVILALGWSQPCDVWSIGCILI 370
Cdd:cd13991 141 CDFGhAECLDPDGLGKSLFTGDYipgtethMAPEVVLGKPCDAKVDVWSSCCMML 195
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
266-401 4.29e-05

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: 45.56  E-value: 4.29e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 266 RKMAYQICKSVNFLHSNKLTHTDLKPENILfVQSDYTEAynpkikrdertlinPDIKVVDFGSATYDDEHHSTLVSTRHY 345
Cdd:cd14018 141 RVMILQLLEGVDHLVRHGIAHRDLKSDNIL-LELDFDGC--------------PWLVIADFGCCLADDSIGLQLPFSSWY 205
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 67551261 346 ---------RAPEVILA-------LGWSQpCDVWSIGCILIEYYLGFTVFPTHDS--KEHLAMMERILGPLPKH 401
Cdd:cd14018 206 vdrggnaclMAPEVSTAvpgpgvvINYSK-ADAWAVGAIAYEIFGLSNPFYGLGDtmLESRSYQESQLPALPSA 278
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
161-386 4.37e-05

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: 45.61  E-value: 4.37e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVvECIDHKAGGRHVAVKIVKNVDRY----CEAARSEIQVLehlntTDPNSTFrCVQMLEWFEHHGH 236
Cdd:cd05629   3 FHTVKVIGKGAFGEV-RLVQKKDTGKIYAMKTLLKSEMFkkdqLAHVKAERDVL-----AESDSPW-VVSLYYSFQDAQY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELLG-------LSTYDFIKEngflpfrlDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQ------SDY-- 301
Cdd:cd05629  76 LYLIMEFLPggdlmtmLIKYDTFSE--------DVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRgghiklSDFgl 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 302 --------TEAYNPKI---KRDERTLINPDIKVVDFGSATYDDEH-------------HSTlVSTRHYRAPEVILALGWS 357
Cdd:cd05629 148 stgfhkqhDSAYYQKLlqgKSNKNRIDNRNSVAVDSINLTMSSKDqiatwkknrrlmaYST-VGTPDYIAPEIFLQQGYG 226
                       250       260
                ....*....|....*....|....*....
gi 67551261 358 QPCDVWSIGCILIEYYLGFTVFPTHDSKE 386
Cdd:cd05629 227 QECDWWSLGAIMFECLIGWPPFCSENSHE 255
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
158-386 4.66e-05

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: 44.83  E-value: 4.66e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 158 SARYEIVDTLGEGAFGKVVECIDHKA-GGRHVAVKIVKNVDRYCEAARS--EIQVLEHLNTTDPNSTFRCVQMLEWFEHH 234
Cdd:cd14112   2 TGRFSFGSEIFRGRFSVIVKAVDSTTeTDAHCAVKIFEVSDEASEAVREfeSLRTLQHENVQRLIAAFKPSNFAYLVMEK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 235 GHICIvfeLLGLSTYDFIKEngflpfrlDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQsdyteaynpkiKRDER 314
Cdd:cd14112  82 LQEDV---FTRFSSNDYYSE--------EQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQS-----------VRSWQ 139
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 67551261 315 tlinpdIKVVDFGSA-TYDDEHHSTLVSTRHYRAPEVILALGWSQP-CDVWSIGCILIEYYLGFTVFPTHDSKE 386
Cdd:cd14112 140 ------VKLVDFGRAqKVSKLGKVPVDGDTDWASPEFHNPETPITVqSDIWGLGVLTFCLLSGFHPFTSEYDDE 207
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
164-391 4.74e-05

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: 45.27  E-value: 4.74e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 164 VDTLGEGAFGKVVECIDHKAG---GRHVAVKIVKN--VDRYCEAARsEIQVLEHLNTtDPNSTFRCVQmleWFEHHGHIC 238
Cdd:cd05081   9 ISQLGKGNFGSVELCRYDPLGdntGALVAVKQLQHsgPDQQRDFQR-EIQILKALHS-DFIVKYRGVS---YGPGRRSLR 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 239 IVFELL-GLSTYDFIKENgflPFRLDHIRKMAY--QICKSVNFLHSNKLTHTDLKPENILfVQSDyteaynpkikrdert 315
Cdd:cd05081  84 LVMEYLpSGCLRDFLQRH---RARLDASRLLLYssQICKGMEYLGSRRCVHRDLAARNIL-VESE--------------- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 316 linPDIKVVDFGSATYDDEHHSTLV------STRHYRAPEVILALGWSQPCDVWSIGCILIEYYLgFTVFPTHDSKEHLA 389
Cdd:cd05081 145 ---AHVKIADFGLAKLLPLDKDYYVvrepgqSPIFWYAPESLSDNIFSRQSDVWSFGVVLYELFT-YCDKSCSPSAEFLR 220

                ..
gi 67551261 390 MM 391
Cdd:cd05081 221 MM 222
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
157-395 4.78e-05

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: 45.44  E-value: 4.78e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 157 LSARYEIVDTLGEGAFGKVVECIDHKAGgRHVAVKIVK--------NVDRYCEAARSEIQVLEHLNTTdpnstfRCVQML 228
Cdd:cd14041   4 LNDRYLLLHLLGRGGFSEVYKAFDLTEQ-RYVAVKIHQlnknwrdeKKENYHKHACREYRIHKELDHP------RIVKLY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 229 EWFE-HHGHICIVFELLGLSTYDF-IKENGFLPFRldHIRKMAYQICKSVNFLHSNK--LTHTDLKPENILFVQSDYTEa 304
Cdd:cd14041  77 DYFSlDTDSFCTVLEYCEGNDLDFyLKQHKLMSEK--EARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLVNGTACG- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 305 ynpkikrdertlinpDIKVVDFG-SATYDDEHHSTL---------VSTRHYRAPEVILaLGWSQP-----CDVWSIGCIL 369
Cdd:cd14041 154 ---------------EIKITDFGlSKIMDDDSYNSVdgmeltsqgAGTYWYLPPECFV-VGKEPPkisnkVDVWSVGVIF 217
                       250       260
                ....*....|....*....|....*.
gi 67551261 370 IEYYLGFTVFPTHDSKEHLAMMERIL 395
Cdd:cd14041 218 YQCLYGRKPFGHNQSQQDILQENTIL 243
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
161-386 5.11e-05

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: 45.43  E-value: 5.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVvECIDHKAGGRHVAVKIVKNVDRYCEAARSEIQVlEHLNTTDPNSTFrCVQMLEWFEHHGHICIV 240
Cdd:cd05627   4 FESLKVIGRGAFGEV-RLVQKKDTGHIYAMKILRKADMLEKEQVAHIRA-ERDILVEADGAW-VVKMFYSFQDKRNLYLI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 241 FELLglSTYDFIKengfLPFRLDHIRKMAYQICKS-----VNFLHSNKLTHTDLKPENILFVQSDYTEAYN----PKIKR 311
Cdd:cd05627  81 MEFL--PGGDMMT----LLMKKDTLSEEATQFYIAetvlaIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDfglcTGLKK 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 312 DERTLI------NPDikvVDFGSATYDDEHHS------------TLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYY 373
Cdd:cd05627 155 AHRTEFyrnlthNPP---SDFSFQNMNSKRKAetwkknrrqlaySTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEML 231
                       250
                ....*....|...
gi 67551261 374 LGFTVFPTHDSKE 386
Cdd:cd05627 232 IGYPPFCSETPQE 244
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
162-393 5.52e-05

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


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 44.70  E-value: 5.52e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 162 EIVDTLGEGAFGKVVECIDHKAggRHVAVKIVKNvdryceaarseiqvlehlNTTDPNSTFRCVQMLEWFEHHGHI---- 237
Cdd:cd05068  11 KLLRKLGSGQFGEVWEGLWNNT--TPVAVKTLKP------------------GTMDPEDFLREAQIMKKLRHPKLIqlya 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 238 -C-------IVFELLGL-STYDFIKENG---FLPFRLDhirkMAYQICKSVNFLHSNKLTHTDLKPENILFVQsdyteay 305
Cdd:cd05068  71 vCtleepiyIITELMKHgSLLEYLQGKGrslQLPQLID----MAAQVASGMAYLESQNYIHRDLAARNVLVGE------- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 306 npkikrdertliNPDIKVVDFGSA---TYDDEHHSTlVSTR---HYRAPEVILALGWSQPCDVWSIGCILIEYY-LGFTV 378
Cdd:cd05068 140 ------------NNICKVADFGLArviKVEDEYEAR-EGAKfpiKWTAPEAANYNRFSIKSDVWSFGILLTEIVtYGRIP 206
                       250
                ....*....|....*
gi 67551261 379 FPTHDSKEHLAMMER 393
Cdd:cd05068 207 YPGMTNAEVLQQVER 221
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
269-380 6.32e-05

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Unlike other FGFRs, there is only one splice form of FGFR4. It binds FGF1, FGF2, FGF6, FGF19, and FGF23. FGF19 is a selective ligand for FGFR4. Although disruption of FGFR4 in mice causes no obvious phenotype, in vivo inhibition of FGFR4 in cultured skeletal muscle cells resulted in an arrest of muscle progenitor differentiation. FGF6 and FGFR4 are uniquely expressed in myofibers and satellite cells. FGF6/FGFR4 signaling appears to play a key role in the regulation of muscle regeneration. A polymorphism in FGFR4 is found in head and neck squamous cell carcinoma. FGFR4 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 44.96  E-value: 6.32e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 269 AYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrdertlinpdIKVVDFGSA--TYDDEHHSTLVSTR--- 343
Cdd:cd05099 140 AYQVARGMEYLESRRCIHRDLAARNVLVTEDNV-------------------MKIADFGLArgVHDIDYYKKTSNGRlpv 200
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 67551261 344 HYRAPEVILALGWSQPCDVWSIGCILIEYY-LGFTVFP 380
Cdd:cd05099 201 KWMAPEALFDRVYTHQSDVWSFGILMWEIFtLGGSPYP 238
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
249-296 6.89e-05

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 44.46  E-value: 6.89e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 67551261  249 YDFIKENGFLpfRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILF 296
Cdd:PHA03390  97 FDLLKKEGKL--SEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLY 142
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
162-373 7.89e-05

Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The DDR subfamily consists of homologs of mammalian DDR1, DDR2, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 44.64  E-value: 7.89e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 162 EIVDTLGEGAFGKVVEC--------IDHKAGGRH-------VAVKIVKN--VDRYCEAARSEIQVLEHLNttDPNstfrC 224
Cdd:cd05051   8 EFVEKLGEGQFGEVHLCeanglsdlTSDDFIGNDnkdepvlVAVKMLRPdaSKNAREDFLKEVKIMSQLK--DPN----I 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 225 VQMLEWFEHHGHICIVFELLglstydfikENGFL-PFRLDHIRK-------------------MAYQICKSVNFLHSNKL 284
Cdd:cd05051  82 VRLLGVCTRDEPLCMIVEYM---------ENGDLnQFLQKHEAEtqgasatnsktlsygtllyMATQIASGMKYLESLNF 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 285 THTDLKPENILfVQSDYTeaynpkikrdertlinpdIKVVDFGSAtyddehhSTLVSTRHYR------------APEVIL 352
Cdd:cd05051 153 VHRDLATRNCL-VGPNYT------------------IKIADFGMS-------RNLYSGDYYRiegravlpirwmAWESIL 206
                       250       260
                ....*....|....*....|.
gi 67551261 353 ALGWSQPCDVWSIGCILIEYY 373
Cdd:cd05051 207 LGKFTTKSDVWAFGVTLWEIL 227
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
162-393 7.98e-05

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: 44.49  E-value: 7.98e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 162 EIVDTLGEGAFGKVveCIDHKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTdpnstfRCVQMLEWFEHHGhICIVF 241
Cdd:cd05067  10 KLVERLGAGQFGEV--WMGYYNGHTKVAIKSLKQGSMSPDAFLAEANLMKQLQHQ------RLVRLYAVVTQEP-IYIIT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 242 ELL-GLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYTeaynpkikrdertlinpd 320
Cdd:cd05067  81 EYMeNGSLVDFLKTPSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSC------------------ 142
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 67551261 321 iKVVDFGSATYDDEHHSTLVSTRHY----RAPEVILALGWSQPCDVWSIGCILIEYY-LGFTVFPTHDSKEHLAMMER 393
Cdd:cd05067 143 -KIADFGLARLIEDNEYTAREGAKFpikwTAPEAINYGTFTIKSDVWSFGILLTEIVtHGRIPYPGMTNPEVIQNLER 219
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
260-477 8.48e-05

Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB2 binds and negatively regulates the mitogen activated protein kinase (MAPK) kinases, MKK7 and MEK1, which are activators of the MAPKs, ERK and JNK. It controls the activation of inflammatory monocytes, which is essential in innate immune responses and the pathogenesis of inflammatory diseases such as atherosclerosis. TRB2 expression is down-regulated in human acute myeloid leukaemia (AML), which may lead to enhanced cell survival and pathogenesis of the disease. TRB2 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 44.26  E-value: 8.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 260 FRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteaynpkiKRDERTLIN----PDIKVVDFGSATYDDEH 335
Cdd:cd14022  81 LREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVF-------------KDEERTRVKleslEDAYILRGHDDSLSDKH 147
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 336 hstlvSTRHYRAPEVILALG--WSQPCDVWSIGCILIEYYLGftVFPTHDSKehlammerilgplPKHMIQKTRKRKYFH 413
Cdd:cd14022 148 -----GCPAYVSPEILNTSGsySGKAADVWSLGVMLYTMLVG--RYPFHDIE-------------PSSLFSKIRRGQFNI 207
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 67551261 414 HDRLDwdehssagryVSRRCkplkefmlsqdveherlfdLIQKMLEYDPAKRITLREALKHPFF 477
Cdd:cd14022 208 PETLS----------PKAKC-------------------LIRSILRREPSERLTSQEILDHPWF 242
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
269-380 1.10e-04

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Alternative splicing of FGFR1 transcripts produces a variety of isoforms, which are differentially expressed in cells. FGFR1 binds the ligands, FGF1 and FGF2, with high affinity and has also been reported to bind FGF4, FGF6, and FGF9. FGFR1 signaling is critical in the control of cell migration during embryo development. It promotes cell proliferation in fibroblasts. Nuclear FGFR1 plays a role in the regulation of transcription. Mutations, insertions or deletions of FGFR1 have been identified in patients with Kallman's syndrome (KS), an inherited disorder characterized by hypogonadotropic hypogonadism and loss of olfaction. Aberrant FGFR1 expression has been found in some human cancers including 8P11 myeloproliferative syndrome (EMS), breast cancer, and pancreatic adenocarcinoma. FGFR1 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 44.23  E-value: 1.10e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 269 AYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrdertlinpdIKVVDFGSATydDEHH----STLVSTR- 343
Cdd:cd05098 141 AYQVARGMEYLASKKCIHRDLAARNVLVTEDNV-------------------MKIADFGLAR--DIHHidyyKKTTNGRl 199
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 67551261 344 --HYRAPEVILALGWSQPCDVWSIGCILIEYY-LGFTVFP 380
Cdd:cd05098 200 pvKWMAPEALFDRIYTHQSDVWSFGVLLWEIFtLGGSPYP 239
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
252-397 1.13e-04

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: 44.51  E-value: 1.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 252 IKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYTEAYNPKIKRDertlINPDIKVVDFGSATY 331
Cdd:cd05104 203 ILEEDELALDTEDLLSFSYQVAKGMEFLASKNCIHRDLAARNILLTHGRITKICDFGLARD----IRNDSNYVVKGNARL 278
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 67551261 332 DDEhhstlvstrhYRAPEVILALGWSQPCDVWSIGCILIEYY-LGFTVFPTH--DSKEHLAMME--RILGP 397
Cdd:cd05104 279 PVK----------WMAPESIFECVYTFESDVWSYGILLWEIFsLGSSPYPGMpvDSKFYKMIKEgyRMDSP 339
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
155-371 1.25e-04

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: 43.80  E-value: 1.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 155 DVLSARYEIVDTLGEGAFGKVVECI--DHKAG--GRHVAVKIVKnvdrycEAArSEIQVLEHLNTTDPNSTFRC---VQM 227
Cdd:cd05061   2 EVSREKITLLRELGQGSFGMVYEGNarDIIKGeaETRVAVKTVN------ESA-SLRERIEFLNEASVMKGFTChhvVRL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 228 LEWFEHHGHICIVFELLG---LSTY------DFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfVQ 298
Cdd:cd05061  75 LGVVSKGQPTLVVMELMAhgdLKSYlrslrpEAENNPGRPPPTLQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCM-VA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 299 SDYTeaynpkikrdertlinpdIKVVDFGsATYDdehhstLVSTRHYR-APEVILALGWSQP-----------CDVWSIG 366
Cdd:cd05061 154 HDFT------------------VKIGDFG-MTRD------IYETDYYRkGGKGLLPVRWMAPeslkdgvfttsSDMWSFG 208

                ....*
gi 67551261 367 CILIE 371
Cdd:cd05061 209 VVLWE 213
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
164-375 1.41e-04

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: 43.88  E-value: 1.41e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 164 VDTLGEGAFGKVveCIDHKAGGRHV-AVKIVKNVDRYCEAARSEIQVLEHLNTTDPNSTfrCVQMLEWFEHHGHICIVFE 242
Cdd:cd05625   6 IKTLGIGAFGEV--CLARKVDTKALyATKTLRKKDVLLRNQVAHVKAERDILAEADNEW--VVRLYYSFQDKDNLYFVMD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 243 LL-GLSTYDFIKENGFLPFRLDHIRkMAYQICkSVNFLHSNKLTHTDLKPENILFVQ------SDYTEAYNPKIKRDER- 314
Cdd:cd05625  82 YIpGGDMMSLLIRMGVFPEDLARFY-IAELTC-AVESVHKMGFIHRDIKPDNILIDRdghiklTDFGLCTGFRWTHDSKy 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 315 --TLINPDIKVVDFGSATYDDEH-----------------------HStLVSTRHYRAPEVILALGWSQPCDVWSIGCIL 369
Cdd:cd05625 160 yqSGDHLRQDSMDFSNEWGDPENcrcgdrlkplerraarqhqrclaHS-LVGTPNYIAPEVLLRTGYTQLCDWWSVGVIL 238

                ....*.
gi 67551261 370 IEYYLG 375
Cdd:cd05625 239 FEMLVG 244
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
167-380 1.42e-04

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Many FGFR3 splice variants have been reported with the IIIb and IIIc isoforms being the predominant forms. FGFR3 IIIc is the isoform expressed in chondrocytes, the cells affected in dwarfism, while IIIb is expressed in epithelial cells. FGFR3 ligands include FGF1, FGF2, FGF4, FGF8, FGF9, and FGF23. It is a negative regulator of long bone growth. In the cochlear duct and in the lens, FGFR3 is involved in differentiation while it appears to have a role in cell proliferation in epithelial cells. Germline mutations in FGFR3 are associated with skeletal disorders including several forms of dwarfism. Some missense mutations are associated with multiple myeloma and carcinomas of the bladder and cervix. Overexpression of FGFR3 is found in thyroid carcinoma. FGFR3 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 43.86  E-value: 1.42e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVV--ECI----DHKAGGRHVAVKIVKN--VDRYCEAARSEIQVLE----HLNTTdpNSTFRCVQ-----MLE 229
Cdd:cd05100  20 LGEGCFGQVVmaEAIgidkDKPNKPVTVAVKMLKDdaTDKDLSDLVSEMEMMKmigkHKNII--NLLGACTQdgplyVLV 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 230 WFEHHGHICIVFELLGLSTYDFIKENGFLP---FRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteayn 306
Cdd:cd05100  98 EYASKGNLREYLRARRPPGMDYSFDTCKLPeeqLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNV----- 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 307 pkikrdertlinpdIKVVDFGSA--TYDDEHHSTLVSTR---HYRAPEVILALGWSQPCDVWSIGCILIEYY-LGFTVFP 380
Cdd:cd05100 173 --------------MKIADFGLArdVHNIDYYKKTTNGRlpvKWMAPEALFDRVYTHQSDVWSFGVLLWEIFtLGGSPYP 238
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
267-371 1.46e-04

Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TESK proteins phosphorylate cofilin and induce actin cytoskeletal reorganization. In the Drosphila eye, TESK is required for epithelial cell organization. Mammals contain two TESK proteins, TESK1 and TESK2, which are highly expressed in testis and play roles in spermatogenesis. TESK1 is found in testicular germ cells while TESK2 is expressed mainly in nongerminal Sertoli cells. TESK1 is stimulated by integrin-mediated signaling pathways. It regulates cell spreading and focal adhesion formation. The TESK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 43.23  E-value: 1.46e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 267 KMAYQICKSVNFLHSNKLTHTDLKPENILfvqsdyteaynpkIKRDERTLinpDIKVVDFGSA----TYDDEHHS-TLVS 341
Cdd:cd14155  92 KLALDIARGLSYLHSKGIFHRDLTSKNCL-------------IKRDENGY---TAVVGDFGLAekipDYSDGKEKlAVVG 155
                        90       100       110
                ....*....|....*....|....*....|
gi 67551261 342 TRHYRAPEVILALGWSQPCDVWSIGCILIE 371
Cdd:cd14155 156 SPYWMAPEVLRGEPYNEKADVFSYGIILCE 185
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
259-414 1.63e-04

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: 43.50  E-value: 1.63e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 259 PFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrdertlinpdIKVVDFGSA---TYDDEH 335
Cdd:cd06645 104 PLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGH-------------------VKLADFGVSaqiTATIAK 164
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 336 HSTLVSTRHYRAPEVILAL---GWSQPCDVWSIGCILIEYY-LGFTVFPTHDSKEHLAMMERILGPlPKhMIQKTRKRKY 411
Cdd:cd06645 165 RKSFIGTPYWMAPEVAAVErkgGYNQLCDIWAVGITAIELAeLQPPMFDLHPMRALFLMTKSNFQP-PK-LKDKMKWSNS 242

                ...
gi 67551261 412 FHH 414
Cdd:cd06645 243 FHH 245
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
167-386 1.88e-04

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


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 43.53  E-value: 1.88e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVeCIDHKAGGRHVAVKIVKN----VDRYCEAARSEIQVLEhLNTTDP-----NSTFRCVQMLeWFehhghi 237
Cdd:cd05587   4 LGKGSFGKVM-LAERKGTDELYAIKILKKdviiQDDDVECTMVEKRVLA-LSGKPPfltqlHSCFQTMDRL-YF------ 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 238 ciVFELLglstydfikENGFLPFRLDHIRKM--------AYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpki 309
Cdd:cd05587  75 --VMEYV---------NGGDLMYHIQQVGKFkepvavfyAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGH-------- 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 310 krdertlinpdIKVVDFG---SATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKE 386
Cdd:cd05587 136 -----------IKIADFGmckEGIFGGKTTRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDE 204
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
157-395 1.89e-04

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: 43.51  E-value: 1.89e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 157 LSARYEIVDTLGEGAFGKVVECIDHKAGgRHVAVKIVK--------NVDRYCEAARSEIQVLEHLNTTdpnstfRCVQML 228
Cdd:cd14040   4 LNERYLLLHLLGRGGFSEVYKAFDLYEQ-RYAAVKIHQlnkswrdeKKENYHKHACREYRIHKELDHP------RIVKLY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 229 EWFE-HHGHICIVFELLGLSTYDF-IKENGFLPFRldHIRKMAYQICKSVNFLHSNK--LTHTDLKPENILFVQSDYTEa 304
Cdd:cd14040  77 DYFSlDTDTFCTVLEYCEGNDLDFyLKQHKLMSEK--EARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACG- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 305 ynpkikrdertlinpDIKVVDFG-SATYDDEHH--------STLVSTRHYRAPEVILaLGWSQP-----CDVWSIGCILI 370
Cdd:cd14040 154 ---------------EIKITDFGlSKIMDDDSYgvdgmdltSQGAGTYWYLPPECFV-VGKEPPkisnkVDVWSVGVIFF 217
                       250       260
                ....*....|....*....|....*
gi 67551261 371 EYYLGFTVFPTHDSKEHLAMMERIL 395
Cdd:cd14040 218 QCLYGRKPFGHNQSQQDILQENTIL 242
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
166-371 2.63e-04

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: 42.84  E-value: 2.63e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 166 TLGEGAFGKVVEC----IDHKAGGRHVAVKIVKNVD--RYCEAARSEIQVLEHLNttDPNSTfRCVQMLEWFEHHghiCI 239
Cdd:cd05046  12 TLGRGEFGEVFLAkakgIEEEGGETLVLVKALQKTKdeNLQSEFRRELDMFRKLS--HKNVV-RLLGLCREAEPH---YM 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 240 VFEL--LG------LSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYTEAYNPKIKR 311
Cdd:cd05046  86 ILEYtdLGdlkqflRATKSKDEKLKPPPLSTKQKVALCTQIALGMDHLSNARFVHRDLAARNCLVSSQREVKVSLLSLSK 165
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 67551261 312 DertlinpdikvvdfgsaTYDDEHH---STLVSTRhYRAPEVILALGWSQPCDVWSIGCILIE 371
Cdd:cd05046 166 D-----------------VYNSEYYklrNALIPLR-WLAPEAVQEDDFSTKSDVWSFGVLMWE 210
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
162-391 2.72e-04

Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A-Raf cooperates with C-Raf in regulating ERK transient phosphorylation that is associated with cyclin D expression and cell cycle progression. Mice deficient in A-Raf are born alive but show neurological and intestinal defects. A-Raf demonstrates low kinase activity to MEK, compared with B- and C-Raf, and may also have alternative functions other than in the ERK signaling cascade. It regulates the M2 type pyruvate kinase, a key glycolytic enzyme. It also plays a role in endocytic membrane trafficking. A-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The A-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 42.70  E-value: 2.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 162 EIVDTLGEGAFGKVVEcidhkaGGRH--VAVKIVKNVDRYCE---AARSEIQVLE---HLN-------TTDPNSTFrcvq 226
Cdd:cd14150   3 SMLKRIGTGSFGTVFR------GKWHgdVAVKILKVTEPTPEqlqAFKNEMQVLRktrHVNillfmgfMTRPNFAI---- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 227 MLEWFE-----HHGHICivfellglstydfikENGFLPFRLDHIrkmAYQICKSVNFLHSNKLTHTDLKPENIlFVQSDY 301
Cdd:cd14150  73 ITQWCEgsslyRHLHVT---------------ETRFDTMQLIDV---ARQTAQGMDYLHAKNIIHRDLKSNNI-FLHEGL 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 302 TeaynpkikrdertlinpdIKVVDFGSATyddehhstlVSTRH--------------YRAPEVILALG---WSQPCDVWS 364
Cdd:cd14150 134 T------------------VKIGDFGLAT---------VKTRWsgsqqveqpsgsilWMAPEVIRMQDtnpYSFQSDVYA 186
                       250       260
                ....*....|....*....|....*..
gi 67551261 365 IGCILIEYYLGFTVFPTHDSKEHLAMM 391
Cdd:cd14150 187 YGVVLYELMSGTLPYSNINNRDQIIFM 213
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
161-379 3.43e-04

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: 42.72  E-value: 3.43e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVeCIDHKAGGRHVAVKIVKNVD--RYCEAA--RSEIQVLEHLNTtdpnstfRCVQMLEW-FEHHG 235
Cdd:cd05597   3 FEILKVIGRGAFGEVA-VVKLKSTEKVYAMKILNKWEmlKRAETAcfREERDVLVNGDR-------RWITKLHYaFQDEN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 236 HICIVFE-------LLGLSTYDFIkengfLPfrLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsDYteaynpk 308
Cdd:cd05597  75 YLYLVMDyycggdlLTLLSKFEDR-----LP--EEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLL---DR------- 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 309 ikrdertliNPDIKVVDFGSATYDDE----HHSTLVSTRHYRAPEVILALG-----WSQPCDVWSIGCILIEYYLGFTVF 379
Cdd:cd05597 138 ---------NGHIRLADFGSCLKLREdgtvQSSVAVGTPDYISPEILQAMEdgkgrYGPECDWWSLGVCMYEMLYGETPF 208
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
161-379 3.65e-04

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: 42.69  E-value: 3.65e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVeCIDHKAGGRHVAVKIVknvDRYCEAARSEIQVLEHLNTTDPNSTFRCVQMLEW-FEHHGHICI 239
Cdd:cd05623  74 FEILKVIGRGAFGEVA-VVKLKNADKVFAMKIL---NKWEMLKRAETACFREERDVLVNGDSQWITTLHYaFQDDNNLYL 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 240 VFE------LLGLSTydfiKENGFLPfrLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVqsdyteaynpkikrde 313
Cdd:cd05623 150 VMDyyvggdLLTLLS----KFEDRLP--EDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMD---------------- 207
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 67551261 314 rtlINPDIKVVDFGSATYDDE----HHSTLVSTRHYRAPEVILAL-----GWSQPCDVWSIGCILIEYYLGFTVF 379
Cdd:cd05623 208 ---MNGHIRLADFGSCLKLMEdgtvQSSVAVGTPDYISPEILQAMedgkgKYGPECDWWSLGVCMYEMLYGETPF 279
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
167-421 4.31e-04

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: 42.29  E-value: 4.31e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVeCIDHKAGGRHVAVKIVKN----VDRYCEAARSEIQVLEHLNT----TDPNSTFRCVQMLEWfehhghic 238
Cdd:cd05615  18 LGKGSFGKVM-LAERKGSDELYAIKILKKdvviQDDDVECTMVEKRVLALQDKppflTQLHSCFQTVDRLYF-------- 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 239 iVFELL-GLSTYDFIKENGflPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrdertli 317
Cdd:cd05615  89 -VMEYVnGGDLMYHIQQVG--KFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGH---------------- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 318 npdIKVVDFGSATyddEHHSTLVSTRH------YRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHL-AM 390
Cdd:cd05615 150 ---IKIADFGMCK---EHMVEGVTTRTfcgtpdYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFqSI 223
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 67551261 391 MERIL---------------GPLPKHMIQK----------TRKRKYFHhdRLDWDE 421
Cdd:cd05615 224 MEHNVsypkslskeavsickGLMTKHPAKRlgcgpegerdIREHAFFR--RIDWDK 277
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
270-380 4.48e-04

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. There are many splice variants of FGFR2 which show differential expression and binding to FGF ligands. Disruption of either FGFR2 or FGFR2b is lethal in mice, due to defects in the placenta or severe impairment of tissue development including lung, limb, and thyroid, respectively. Disruption of FGFR2c in mice results in defective bone and skull development. Genetic alterations of FGFR2 are associated with many human skeletal disorders including Apert syndrome, Crouzon syndrome, Jackson-Weiss syndrome, and Pfeiffer syndrome. FGFR2 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 42.31  E-value: 4.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 270 YQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrdertlinpdIKVVDFGSA--TYDDEHHSTLVSTR---H 344
Cdd:cd05101 153 YQLARGMEYLASQKCIHRDLAARNVLVTENNV-------------------MKIADFGLArdINNIDYYKKTTNGRlpvK 213
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 67551261 345 YRAPEVILALGWSQPCDVWSIGCILIEYY-LGFTVFP 380
Cdd:cd05101 214 WMAPEALFDRVYTHQSDVWSFGVLMWEIFtLGGSPYP 250
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
166-380 5.08e-04

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: 42.14  E-value: 5.08e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 166 TLGEGAFGKVVECIDHKAGGR----HVAVKIVK---NVDRYcEAARSEIQVLEHLNTTDP--NSTFRCVQ-----MLEWF 231
Cdd:cd05106  45 TLGAGAFGKVVEATAFGLGKEdnvlRVAVKMLKasaHTDER-EALMSELKILSHLGQHKNivNLLGACTHggpvlVITEY 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 232 EHHG-------------------------------HICIV---------FELLGLSTY-----------------DFIKE 254
Cdd:cd05106 124 CCYGdllnflrkkaetflnfvmalpeisetssdykNITLEkkyirsdsgFSSQGSDTYvemrpvsssssqssdskDEEDT 203
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 255 NGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVqsdyteaynpkikrDERTlinpdIKVVDFGSATyDDE 334
Cdd:cd05106 204 EDSWPLDLDDLLRFSSQVAQGMDFLASKNCIHRDVAARNVLLT--------------DGRV-----AKICDFGLAR-DIM 263
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 67551261 335 HHSTLVSTRHYR------APEVILALGWSQPCDVWSIGCILIEYY-LGFTVFP 380
Cdd:cd05106 264 NDSNYVVKGNARlpvkwmAPESIFDCVYTVQSDVWSYGILLWEIFsLGKSPYP 316
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
269-373 5.81e-04

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


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 41.59  E-value: 5.81e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 269 AYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteaynpkikRDERTlinpdIKVVDFG------SATYDDEHHSTLVST 342
Cdd:cd05048 130 AIQIAAGMEYLSSHHYVHRDLAARNCLV--------------GDGLT-----VKISDFGlsrdiySSDYYRVQSKSLLPV 190
                        90       100       110
                ....*....|....*....|....*....|.
gi 67551261 343 RhYRAPEVILALGWSQPCDVWSIGCILIEYY 373
Cdd:cd05048 191 R-WMPPEAILYGKFTTESDVWSFGVVLWEIF 220
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
167-371 6.63e-04

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: 41.47  E-value: 6.63e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVEcIDHKAGGRhvaVKIVKNVDRYCEAAR----SEIQVLEHLnttDPNSTFRCVQMLEwfeHHGHICIVFE 242
Cdd:cd14222   1 LGKGFFGQAIK-VTHKATGK---VMVMKELIRCDEETQktflTEVKVMRSL---DHPNVLKFIGVLY---KDKRLNLLTE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 243 LL-GLSTYDFIKENGFLPFRldHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfVQSDYTEAYN----PKIKRDERTLI 317
Cdd:cd14222  71 FIeGGTLKDFLRADDPFPWQ--QKVSFAKGIASGMAYLHSMSIIHRDLNSHNCL-IKLDKTVVVAdfglSRLIVEEKKKP 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 67551261 318 NPD---IKVVDFGSAtyDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIE 371
Cdd:cd14222 148 PPDkptTKKRTLRKN--DRKKRYTVVGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCE 202
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
167-395 6.68e-04

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: 41.79  E-value: 6.68e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECiDHKAGGRHVAVKIV-----KNVDRYcEAARSEIQVLEHLNttdpnSTFrCVQMLEWFEHHGHICIVF 241
Cdd:cd05608   9 LGKGGFGEVSAC-QMRATGKLYACKKLnkkrlKKRKGY-EGAMVEKRILAKVH-----SRF-IVSLAYAFQTKTDLCLVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 242 EL-----LGLSTYDFIKEN-GFlpfrlDHIRKMAY--QICKSVNFLHSNKLTHTDLKPENILFVQSDyteaynpkikrde 313
Cdd:cd05608  81 TImnggdLRYHIYNVDEENpGF-----QEPRACFYtaQIISGLEHLHQRRIIYRDLKPENVLLDDDG------------- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 314 rtlinpDIKVVDFGSAT-YDDEHHST--LVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSK-EHLA 389
Cdd:cd05608 143 ------NVRISDLGLAVeLKDGQTKTkgYAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFRARGEKvENKE 216

                ....*.
gi 67551261 390 MMERIL 395
Cdd:cd05608 217 LKQRIL 222
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
263-379 7.16e-04

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: 41.64  E-value: 7.16e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 263 DHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrdertlinpdIKVVDFG---SATYDDEHHSTL 339
Cdd:cd05588  96 EHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGH-------------------IKLTDYGmckEGLRPGDTTSTF 156
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 67551261 340 VSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVF 379
Cdd:cd05588 157 CGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPF 196
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
161-371 7.31e-04

Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER1, ErbB1) is a receptor PTK (RTK) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands for EGFR include EGF, heparin binding EGF-like growth factor (HBEGF), epiregulin, amphiregulin, TGFalpha, and betacellulin. Upon ligand binding, EGFR can form homo- or heterodimers with other EGFR subfamily members. The EGFR signaling pathway is one of the most important pathways regulating cell proliferation, differentiation, survival, and growth. Overexpression and mutation in the kinase domain of EGFR have been implicated in the development and progression of a variety of cancers. A number of monoclonal antibodies and small molecule inhibitors have been developed that target EGFR, including the antibodies Cetuximab and Panitumumab, which are used in combination with other therapies for the treatment of colorectal cancer and non-small cell lung carcinoma (NSCLC). The small molecule inhibitors Gefitinib (Iressa) and Erlotinib (Tarceva), already used for NSCLC, are undergoing clinical trials for other types of cancer including gastrointestinal, breast, head and neck, and bladder. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 41.55  E-value: 7.31e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVECIdHKAGGRHVAVKIVKNVDRYCEAARSEIQVLehlnttDPNSTFRCVQmlewfehHGHICiv 240
Cdd:cd05108   9 FKKIKVLGSGAFGTVYKGL-WIPEGEKVKIPVAIKELREATSPKANKEIL------DEAYVMASVD-------NPHVC-- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 241 fELLGL---STYDFIKEngFLPF--RLDHIRK------------MAYQICKSVNFLHSNKLTHTDLKPENILfvqsdyte 303
Cdd:cd05108  73 -RLLGIcltSTVQLITQ--LMPFgcLLDYVREhkdnigsqyllnWCVQIAKGMNYLEDRRLVHRDLAARNVL-------- 141
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 67551261 304 aynpkikrdertLINPD-IKVVDFGSATY----DDEHHST--LVSTRhYRAPEVILALGWSQPCDVWSIGCILIE 371
Cdd:cd05108 142 ------------VKTPQhVKITDFGLAKLlgaeEKEYHAEggKVPIK-WMALESILHRIYTHQSDVWSYGVTVWE 203
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
161-379 8.53e-04

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: 41.56  E-value: 8.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 161 YEIVDTLGEGAFGKVVeCIDHKAGGRHVAVKIVK----NVDRYCEAARSEIQVLEHLNTTDpnstfRCVQMLEWFEHHGH 236
Cdd:cd05618  22 FDLLRVIGRGSYAKVL-LVRLKKTERIYAMKVVKkelvNDDEDIDWVQTEKHVFEQASNHP-----FLVGLHSCFQTESR 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELLGLSTYDF-IKENGFLPfrLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrdert 315
Cdd:cd05618  96 LFFVIEYVNGGDLMFhMQRQRKLP--EEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGH-------------- 159
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 67551261 316 linpdIKVVDFG---SATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVF 379
Cdd:cd05618 160 -----IKLTDYGmckEGLRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPF 221
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
165-351 9.81e-04

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: 41.10  E-value: 9.81e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 165 DTLGEGAFGKVvecidhKAG---GRHVAVKIVKNVDR---YCEAARSEIQVLEHLN-----TTDPNSTFRCVQMLEWFEH 233
Cdd:cd14056   1 KTIGKGRYGEV------WLGkyrGEKVAVKIFSSRDEdswFRETEIYQTVMLRHENilgfiAADIKSTGSWTQLWLITEY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 234 HGHicivfellGlSTYDFIKENgflPFRLDHIRKMAYQICKSVNFLHS------NK--LTHTDLKPENILfVQSDYTEAy 305
Cdd:cd14056  75 HEH--------G-SLYDYLQRN---TLDTEEALRLAYSAASGLAHLHTeivgtqGKpaIAHRDLKSKNIL-VKRDGTCC- 140
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 67551261 306 npkikrdertlinpdikVVDFGSATYDDEHHSTL-------VSTRHYRAPEVI 351
Cdd:cd14056 141 -----------------IADLGLAVRYDSDTNTIdippnprVGTKRYMAPEVL 176
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
167-375 1.09e-03

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: 40.94  E-value: 1.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVecIDHKAGGRHV-AVKIVK------NVDRYCEAARSEIQVL--EHLNTTDPNSTFRCVQMLeWFehhghi 237
Cdd:cd05591   3 LGKGSFGKVM--LAERKGTDEVyAIKVLKkdvilqDDDVDCTMTEKRILALaaKHPFLTALHSCFQTKDRL-FF------ 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 238 ciVFELLglstydfikENGFLPFRLDHIRKM--------AYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpki 309
Cdd:cd05591  74 --VMEYV---------NGGDLMFQIQRARKFdeprarfyAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGH-------- 134
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 67551261 310 krdertlinpdIKVVDFG---SATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLG 375
Cdd:cd05591 135 -----------CKLADFGmckEGILNGKTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAG 192
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
167-295 1.30e-03

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: 40.51  E-value: 1.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVEcIDHKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTDPNSTFRCVQMLEWFEHHGhicIVFELLGL 246
Cdd:cd13978   1 LGSGGFGTVSK-ARHVSWFGMVAIKCLHSSPNCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLG---LVMEYMEN 76
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 67551261 247 STYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNK--LTHTDLKPENIL 295
Cdd:cd13978  77 GSLKSLLEREIQDVPWSLRFRIIHEIALGMNFLHNMDppLLHHDLKPENIL 127
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
167-386 1.30e-03

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: 40.82  E-value: 1.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECidHKAG-GRHVAVKIVKNvdRYCEAARSEIQVLEHLNTTDPNSTFRC---VQMLEWFEHHGHICIVFE 242
Cdd:cd05633  13 IGRGGFGEVYGC--RKADtGKMYAMKCLDK--KRIKMKQGETLALNERIMLSLVSTGDCpfiVCMTYAFHTPDKLCFILD 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 243 LL-GLSTYDFIKENGFlpFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYTeaynpkikrdertlinpdi 321
Cdd:cd05633  89 LMnGGDLHYHLSQHGV--FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHV------------------- 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 67551261 322 KVVDFGSAT-YDDEHHSTLVSTRHYRAPEVIL-ALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKE 386
Cdd:cd05633 148 RISDLGLACdFSKKKPHASVGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKD 214
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
260-373 1.90e-03

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: 40.23  E-value: 1.90e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 260 FRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfVQSDYTeaynpkikrdertlinpdIKVVDFGSATY--DDEHHS 337
Cdd:cd05114  97 LSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCL-VNDTGV------------------VKVSDFGMTRYvlDDQYTS 157
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 67551261 338 TLVST--RHYRAPEVILALGWSQPCDVWSIGCILIEYY 373
Cdd:cd05114 158 SSGAKfpVKWSPPEVFNYSKFSSKSDVWSFGVLMWEVF 195
STKc_TTBK2 cd14129
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze ...
160-293 1.92e-03

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. Mutations in TTBK2 is associated with the development of spinocerebellar ataxia type 11, belonging to a group of neurodegenerative disorders characterized by progressive incoordination, dysarthria and impairment of eye movements. Brain tissues of SCA11 patients show the presence of neurofibrillary tangles and tau deposition in the brain, similar to Alzheimer's disease (AD) patients. The TTBK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271031 [Multi-domain]  Cd Length: 262  Bit Score: 40.04  E-value: 1.92e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDHKAGgRHVAVKiVKNVDRYCEAARSEIQVLEHLNTTDPNSTFRCVQMLEWFEHhghicI 239
Cdd:cd14129   1 RWKVLRKIGGGGFGEIYDALDLLTR-ENVALK-VESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNDRFNY-----V 73
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 67551261 240 VFELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPEN 293
Cdd:cd14129  74 VMQLQGRNLADLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSN 127
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
260-478 2.00e-03

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: 40.11  E-value: 2.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 260 FRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFvqsdyteaynpkikrDErtliNPDIKVVDFGSAT-YDDEHHST 338
Cdd:cd05606  95 FSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILL---------------DE----HGHVRISDLGLACdFSKKKPHA 155
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 339 LVSTRHYRAPEVIL-ALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEhlammerilgplpKHMIqktrkrkyfhhDRL 417
Cdd:cd05606 156 SVGTHGYMAPEVLQkGVAYDSSADWFSLGCMLYKLLKGHSPFRQHKTKD-------------KHEI-----------DRM 211
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 67551261 418 dwdehssagryvsrrckplkefMLSQDVEHERLF-----DLIQKMLEYDPAKRITLR-----EALKHPFFD 478
Cdd:cd05606 212 ----------------------TLTMNVELPDSFspelkSLLEGLLQRDVSKRLGCLgrgatEVKEHPFFK 260
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
167-375 3.48e-03

Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. C-Raf, also known as Raf-1 or c-Raf-1, is ubiquitously expressed and was the first Raf identified. It was characterized as the acquired oncogene from an acutely transforming murine sarcoma virus (3611-MSV) and the transforming agent from the avian retrovirus MH2. C-Raf-deficient mice embryos die around midgestation with increased apoptosis of embryonic tissues, especially in the fetal liver. One of the main functions of C-Raf is restricting caspase activation to promote survival in response to specific stimuli such as Fas stimulation, macrophage apoptosis, and erythroid differentiation. C-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The C-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 39.24  E-value: 3.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIDHKaggrHVAVKIVKNVDRYCE---AARSEIQVLE---HLNttdpnstfrcVQMLEWFEHHGHICIV 240
Cdd:cd14149  20 IGSGSFGTVYKGKWHG----DVAVKILKVVDPTPEqfqAFRNEVAVLRktrHVN----------ILLFMGYMTKDNLAIV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 241 FELL-GLSTYDF--IKENGFLPFRLDHIrkmAYQICKSVNFLHSNKLTHTDLKPENIlFVQSDYTeaynpkikrdertli 317
Cdd:cd14149  86 TQWCeGSSLYKHlhVQETKFQMFQLIDI---ARQTAQGMDYLHAKNIIHRDMKSNNI-FLHEGLT--------------- 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 67551261 318 npdIKVVDFGSATYD-----DEHHSTLVSTRHYRAPEVILALG---WSQPCDVWSIGCILIEYYLG 375
Cdd:cd14149 147 ---VKIGDFGLATVKsrwsgSQQVEQPTGSILWMAPEVIRMQDnnpFSFQSDVYSYGIVLYELMTG 209
STKc_TTBK1 cd14130
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze ...
160-293 4.37e-03

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. Genetic variations in TTBK1 are linked to Alzheimer's disease (AD). Hyperphosphorylated tau is a major component of paired helical filaments that accumulate in the brain of AD patients. Studies in transgenic mice show that TTBK1 is involved in the phosphorylation-dependent pathogenic aggregation of tau. The TTBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271032 [Multi-domain]  Cd Length: 262  Bit Score: 38.85  E-value: 4.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 160 RYEIVDTLGEGAFGKVVECIDHKAGgRHVAVKiVKNVDRYCEAARSEIQVLEHLNTTDPNSTFRCVQMLEWFEHhghicI 239
Cdd:cd14130   1 RWKVLKKIGGGGFGEIYEAMDLLTR-ENVALK-VESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNY-----V 73
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 67551261 240 VFELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPEN 293
Cdd:cd14130  74 VMQLQGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSN 127
PK_VRK3 cd14124
Pseudokinase domain of Vaccinia Related Kinase 3; The pseudokinase domain shows similarity to ...
233-305 4.38e-03

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


Pssm-ID: 271026 [Multi-domain]  Cd Length: 298  Bit Score: 39.06  E-value: 4.38e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 67551261 233 HHGHICIVFELLGLSTYDFIKE-NGFLPFRldHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYTEAY 305
Cdd:cd14124  93 HDSYRFLVFPSLGQSLQSALDEgKGVLSEK--AVLQLACRLLDALEFIHENEYVHGDITAENIFVDPEDQSEVY 164
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
265-386 5.94e-03

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: 38.88  E-value: 5.94e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 265 IRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYteaynpkikrdertlinpdIKVVDFGSAT-YDDEHHSTLVSTR 343
Cdd:cd14223 105 MRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGH-------------------VRISDLGLACdFSKKKPHASVGTH 165
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 67551261 344 HYRAPEVIL-ALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKE 386
Cdd:cd14223 166 GYMAPEVLQkGVAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKD 209
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
167-371 7.38e-03

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: 38.48  E-value: 7.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIdhkAGG-------RHVAVKIVKnvdrycEAArSEIQVLEHLNTTDPNSTFRC---VQMLEWFEHHGH 236
Cdd:cd05062  14 LGQGSFGMVYEGI---AKGvvkdepeTRVAIKTVN------EAA-SMRERIEFLNEASVMKEFNChhvVRLLGVVSQGQP 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 237 ICIVFELL---GLSTY------DFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILfVQSDYTeaynp 307
Cdd:cd05062  84 TLVIMELMtrgDLKSYlrslrpEMENNPVQAPPSLKKMIQMAGEIADGMAYLNANKFVHRDLAARNCM-VAEDFT----- 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 308 kikrdertlinpdIKVVDFGSA--TYDDEHHST----LVSTRhYRAPEVILALGWSQPCDVWSIGCILIE 371
Cdd:cd05062 158 -------------VKIGDFGMTrdIYETDYYRKggkgLLPVR-WMSPESLKDGVFTTYSDVWSFGVVLWE 213
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
167-332 9.03e-03

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


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 37.86  E-value: 9.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 167 LGEGAFGKVVECIdHKAGGrHVAVKIV---KNVDRYCEAARSEIQVLEHLNTTdpnstfRCVQMLEWFEHHGHICIVFEL 243
Cdd:cd14027   1 LDSGGFGKVSLCF-HRTQG-LVVLKTVytgPNCIEHNEALLEEGKMMNRLRHS------RVVKLLGVILEEGKYSLVMEY 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67551261 244 LGLSTYDFIKENGFLP------FRLDHIRKMAYqicksvnfLHSNKLTHTDLKPENILfVQSDYteaynpkikrdertli 317
Cdd:cd14027  73 MEKGNLMHVLKKVSVPlsvkgrIILEIIEGMAY--------LHGKGVIHKDLKPENIL-VDNDF---------------- 127
                       170
                ....*....|....*
gi 67551261 318 npDIKVVDFGSATYD 332
Cdd:cd14027 128 --HIKIADLGLASFK 140
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH