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Conserved domains on  [gi|23510391|ref|NP_002489|]
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serine/threonine-protein kinase Nek3 isoform a [Homo sapiens]

Protein Classification

STKc_Nek3 domain-containing protein( domain architecture ID 10169484)

STKc_Nek3 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
3-257 0e+00

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: 571.92  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYC 82
Cdd:cd08219   1 QYNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIRLPKSSSAVEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVMEYC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  83 DGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTY 162
Cdd:cd08219  81 DGGDLMQKIKLQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSPGAYACTY 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 163 VGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQMFKRNP 242
Cdd:cd08219 161 VGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGSYKPLPSHYSYELRSLIKQMFKRNP 240
                       250
                ....*....|....*
gi 23510391 243 SHRPSATTLLSRGIV 257
Cdd:cd08219 241 RSRPSATTILSRGSL 255
 
Name Accession Description Interval E-value
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
3-257 0e+00

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: 571.92  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYC 82
Cdd:cd08219   1 QYNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIRLPKSSSAVEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVMEYC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  83 DGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTY 162
Cdd:cd08219  81 DGGDLMQKIKLQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSPGAYACTY 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 163 VGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQMFKRNP 242
Cdd:cd08219 161 VGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGSYKPLPSHYSYELRSLIKQMFKRNP 240
                       250
                ....*....|....*
gi 23510391 243 SHRPSATTLLSRGIV 257
Cdd:cd08219 241 RSRPSATTILSRGSL 255
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
4-252 3.97e-98

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 296.36  E-value: 3.97e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391      4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCD 83
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391     84 GGDLMQKIKQQKGklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMaFACTYV 163
Cdd:smart00220  81 GGDLFDLLKKRGR--LSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGE-KLTTFV 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391    164 GTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLPSH---YSYELQFLVKQMFKR 240
Cdd:smart00220 158 GTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPewdISPEAKDLIRKLLVK 237
                          250
                   ....*....|..
gi 23510391    241 NPSHRPSATTLL 252
Cdd:smart00220 238 DPEKRLTAEEAL 249
Pkinase pfam00069
Protein kinase domain;
4-253 2.71e-85

Protein kinase domain;


Pssm-ID: 425449 [Multi-domain]  Cd Length: 254  Bit Score: 263.32  E-value: 2.71e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391     4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNT-QNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYC 82
Cdd:pfam00069   1 YEVLEKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKdKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391    83 DGGDLMQKIKQQKGklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPmAFACTY 162
Cdd:pfam00069  81 EGGSLFDLLSEKGA--FSEREAKFIMKQILEGLEYLHSNGIVHRDLKPENILIDEDGNLKITDFGLARQLNSG-SSLTTF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   163 VGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCI--SPLPSHYSYELQFLVKQMFKR 240
Cdd:pfam00069 158 VGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYafPELPSNLSEEAKDLLKKLLKK 237
                         250
                  ....*....|...
gi 23510391   241 NPSHRPSATTLLS 253
Cdd:pfam00069 238 DPSKRLTATEALQ 250
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
47-299 1.86e-51

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 182.14  E-value: 1.86e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   47 SRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDLMQKIKQQ-KGKL-FPEDMILNWFTQMCLGVNHIHKKRVL 124
Cdd:PTZ00267 112 ARSELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYGSGGDLNKQIKQRlKEHLpFQEYEVGLLFYQIVLALDEVHSRKMM 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  125 HRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAF--ACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPF 202
Cdd:PTZ00267 192 HRDLKSANIFLMPTGIIKLGDFGFSKQYSDSVSLdvASSFCGTPYYLAPELWERKRYSKKADMWSLGVILYELLTLHRPF 271
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  203 QANSWKNLILKVCQGCISPLPSHYSYELQFLVKQMFKRNPSHRPSATTLLSRGI---VARLVQKCL-PPEIIMEYG-EEV 277
Cdd:PTZ00267 272 KGPSQREIMQQVLYGKYDPFPCPVSSGMKALLDPLLSKNPALRPTTQQLLHTEFlkyVANLFQDIVrHSETISPHDrEEI 351
                        250       260
                 ....*....|....*....|..
gi 23510391  278 LEEIKNSKHNTPrkktNPSRIR 299
Cdd:PTZ00267 352 LRQLQESGERAP----PPSSIR 369
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
3-360 7.72e-50

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 175.32  E-value: 7.72e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHessNQMFAMKEIRLPKSFSNTQNSR--KEAVLLAKMKHP-NIVAFKESFEAEGHLYIVM 79
Cdd:COG0515   1 SYRILRKLGEGSFGEVYLARD---RKLVALKVLAKKLESKSKEVERflREIQILASLNHPpNIVKLYDFFQDEGSLYLVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  80 EYCDGGDLMQKIKQ-QKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNG-KVKLGDFGSARLLSNPM- 156
Cdd:COG0515  78 EYVDGGSLEDLLKKiGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGrVVKLIDFGLAKLLPDPGs 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 157 -----AFACTYVGTPYYVPPEIWENL---PYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKV------------CQ 216
Cdd:COG0515 158 tssipALPSTSVGTPGYMAPEVLLGLslaYASSSSDIWSLGITLYELLTGLPPFEGEKNSSATSQTlkiilelptpslAS 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 217 GCISPLPSHYSYELQFLVKQMFKRNPSHRPSATTLLSRGIVARLVQKCLPPEIIMEYGEEVLEEIKNSKHNTPRKKTNPS 296
Cdd:COG0515 238 PLSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSDLLKPDDSAPLRLSLPPSLEALISSLNS 317
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23510391 297 RIRIALGNEASTVQEEE--QDRKGSHTDLESINENLVESALRRVNREEKGNKSVHLRKASSPNLHR 360
Cdd:COG0515 318 LAISGSDLKLDDSNFSKelAPNGVSSSPHNSSSLLLSTASSKRSSLPKISARSSPSSLSSSSRQQA 383
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
48-206 1.53e-33

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 411126 [Multi-domain]  Cd Length: 563  Bit Score: 133.77  E-value: 1.53e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   48 RKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDLMQKIkQQKGKLFPEDmILNWFTQMCLGVNHIHKKRVLHRD 127
Cdd:NF033483  55 RREAQSAASLSHPNIVSVYDVGEDGGIPYIVMEYVDGRTLKDYI-REHGPLSPEE-AVEIMIQILSALEHAHRNGIVHRD 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  128 IKSKNIFLTQNGKVKLGDFGSARLLSN-PMAFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANS 206
Cdd:NF033483 133 IKPQNILITKDGRVKVTDFGIARALSStTMTQTNSVLGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFDGDS 212
 
Name Accession Description Interval E-value
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
3-257 0e+00

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: 571.92  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYC 82
Cdd:cd08219   1 QYNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIRLPKSSSAVEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVMEYC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  83 DGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTY 162
Cdd:cd08219  81 DGGDLMQKIKLQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSPGAYACTY 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 163 VGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQMFKRNP 242
Cdd:cd08219 161 VGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGSYKPLPSHYSYELRSLIKQMFKRNP 240
                       250
                ....*....|....*
gi 23510391 243 SHRPSATTLLSRGIV 257
Cdd:cd08219 241 RSRPSATTILSRGSL 255
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
3-257 5.42e-154

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: 438.82  E-value: 5.42e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPK-SFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd08215   1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNmSEKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDLMQKIKQQK--GKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFA 159
Cdd:cd08215  81 ADGGDLAQKIKKQKkkGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISKVLESTTDLA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 160 CTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQMFK 239
Cdd:cd08215 161 KTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYPPIPSQYSSELRDLVNSMLQ 240
                       250
                ....*....|....*...
gi 23510391 240 RNPSHRPSATTLLSRGIV 257
Cdd:cd08215 241 KDPEKRPSANEILSSPFI 258
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
4-257 4.07e-128

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: 372.99  E-value: 4.07e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPK-SFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYC 82
Cdd:cd08218   2 YVRIKKIGEGSFGKALLVKSKEDGKQYVIKEINISKmSPKEREESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDYC 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  83 DGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTY 162
Cdd:cd08218  82 DGGDLYKRINAQRGVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVLNSTVELARTC 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 163 VGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQMFKRNP 242
Cdd:cd08218 162 IGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKIIRGSYPPVPSRYSYDLRSLVSQLFKRNP 241
                       250
                ....*....|....*
gi 23510391 243 SHRPSATTLLSRGIV 257
Cdd:cd08218 242 RDRPSINSILEKPFI 256
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
4-254 3.37e-122

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: 358.12  E-value: 3.37e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPK-SFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYC 82
Cdd:cd08225   2 YEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKmPVKEKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEYC 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  83 DGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKV-KLGDFGSARLLSNPMAFACT 161
Cdd:cd08225  82 DGGDLMKRINRQRGVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVaKLGDFGIARQLNDSMELAYT 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 162 YVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQMFKRN 241
Cdd:cd08225 162 CVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNNLHQLVLKICQGYFAPISPNFSRDLRSLISQLFKVS 241
                       250
                ....*....|...
gi 23510391 242 PSHRPSATTLLSR 254
Cdd:cd08225 242 PRDRPSITSILKR 254
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
3-252 5.10e-100

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: 301.77  E-value: 5.10e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIrlpkSFSNTQNSRKEAV-----LLAKMKHPNIVAFKESF--EAEGHL 75
Cdd:cd08217   1 DYEVLETIGKGSFGTVRKVRRKSDGKILVWKEI----DYGKMSEKEKQQLvsevnILRELKHPNIVRYYDRIvdRANTTL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  76 YIVMEYCDGGDLMQKIKQQK--GKLFPEDMILNWFTQMCLGVNHIH-----KKRVLHRDIKSKNIFLTQNGKVKLGDFGS 148
Cdd:cd08217  77 YIVMEYCEGGDLAQLIKKCKkeNQYIPEEFIWKIFTQLLLALYECHnrsvgGGKILHRDLKPANIFLDSDNNVKLGDFGL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 149 ARLLSNPMAFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLPSHYSY 228
Cdd:cd08217 157 ARVLSHDSSFAKTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAANQLELAKKIKEGKFPRIPSRYSS 236
                       250       260
                ....*....|....*....|....
gi 23510391 229 ELQFLVKQMFKRNPSHRPSATTLL 252
Cdd:cd08217 237 ELNEVIKSMLNVDPDKRPSVEELL 260
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
4-252 3.97e-98

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 296.36  E-value: 3.97e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391      4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCD 83
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391     84 GGDLMQKIKQQKGklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMaFACTYV 163
Cdd:smart00220  81 GGDLFDLLKKRGR--LSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGE-KLTTFV 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391    164 GTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLPSH---YSYELQFLVKQMFKR 240
Cdd:smart00220 158 GTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPewdISPEAKDLIRKLLVK 237
                          250
                   ....*....|..
gi 23510391    241 NPSHRPSATTLL 252
Cdd:smart00220 238 DPEKRLTAEEAL 249
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
3-252 1.28e-95

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: 290.08  E-value: 1.28e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPK-SFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd08529   1 DFEILNKLGKGSFGVVYKVVRKVDGRVYALKQIDISRmSRKMREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACT 161
Cdd:cd08529  81 AENGDLHSLIKSQRGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAKILSDTTNFAQT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 162 YVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQMFKRN 241
Cdd:cd08529 161 IVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKYPPISASYSQDLSQLIDSCLTKD 240
                       250
                ....*....|.
gi 23510391 242 PSHRPSATTLL 252
Cdd:cd08529 241 YRQRPDTTELL 251
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
3-252 3.72e-91

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: 278.51  E-value: 3.72e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPksfSNTQNSRKEAV----LLAKMKHPNIVAFKESFEAEGHLYIV 78
Cdd:cd08530   1 DFKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLG---SLSQKEREDSVneirLLASVNHPNIIRYKEAFLDGNRLCIV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  79 MEYCDGGDLMQKIK--QQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPM 156
Cdd:cd08530  78 MEYAPFGDLSKLISkrKKKRRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISKVLKKNL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 157 AFacTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQ 236
Cdd:cd08530 158 AK--TQIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQELRYKVCRGKFPPIPPVYSQDLQQIIRS 235
                       250
                ....*....|....*.
gi 23510391 237 MFKRNPSHRPSATTLL 252
Cdd:cd08530 236 LLQVNPKKRPSCDKLL 251
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
3-253 2.79e-89

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: 273.93  E-value: 2.79e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNS-RKEAVLLAKMKHPNIVAFKESFEAE-GHLYIVME 80
Cdd:cd08223   1 EYQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKAaEQEAKLLSKLKHPNIVSYKESFEGEdGFLYIVMG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  81 YCDGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFAC 160
Cdd:cd08223  81 FCEGGDLYTRLKEQKGVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLESSSDMAT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 161 TYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQMFKR 240
Cdd:cd08223 161 TLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEGKLPPMPKQYSPELGELIKAMLHQ 240
                       250
                ....*....|...
gi 23510391 241 NPSHRPSATTLLS 253
Cdd:cd08223 241 DPEKRPSVKRILR 253
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
4-252 5.00e-87

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: 268.14  E-value: 5.00e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSN---QMFAMKEIRLPK-SFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVM 79
Cdd:cd08222   2 YRVVRKLGSGNFGTVYLVSDLKATadeELKVLKEISVGElQPDETVDANREAKLLSKLDHPAIVKFHDSFVEKESFCIVT 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  80 EYCDGGDLMQKIKQ--QKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLtQNGKVKLGDFGSARLLSNPMA 157
Cdd:cd08222  82 EYCEGGDLDDKISEykKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFL-KNNVIKVGDFGISRILMGTSD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 158 FACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQM 237
Cdd:cd08222 161 LATTFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVEGETPSLPDKYSKELNAIYSRM 240
                       250
                ....*....|....*
gi 23510391 238 FKRNPSHRPSATTLL 252
Cdd:cd08222 241 LNKDPALRPSAAEIL 255
Pkinase pfam00069
Protein kinase domain;
4-253 2.71e-85

Protein kinase domain;


Pssm-ID: 425449 [Multi-domain]  Cd Length: 254  Bit Score: 263.32  E-value: 2.71e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391     4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNT-QNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYC 82
Cdd:pfam00069   1 YEVLEKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKdKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391    83 DGGDLMQKIKQQKGklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPmAFACTY 162
Cdd:pfam00069  81 EGGSLFDLLSEKGA--FSEREAKFIMKQILEGLEYLHSNGIVHRDLKPENILIDEDGNLKITDFGLARQLNSG-SSLTTF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   163 VGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCI--SPLPSHYSYELQFLVKQMFKR 240
Cdd:pfam00069 158 VGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYafPELPSNLSEEAKDLLKKLLKK 237
                         250
                  ....*....|...
gi 23510391   241 NPSHRPSATTLLS 253
Cdd:pfam00069 238 DPSKRLTATEALQ 250
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
4-253 2.01e-75

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: 238.25  E-value: 2.01e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSR--KEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd14014   2 YRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERflREARALARLSHPNIVRVYDVGEDDGRPYIVMEY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDLMQKIKQQkGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLL-SNPMAFAC 160
Cdd:cd14014  82 VEGGSLADLLRER-GPL-PPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALgDSGLTQTG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 161 TYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCI---SPLPSHYSYELQFLVKQM 237
Cdd:cd14014 160 SVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPpppSPLNPDVPPALDAIILRA 239
                       250
                ....*....|....*..
gi 23510391 238 FKRNPSHRP-SATTLLS 253
Cdd:cd14014 240 LAKDPEERPqSAAELLA 256
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
4-257 4.09e-75

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: 237.33  E-value: 4.09e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQ-NSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYC 82
Cdd:cd08221   2 YIPVRVLGRGAFGEAVLYRKTEDNSLVVWKEVNLSRLSEKERrDALNEIDILSLLNHDNIITYYNHFLDGESLFIEMEYC 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  83 DGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTY 162
Cdd:cd08221  82 NGGNLHDKIAQQKNQLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVLDSESSMAESI 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 163 VGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQMFKRNP 242
Cdd:cd08221 162 VGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFDATNPLRLAVKIVQGEYEDIDEQYSEEIIQLVHDCLHQDP 241
                       250
                ....*....|....*
gi 23510391 243 SHRPSATTLLSRGIV 257
Cdd:cd08221 242 EDRPTAEELLERPLL 256
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
3-257 1.16e-72

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: 231.16  E-value: 1.16e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPK-SFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd08220   1 KYEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIPVEQmTKEERQAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGK-VKLGDFGSARLLSNPmAFAC 160
Cdd:cd08220  81 APGGTLFEYIQQRKGSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTvVKIGDFGISKILSSK-SKAY 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 161 TYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQMFKR 240
Cdd:cd08220 160 TVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMRGTFAPISDRYSEELRHLILSMLHL 239
                       250
                ....*....|....*..
gi 23510391 241 NPSHRPSATTLLSRGIV 257
Cdd:cd08220 240 DPNKRPTLSEIMAQPII 256
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
10-253 2.29e-72

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: 228.69  E-value: 2.29e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDLMQ 89
Cdd:cd00180   1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSLKD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  90 KIKQQKGKlFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTYVG--TPY 167
Cdd:cd00180  81 LLKENKGP-LSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKTTGGttPPY 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 168 YVPPEIWENLPYNNKSDIWSLGCILYELctlkhpfqanswknlilkvcqgcisplpshysYELQFLVKQMFKRNPSHRPS 247
Cdd:cd00180 160 YAPPELLGGRYYGPKVDIWSLGVILYEL--------------------------------EELKDLIRRMLQYDPKKRPS 207

                ....*.
gi 23510391 248 ATTLLS 253
Cdd:cd00180 208 AKELLE 213
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
3-253 1.05e-71

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: 228.69  E-value: 1.05e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRL-----PKSfsnTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYI 77
Cdd:cd08224   1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQIfemmdAKA---RQDCLKEIDLLQQLNHPNIIKYLASFIENNELNI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  78 VMEYCDGGDLMQKIK--QQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNP 155
Cdd:cd08224  78 VLELADAGDLSRLIKhfKKQKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGLGRFFSSK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 156 MAFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSwKNLIL---KVCQGCISPLPS-HYSYELQ 231
Cdd:cd08224 158 TTAAHSLVGTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYGEK-MNLYSlckKIEKCEYPPLPAdLYSQELR 236
                       250       260
                ....*....|....*....|..
gi 23510391 232 FLVKQMFKRNPSHRPSATTLLS 253
Cdd:cd08224 237 DLVAACIQPDPEKRPDISYVLD 258
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
3-253 5.23e-68

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: 218.54  E-value: 5.23e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHESSNQMFAMKEI-RLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd14003   1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKIIdKSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETENKIYLVMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDLMQKIKQqKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGsarlLSNPMAFAC- 160
Cdd:cd14003  81 ASGGELFDYIVN-NGRL-SEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFG----LSNEFRGGSl 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 161 --TYVGTPYYVPPEIWENLPYNN-KSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCIsPLPSHYSYELQFLVKQM 237
Cdd:cd14003 155 lkTFCGTPAYAAPEVLLGRKYDGpKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKY-PIPSHLSPDARDLIRRM 233
                       250
                ....*....|....*.
gi 23510391 238 FKRNPSHRPSATTLLS 253
Cdd:cd14003 234 LVVDPSKRITIEEILN 249
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
3-252 1.39e-67

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: 217.77  E-value: 1.39e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNS-RKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd06606   1 RWKKGELLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEELEAlEREIRILSSLKHPNIVRYLGTERTENTLNIFLEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDLMQKIKQQKGklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACT 161
Cdd:cd06606  81 VPGGSLASLLKKFGK--LPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKRLAEIATGEGT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 162 Y--VGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPF-QANSWKNLILKVCQGCISP-LPSHYSYELQFLVKQM 237
Cdd:cd06606 159 KslRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWsELGNPVAALFKIGSSGEPPpIPEHLSEEAKDFLRKC 238
                       250
                ....*....|....*
gi 23510391 238 FKRNPSHRPSATTLL 252
Cdd:cd06606 239 LQRDPKKRPTADELL 253
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
3-253 3.02e-67

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: 216.96  E-value: 3.02e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPK-SFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd05117   1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKlKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVMEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDLMQKIKQQkgKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLT---QNGKVKLGDFGSARLLSNPMaF 158
Cdd:cd05117  81 CTGGELFDRIVKK--GSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLAskdPDSPIKIIDFGLAKIFEEGE-K 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 159 ACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCI---SPLPSHYSYELQFLVK 235
Cdd:cd05117 158 LKTVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYsfdSPEWKNVSEEAKDLIK 237
                       250
                ....*....|....*...
gi 23510391 236 QMFKRNPSHRPSATTLLS 253
Cdd:cd05117 238 RLLVVDPKKRLTAAEALN 255
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
3-252 2.86e-65

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: 211.68  E-value: 2.86e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLpKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYC 82
Cdd:cd05122   1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKINL-ESKEKKESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVMEFC 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  83 DGGDLMQKIKQqKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFG-SARLLSNPMAFacT 161
Cdd:cd05122  80 SGGSLKDLLKN-TNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGlSAQLSDGKTRN--T 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 162 YVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPF-QANSWKNLILKVCQGCIS-PLPSHYSYELQFLVKQMFK 239
Cdd:cd05122 157 FVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYsELPPMKALFLIATNGPPGlRNPKKWSKEFKDFLKKCLQ 236
                       250
                ....*....|...
gi 23510391 240 RNPSHRPSATTLL 252
Cdd:cd05122 237 KDPEKRPTAEQLL 249
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
10-249 5.96e-65

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: 210.84  E-value: 5.96e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKEIRlpKSF----SNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGG 85
Cdd:cd05123   1 LGKGSFGKVLLVRKKDTGKLYAMKVLR--KKEiikrKEVEHTLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  86 DLMQKIKQQKgkLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTYVGT 165
Cdd:cd05123  79 ELFSHLSKEG--RFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSDGDRTYTFCGT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 166 PYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWK---NLILKvcqgciSPL--PSHYSYELQFLVKQMFKR 240
Cdd:cd05123 157 PEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKeiyEKILK------SPLkfPEYVSPEAKSLISGLLQK 230

                ....*....
gi 23510391 241 NPSHRPSAT 249
Cdd:cd05123 231 DPTKRLGSG 239
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
2-253 1.24e-60

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: 200.13  E-value: 1.24e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd06623   1 SDLERVKVLGQGSSGVVYKVRHKPTGKIYALKKIHVDGDEEFRKQLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDLMQKIKqqKGKLFPEDMILNWFTQMCLGVNHIHKKR-VLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFAC 160
Cdd:cd06623  81 MDGGSLADLLK--KVGKIPEPVLAYIARQILKGLDYLHTKRhIIHRDIKPSNLLINSKGEVKIADFGISKVLENTLDQCN 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 161 TYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQAN---SWKNLILKVCQGCISPLPS-HYSYELQFLVKQ 236
Cdd:cd06623 159 TFVGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPgqpSFFELMQAICDGPPPSLPAeEFSPEFRDFISA 238
                       250
                ....*....|....*..
gi 23510391 237 MFKRNPSHRPSATTLLS 253
Cdd:cd06623 239 CLQKDPKKRPSAAELLQ 255
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
3-253 2.07e-60

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: 198.85  E-value: 2.07e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPK--SFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVME 80
Cdd:cd14007   1 DFEIGKPLGKGKFGNVYLAREKKSGFIVALKVISKSQlqKSGLEHQLRREIEIQSHLRHPNILRLYGYFEDKKRIYLILE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  81 YCDGGDLMQKIKQQKgkLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFG-SARLLSNPMAfa 159
Cdd:cd14007  81 YAPNGELYKELKKQK--RFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGwSVHAPSNRRK-- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 160 cTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISpLPSHYSYELQFLVKQMFK 239
Cdd:cd14007 157 -TFCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDIK-FPSSVSPEAKDLISKLLQ 234
                       250
                ....*....|....
gi 23510391 240 RNPSHRPSATTLLS 253
Cdd:cd14007 235 KDPSKRLSLEQVLN 248
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
10-254 4.67e-59

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: 195.06  E-value: 4.67e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHEssNQMFAMKEIRLPKSFSNTQNS-RKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDLM 88
Cdd:cd13999   1 IGSGSFGEVYKGKWR--GTDVAIKKLKVEDDNDELLKEfRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSLY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  89 QKIKQQKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTYVGTPYY 168
Cdd:cd13999  79 DLLHKKKIPL-SWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKMTGVVGTPRW 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 169 VPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCI-SPLPSHYSYELQFLVKQMFKRNPSHRPS 247
Cdd:cd13999 158 MAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAVVQKGLrPPIPPDCPPELSKLIKRCWNEDPEKRPS 237

                ....*..
gi 23510391 248 ATTLLSR 254
Cdd:cd13999 238 FSEIVKR 244
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
3-246 2.86e-58

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: 193.87  E-value: 2.86e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHESSNQMF-AMKEIRLPK-SFSNTQNSRKEAV---------LLAKMKHPNIVAFKESFEA 71
Cdd:cd08528   1 EYAVLELLGSGAFGCVYKVRKKSNGQTLlALKEINMTNpAFGRTEQERDKSVgdiisevniIKEQLRHPNIVRYYKTFLE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  72 EGHLYIVMEYCDG---GDLMQKIKQQKGKlFPEDMILNWFTQMCLGVNHIHK-KRVLHRDIKSKNIFLTQNGKVKLGDFG 147
Cdd:cd08528  81 NDRLYIVMELIEGaplGEHFSSLKEKNEH-FTEDRIWNIFVQMVLALRYLHKeKQIVHRDLKPNNIMLGEDDKVTITDFG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 148 SARLLSNPMAFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLPSH-Y 226
Cdd:cd08528 160 LAKQKGPESSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIVEAEYEPLPEGmY 239
                       250       260
                ....*....|....*....|
gi 23510391 227 SYELQFLVKQMFKRNPSHRP 246
Cdd:cd08528 240 SDDITFVIRSCLTPDPEARP 259
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
2-252 3.62e-58

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: 193.24  E-value: 3.62e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEI-RLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVME 80
Cdd:cd14002   1 ENYHVLELIGEGSFGKVYKGRRKYTGQVVALKFIpKRGKSEKELRNLRQEIEILRKLNHPNIIEMLDSFETKKEFVVVTE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  81 YCDGgDLMQkIKQQKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFAC 160
Cdd:cd14002  81 YAQG-ELFQ-ILEDDGTL-PEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARAMSCNTLVLT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 161 TYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCIsPLPSHYSYELQFLVKQMFKR 240
Cdd:cd14002 158 SIKGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIVKDPV-KWPSNMSPEFKSFLQGLLNK 236
                       250
                ....*....|..
gi 23510391 241 NPSHRPSATTLL 252
Cdd:cd14002 237 DPSKRLSWPDLL 248
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
1-246 4.71e-58

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: 193.32  E-value: 4.71e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   1 MDDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNT--QNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIV 78
Cdd:cd08228   1 LANFQIEKKIGRGQFSEVYRATCLLDRKPVALKKVQIFEMMDAKarQDCVKEIDLLKQLNHPNVIKYLDSFIEDNELNIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  79 MEYCDGGDLMQKIK--QQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPM 156
Cdd:cd08228  81 LELADAGDLSQMIKyfKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 157 AFACTYVGTPYYVPPE-IWENlPYNNKSDIWSLGCILYELCTLKHPFQANSWK--NLILKVCQGCISPLPS-HYSYELQF 232
Cdd:cd08228 161 TAAHSLVGTPYYMSPErIHEN-GYNFKSDIWSLGCLLYEMAALQSPFYGDKMNlfSLCQKIEQCDYPPLPTeHYSEKLRE 239
                       250
                ....*....|....
gi 23510391 233 LVKQMFKRNPSHRP 246
Cdd:cd08228 240 LVSMCIYPDPDQRP 253
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
8-252 1.53e-55

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: 186.45  E-value: 1.53e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRK----EAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCD 83
Cdd:cd06632   6 QLLGSGSFGSVYEGFNGDTGDFFAVKEVSLVDDDKKSRESVKqleqEIALLSKLRHPNIVQYYGTEREEDNLYIFLEYVP 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  84 GGDLmQKIKQQKGKlFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPmAFACTYV 163
Cdd:cd06632  86 GGSI-HKLLQRYGA-FEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHVEAF-SFAKSFK 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 164 GTPYYVPPEIW--ENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQ-GCISPLPSHYSYELQFLVKQMFKR 240
Cdd:cd06632 163 GSPYWMAPEVImqKNSGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIGNsGELPPIPDHLSPDAKDFIRLCLQR 242
                       250
                ....*....|..
gi 23510391 241 NPSHRPSATTLL 252
Cdd:cd06632 243 DPEDRPTASQLL 254
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
10-248 4.77e-55

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: 185.45  E-value: 4.77e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKEI------------RLPKSFSN-TQNSRKEAVLLAKMKHPNIVAFKESFE--AEGH 74
Cdd:cd14008   1 LGRGSFGKVKLALDTETGQLYAIKIFnksrlrkrregkNDRGKIKNaLDDVRREIAIMKKLDHPNIVRLYEVIDdpESDK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  75 LYIVMEYCDGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSN 154
Cdd:cd14008  81 LYLVLEYCEGGPVMELDSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGVSEMFED 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 155 PMAFACTYVGTPYYVPPEIW--ENLPYNNK-SDIWSLGCILYELCTLKHPFQANSwknlILKVCQGCI-----SPLPSHY 226
Cdd:cd14008 161 GNDTLQKTAGTPAFLAPELCdgDSKTYSGKaADIWALGVTLYCLVFGRLPFNGDN----ILELYEAIQnqndeFPIPPEL 236
                       250       260
                ....*....|....*....|..
gi 23510391 227 SYELQFLVKQMFKRNPSHRPSA 248
Cdd:cd14008 237 SPELKDLLRRMLEKDPEKRITL 258
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
4-253 5.11e-54

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: 182.38  E-value: 5.11e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSN--QMFAMKEI---RLPKSFSNTQNSRkEAVLLAKMKHPNIVAFKESFEAEGHLYIV 78
Cdd:cd14080   2 YRLGKTIGEGSYSKVKLAEYTKSGlkEKVACKIIdkkKAPKDFLEKFLPR-ELEILRKLRHPNIIQVYSIFERGSKVFIF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  79 MEYCDGGDLMQKIkQQKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLS--NPM 156
Cdd:cd14080  81 MEYAEHGDLLEYI-QKRGAL-SESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFARLCPddDGD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 157 AFACTYVGTPYYVPPEIWENLPYNNK-SDIWSLGCILYELCTLKHPFQANSWKNLIlKVCQG---CISPLPSHYSYELQF 232
Cdd:cd14080 159 VLSKTFCGSAAYAAPEILQGIPYDPKkYDIWSLGVILYIMLCGSMPFDDSNIKKML-KDQQNrkvRFPSSVKKLSPECKD 237
                       250       260
                ....*....|....*....|.
gi 23510391 233 LVKQMFKRNPSHRPSATTLLS 253
Cdd:cd14080 238 LIDQLLEPDPTKRATIEEILN 258
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
9-253 1.08e-53

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: 181.27  E-value: 1.08e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   9 MIGEGSFG---RALlvqHESSNQMFAMKEIRLPK-SFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDG 84
Cdd:cd06627   7 LIGRGAFGsvyKGL---NLNTGEFVAIKQISLEKiPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEYVEN 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  85 GDLMQKIKQQkGKlFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFG-SARLLSN-PMAFacTY 162
Cdd:cd06627  84 GSLASIIKKF-GK-FPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGvATKLNEVeKDEN--SV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 163 VGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLK------HPFQAnswknlILKVCQGCISPLPSHYSYELQFLVKQ 236
Cdd:cd06627 160 VGTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNppyydlQPMAA------LFRIVQDDHPPLPENISPELRDFLLQ 233
                       250
                ....*....|....*..
gi 23510391 237 MFKRNPSHRPSATTLLS 253
Cdd:cd06627 234 CFQKDPTLRPSAKELLK 250
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
8-252 2.92e-53

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: 180.58  E-value: 2.92e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNT-QNSRKEAVLLAKMKHPNIVAFkesFEAEGH---LYIVMEYCD 83
Cdd:cd06626   6 NKIGEGTFGKVYTAVNLDTGELMAMKEIRFQDNDPKTiKEIADEMKVLEGLDHPNLVRY---YGVEVHreeVYIFMEYCQ 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  84 GGDLMQKIKQqkGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSN---PMAFA- 159
Cdd:cd06626  83 EGTLEELLRH--GRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAVKLKNnttTMAPGe 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 160 -CTYVGTPYYVPPEIWENLPYNNK---SDIWSLGCILYELCTLKHPFQA--NSWKnLILKVCQGCISPLPSH--YSYELQ 231
Cdd:cd06626 161 vNSLVGTPAYMAPEVITGNKGEGHgraADIWSLGCVVLEMATGKRPWSEldNEWA-IMYHVGMGHKPPIPDSlqLSPEGK 239
                       250       260
                ....*....|....*....|.
gi 23510391 232 FLVKQMFKRNPSHRPSATTLL 252
Cdd:cd06626 240 DFLSRCLESDPKKRPTASELL 260
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
10-245 4.18e-53

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: 179.73  E-value: 4.18e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQ-NSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDLM 88
Cdd:cd14009   1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNKKLQeNLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGGDLS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  89 QKIKqqKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGK---VKLGDFGSARLLSnPMAFACTYVGT 165
Cdd:cd14009  81 QYIR--KRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDdpvLKIADFGFARSLQ-PASMAETLCGS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 166 PYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNL---ILKVCQGCISPLPSHYSYELQFLVKQMFKRNP 242
Cdd:cd14009 158 PLYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLlrnIERSDAVIPFPIAAQLSPDCKDLLRRLLRRDP 237

                ...
gi 23510391 243 SHR 245
Cdd:cd14009 238 AER 240
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
2-253 5.34e-53

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: 179.67  E-value: 5.34e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLpKSFSNTQNSRK---EAVLLAKMKHPNIVAFKESFEAEGHLYIV 78
Cdd:cd14099   1 KRYRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPK-SSLTKPKQREKlksEIKIHRSLKHPNIVKFHDCFEDEENVYIL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  79 MEYCDGGDLMQKIKQQKGklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAF 158
Cdd:cd14099  80 LELCSNGSLMELLKRRKA--LTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAARLEYDGER 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 159 ACTYVGTPYYVPPEIWENLP-YNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCIS-PLPSHYSYELQFLVKQ 236
Cdd:cd14099 158 KKTLCGTPNYIAPEVLEKKKgHSFEVDIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNEYSfPSHLSISDEAKDLIRS 237
                       250
                ....*....|....*..
gi 23510391 237 MFKRNPSHRPSATTLLS 253
Cdd:cd14099 238 MLQPDPTKRPSLDEILS 254
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
2-253 3.03e-52

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: 177.84  E-value: 3.03e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRlpkSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd06612   3 EVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVVP---VEEDLQEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVMEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGG---DLMQKIkqqkGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAF 158
Cdd:cd06612  80 CGAGsvsDIMKIT----NKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLTDTMAK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 159 ACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLK------HPFQA---------NSWKNlilkvcqgcisplP 223
Cdd:cd06612 156 RNTVIGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKppysdiHPMRAifmipnkppPTLSD-------------P 222
                       250       260       270
                ....*....|....*....|....*....|
gi 23510391 224 SHYSYELQFLVKQMFKRNPSHRPSATTLLS 253
Cdd:cd06612 223 EKWSPEFNDFVKKCLVKDPEERPSAIQLLQ 252
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
4-253 1.46e-51

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: 175.86  E-value: 1.46e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSfsNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCD 83
Cdd:cd06614   2 YKNLEKIGEGASGEVYKATDRATGKEVAIKKMRLRKQ--NKELIINEILIMKECKHPNIVDYYDSYLVGDELWVVMEYMD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  84 GGDLMQKIKQQKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTYV 163
Cdd:cd06614  80 GGSLTDIITQNPVRM-NESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAAQLTKEKSKRNSVV 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 164 GTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHP-FQANSWKNLILKVCQGcISPL--PSHYSYELQFLVKQMFKR 240
Cdd:cd06614 159 GTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPyLEEPPLRALFLITTKG-IPPLknPEKWSPEFKDFLNKCLVK 237
                       250
                ....*....|...
gi 23510391 241 NPSHRPSATTLLS 253
Cdd:cd06614 238 DPEKRPSAEELLQ 250
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
47-299 1.86e-51

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 182.14  E-value: 1.86e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   47 SRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDLMQKIKQQ-KGKL-FPEDMILNWFTQMCLGVNHIHKKRVL 124
Cdd:PTZ00267 112 ARSELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYGSGGDLNKQIKQRlKEHLpFQEYEVGLLFYQIVLALDEVHSRKMM 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  125 HRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAF--ACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPF 202
Cdd:PTZ00267 192 HRDLKSANIFLMPTGIIKLGDFGFSKQYSDSVSLdvASSFCGTPYYLAPELWERKRYSKKADMWSLGVILYELLTLHRPF 271
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  203 QANSWKNLILKVCQGCISPLPSHYSYELQFLVKQMFKRNPSHRPSATTLLSRGI---VARLVQKCL-PPEIIMEYG-EEV 277
Cdd:PTZ00267 272 KGPSQREIMQQVLYGKYDPFPCPVSSGMKALLDPLLSKNPALRPTTQQLLHTEFlkyVANLFQDIVrHSETISPHDrEEI 351
                        250       260
                 ....*....|....*....|..
gi 23510391  278 LEEIKNSKHNTPrkktNPSRIR 299
Cdd:PTZ00267 352 LRQLQESGERAP----PPSSIR 369
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
2-248 2.19e-51

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: 176.25  E-value: 2.19e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKeiRLPKSFSNTQNSRK----EAVLLAKMKHPNIVAFKESFEAEGHLYI 77
Cdd:cd05581   1 NDFKFGKPLGEGSYSTVVLAKEKETGKEYAIK--VLDKRHIIKEKKVKyvtiEKEVLSRLAHPGIVKLYYTFQDESKLYF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  78 VMEYCDGGDLMQKIKqqKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNP-- 155
Cdd:cd05581  79 VLEYAPNGDLLEYIR--KYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGTAKVLGPDss 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 156 ---------------MAFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCIS 220
Cdd:cd05581 157 pestkgdadsqiaynQARAASFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIVKLEYE 236
                       250       260
                ....*....|....*....|....*...
gi 23510391 221 pLPSHYSYELQFLVKQMFKRNPSHRPSA 248
Cdd:cd05581 237 -FPENFPPDAKDLIQKLLVLDPSKRLGV 263
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
4-252 2.51e-51

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: 175.99  E-value: 2.51e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKeirlpKSFSNTQNSRKEAVL-LAKMK----HPNIVAF--KESFEAEGHL- 75
Cdd:cd13985   2 YQVTKQLGEGGFSYVYLAHDVNTGRRYALK-----RMYFNDEEQLRVAIKeIEIMKrlcgHPNIVQYydSAILSSEGRKe 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  76 -YIVMEYCdGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKK--RVLHRDIKSKNIFLTQNGKVKLGDFGSARLL 152
Cdd:cd13985  77 vLLLMEYC-PGSLVDILEKSPPSPLSEEEVLRIFYQICQAVGHLHSQspPIIHRDIKIENILFSNTGRFKLCDFGSATTE 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 153 SNPMAFACTYV---------GTPYYVPPEI---WENLPYNNKSDIWSLGCILYELCTLKHPFQANSwknlILKVCQG-CI 219
Cdd:cd13985 156 HYPLERAEEVNiieeeiqknTTPMYRAPEMidlYSKKPIGEKADIWALGCLLYKLCFFKLPFDESS----KLAIVAGkYS 231
                       250       260       270
                ....*....|....*....|....*....|...
gi 23510391 220 SPLPSHYSYELQFLVKQMFKRNPSHRPSATTLL 252
Cdd:cd13985 232 IPEQPRYSPELHDLIRHMLTPDPAERPDIFQVI 264
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
2-252 8.57e-51

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: 174.36  E-value: 8.57e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd06609   1 ELFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDLEEAEDEIEDIQQEIQFLSQCDSPYITKYYGSFLKGSKLWIIMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGG---DLMQKIKqqkgklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAF 158
Cdd:cd06609  81 CGGGsvlDLLKPGP------LDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSGQLTSTMSK 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 159 ACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQA-NSWKNLILKVCQGCISPLPSHYSYELQFLVKQM 237
Cdd:cd06609 155 RNTFVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLSDlHPMRVLFLIPKNNPPSLEGNKFSKPFKDFVELC 234
                       250
                ....*....|....*
gi 23510391 238 FKRNPSHRPSATTLL 252
Cdd:cd06609 235 LNKDPKERPSAKELL 249
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
4-252 1.11e-50

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: 174.26  E-value: 1.11e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKeiRLPKSFSNTQ--NSRKEAVLLAKMK-HPNIVAFKESFEAEGHLYIVME 80
Cdd:cd07830   1 YKVIKQLGDGTFGSVYLARNKETGELVAIK--KMKKKFYSWEecMNLREVKSLRKLNeHPNIVKLKEVFRENDELYFVFE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  81 YCDGgDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSAR-LLSNPmAFA 159
Cdd:cd07830  79 YMEG-NLYQLMKDRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLAReIRSRP-PYT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 160 cTYVGTPYYVPPEIWENLP-YNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQ------------GC-------- 218
Cdd:cd07830 157 -DYVSTRWYRAPEILLRSTsYSSPVDIWALGCIMAELYTLRPLFPGSSEIDQLYKICSvlgtptkqdwpeGYklasklgf 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 23510391 219 ----ISPLPSHY-----SYELQFLVKQMFKRNPSHRPSATTLL 252
Cdd:cd07830 236 rfpqFAPTSLHQlipnaSPEAIDLIKDMLRWDPKKRPTASQAL 278
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
1-253 1.66e-50

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: 174.45  E-value: 1.66e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   1 MDDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNT--QNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIV 78
Cdd:cd08229  23 LANFRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIFDLMDAKarADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIV 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  79 MEYCDGGDLMQKIK--QQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPM 156
Cdd:cd08229 103 LELADAGDLSRMIKhfKKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKT 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 157 AFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWK--NLILKVCQGCISPLPS-HYSYELQFL 233
Cdd:cd08229 183 TAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNlySLCKKIEQCDYPPLPSdHYSEELRQL 262
                       250       260
                ....*....|....*....|
gi 23510391 234 VKQMFKRNPSHRPSATTLLS 253
Cdd:cd08229 263 VNMCINPDPEKRPDITYVYD 282
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
4-252 6.35e-50

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 178.14  E-value: 6.35e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391    4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLpKSFSNTQNSRKEAVL--LAKMKHPNIVAFKESF--------EAEG 73
Cdd:PTZ00283  34 YWISRVLGSGATGTVLCAKRVSDGEPFAVKVVDM-EGMSEADKNRAQAEVccLLNCDFFSIVKCHEDFakkdprnpENVL 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   74 HLYIVMEYCDGGDLMQKIKQ--QKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARL 151
Cdd:PTZ00283 113 MIALVLDYANAGDLRQEIKSraKTNRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDFGFSKM 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  152 LSNPMA--FACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLPSHYSYE 229
Cdd:PTZ00283 193 YAATVSddVGRTFCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGENMEEVMHKTLAGRYDPLPPSISPE 272
                        250       260
                 ....*....|....*....|...
gi 23510391  230 LQFLVKQMFKRNPSHRPSATTLL 252
Cdd:PTZ00283 273 MQEIVTALLSSDPKRRPSSSKLL 295
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
3-360 7.72e-50

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 175.32  E-value: 7.72e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHessNQMFAMKEIRLPKSFSNTQNSR--KEAVLLAKMKHP-NIVAFKESFEAEGHLYIVM 79
Cdd:COG0515   1 SYRILRKLGEGSFGEVYLARD---RKLVALKVLAKKLESKSKEVERflREIQILASLNHPpNIVKLYDFFQDEGSLYLVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  80 EYCDGGDLMQKIKQ-QKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNG-KVKLGDFGSARLLSNPM- 156
Cdd:COG0515  78 EYVDGGSLEDLLKKiGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGrVVKLIDFGLAKLLPDPGs 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 157 -----AFACTYVGTPYYVPPEIWENL---PYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKV------------CQ 216
Cdd:COG0515 158 tssipALPSTSVGTPGYMAPEVLLGLslaYASSSSDIWSLGITLYELLTGLPPFEGEKNSSATSQTlkiilelptpslAS 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 217 GCISPLPSHYSYELQFLVKQMFKRNPSHRPSATTLLSRGIVARLVQKCLPPEIIMEYGEEVLEEIKNSKHNTPRKKTNPS 296
Cdd:COG0515 238 PLSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSDLLKPDDSAPLRLSLPPSLEALISSLNS 317
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23510391 297 RIRIALGNEASTVQEEE--QDRKGSHTDLESINENLVESALRRVNREEKGNKSVHLRKASSPNLHR 360
Cdd:COG0515 318 LAISGSDLKLDDSNFSKelAPNGVSSSPHNSSSLLLSTASSKRSSLPKISARSSPSSLSSSSRQQA 383
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
2-253 2.71e-49

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: 170.55  E-value: 2.71e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd13996   6 NDFEEIELLGSGGFGSVYKVRNKVDGVTYAIKKIRLTEKSSASEKVLREVKALAKLNHPNIVRYYTAWVEEPPLYIQMEL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDLMQKI-KQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQN-GKVKLGDFGSARLLSNPMAFA 159
Cdd:cd13996  86 CEGGTLRDWIdRRNSSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDdLQVKIGDFGLATSIGNQKREL 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 160 C--------------TYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCtlkHPFQANSWKNLILK-VCQGCISP-LP 223
Cdd:cd13996 166 NnlnnnnngntsnnsVGIGTPLYASPEQLDGENYNEKADIYSLGIILFEML---HPFKTAMERSTILTdLRNGILPEsFK 242
                       250       260       270
                ....*....|....*....|....*....|
gi 23510391 224 SHYSYELQfLVKQMFKRNPSHRPSATTLLS 253
Cdd:cd13996 243 AKHPKEAD-LIQSLLSKNPEERPSAEQLLR 271
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
7-254 3.75e-49

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: 169.65  E-value: 3.75e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391      7 LRMIGEGSFG---RALLVQHESSNQMF-AMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYC 82
Cdd:smart00221   4 GKKLGEGAFGevyKGTLKGKGDGKEVEvAVKTLKEDASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIVMEYM 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391     83 DGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNpmafacty 162
Cdd:smart00221  84 PGGDLLDYLRKNRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYD-------- 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391    163 vgTPYYV-----------PPEIWENLPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQGCISPLPSHYSYEL 230
Cdd:smart00221 156 --DDYYKvkggklpirwmAPESLKEGKFTSKSDVWSFGVLLWEIFTLgEEPYPGMSNAEVLEYLKKGYRLPKPPNCPPEL 233
                          250       260
                   ....*....|....*....|....
gi 23510391    231 QFLVKQMFKRNPSHRPSATTLLSR 254
Cdd:smart00221 234 YKLMLQCWAEDPEDRPTFSELVEI 257
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
4-252 9.01e-49

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: 169.20  E-value: 9.01e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFS-NTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYC 82
Cdd:cd07829   1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIRLDNEEEgIPSTALREISLLKELKHPNIVKLLDVIHTENKLYLVFEYC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  83 DGgDLMQKIKQQKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAfacTY 162
Cdd:cd07829  81 DQ-DLKKYLDKRPGPL-PPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLARAFGIPLR---TY 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 163 ---VGTPYYVPPEIwenL----PYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLPS---------HY 226
Cdd:cd07829 156 theVVTLWYRAPEI---LlgskHYSTAVDIWSVGCIFAELITGKPLFPGDSEIDQLFKIFQILGTPTEEswpgvtklpDY 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 23510391 227 SYEL-QF------------------LVKQMFKRNPSHRPSATTLL 252
Cdd:cd07829 233 KPTFpKWpkndlekvlprldpegidLLSKMLQYNPAKRISAKEAL 277
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
4-245 9.34e-49

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: 168.59  E-value: 9.34e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSN--TQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd05578   2 FQILRVIGKGSFGKVCIVQKKDTKKMFAMKYMNKQKCIEKdsVRNVLNELEILQELEHPFLVNLWYSFQDEEDMYMVVDL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDLMQKIkQQKGKlFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSnPMAFACT 161
Cdd:cd05578  82 LLGGDLRYHL-QQKVK-FSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATKLT-DGTLATS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 162 YVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWK--NLILKVCQGCISPLPSHYSYELQFLVKQMFK 239
Cdd:cd05578 159 TSGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEIHSRTsiEEIRAKFETASVLYPAGWSEEAIDLINKLLE 238

                ....*.
gi 23510391 240 RNPSHR 245
Cdd:cd05578 239 RDPQKR 244
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
3-253 3.31e-48

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: 167.10  E-value: 3.31e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSfSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYC 82
Cdd:cd06613   1 DYELIQRIGSGTYGDVYKARNIATGELAAVKVIKLEPG-DDFEIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVMEYC 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  83 DGGDLmQKIKQQKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTY 162
Cdd:cd06613  80 GGGSL-QDIYQVTGPL-SELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQLTATIAKRKSF 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 163 VGTPYYVPPEIWE---NLPYNNKSDIWSLGCILYELCTLK------HPFQAnswknLILKVCQGCISPL---PSHYSYEL 230
Cdd:cd06613 158 IGTPYWMAPEVAAverKGGYDGKCDIWALGITAIELAELQppmfdlHPMRA-----LFLIPKSNFDPPKlkdKEKWSPDF 232
                       250       260
                ....*....|....*....|...
gi 23510391 231 QFLVKQMFKRNPSHRPSATTLLS 253
Cdd:cd06613 233 HDFIKKCLTKNPKKRPTATKLLQ 255
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
8-245 1.28e-47

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: 165.50  E-value: 1.28e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFGRALLVQHESSNQMFAMKEIrlPK-SFSNTQNSRK---EAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCD 83
Cdd:cd14081   7 KTLGKGQTGLVKLAKHCVTGQKVAIKIV--NKeKLSKESVLMKverEIAIMKLIEHPNVLKLYDVYENKKYLYLVLEYVS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  84 GGDLMQKIkQQKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARL-LSNPMAFacTY 162
Cdd:cd14081  85 GGELFDYL-VKKGRL-TEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMASLqPEGSLLE--TS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 163 VGTPYYVPPEIWENLPYNN-KSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGcISPLPSHYSYELQFLVKQMFKRN 241
Cdd:cd14081 161 CGSPHYACPEVIKGEKYDGrKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRG-VFHIPHFISPDAQDLLRRMLEVN 239

                ....
gi 23510391 242 PSHR 245
Cdd:cd14081 240 PEKR 243
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
2-252 2.09e-47

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: 165.21  E-value: 2.09e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRL-PKSFSNTQNSRKEAVLLaKMKHPNIVAFKESFEAEGHLYIVME 80
Cdd:cd06605   1 DDLEYLGELGEGNGGVVSKVRHRPSGQIMAVKVIRLeIDEALQKQILRELDVLH-KCNSPYIVGFYGAFYSEGDISICME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  81 YCDGGDLMQKIKQQKGklFPEDMILNWFTQMCLGVNHIHKKR-VLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFa 159
Cdd:cd06605  80 YMDGGSLDKILKEVGR--IPERILGKIAVAVVKGLIYLHEKHkIIHRDVKPSNILVNSRGQVKLCDFGVSGQLVDSLAK- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 160 cTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPF---QANSWKN---LILKVCQGCISPLPSH-YSYELQF 232
Cdd:cd06605 157 -TFVGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPYpppNAKPSMMifeLLSYIVDEPPPLLPSGkFSPDFQD 235
                       250       260
                ....*....|....*....|
gi 23510391 233 LVKQMFKRNPSHRPSATTLL 252
Cdd:cd06605 236 FVSQCLQKDPTERPSYKELM 255
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
10-248 2.19e-47

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: 165.47  E-value: 2.19e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKEIrlPKS---FSNTQNSRK-EAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGG 85
Cdd:cd05579   1 ISRGAYGRVYLAKKKSTGDLYAIKVI--KKRdmiRKNQVDSVLaERNILSQAQNPFVVKLYYSFQGKKNLYLVMEYLPGG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  86 DLmQKIKQQKGKlFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARL-LSNPMAFAC---- 160
Cdd:cd05579  79 DL-YSLLENVGA-LDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKVgLVRRQIKLSiqkk 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 161 ----------TYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCIS-PLPSHYSYE 229
Cdd:cd05579 157 sngapekedrRIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNILNGKIEwPEDPEVSDE 236
                       250
                ....*....|....*....
gi 23510391 230 LQFLVKQMFKRNPSHRPSA 248
Cdd:cd05579 237 AKDLISKLLTPDPEKRLGA 255
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
7-254 4.07e-47

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 164.24  E-value: 4.07e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391      7 LRMIGEGSFG---RALLVQHESSNQMF-AMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYC 82
Cdd:smart00219   4 GKKLGEGAFGevyKGKLKGKGGKKKVEvAVKTLKEDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIVMEYM 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391     83 DGGDLMQKIKQQKGKLFPEDMiLNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNpmafacty 162
Cdd:smart00219  84 EGGDLLSYLRKNRPKLSLSDL-LSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYD-------- 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391    163 vgTPYYV-----------PPEIWENLPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQGCISPLPSHYSYEL 230
Cdd:smart00219 155 --DDYYRkrggklpirwmAPESLKEGKFTSKSDVWSFGVLLWEIFTLgEQPYPGMSNEEVLEYLKNGYRLPQPPNCPPEL 232
                          250       260
                   ....*....|....*....|....
gi 23510391    231 QFLVKQMFKRNPSHRPSATTLLSR 254
Cdd:smart00219 233 YDLMLQCWAEDPEDRPTFSELVEI 256
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
10-259 6.16e-47

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: 164.53  E-value: 6.16e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKEIRLpKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGG---D 86
Cdd:cd06611  13 LGDGAFGKVYKAQHKETGLFAAAKIIQI-ESEEELEDFMVEIDILSECKHPNIVGLYEAYFYENKLWILIEFCDGGaldS 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  87 LMQKIkqqkGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTYVGTP 166
Cdd:cd06611  92 IMLEL----ERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAKNKSTLQKRDTFIGTP 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 167 YYVPPEI-----WENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPL--PSHYSYELQFLVKQMFK 239
Cdd:cd06611 168 YWMAPEVvacetFKDNPYDYKADIWSLGITLIELAQMEPPHHELNPMRVLLKILKSEPPTLdqPSKWSSSFNDFLKSCLV 247
                       250       260
                ....*....|....*....|
gi 23510391 240 RNPSHRPSATTLLSRGIVAR 259
Cdd:cd06611 248 KDPDDRPTAAELLKHPFVSD 267
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
10-245 2.11e-46

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: 162.39  E-value: 2.11e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQ--NSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDL 87
Cdd:cd05572   1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIVQTRQqeHIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLGGEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  88 MQkIKQQKGkLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPmAFACTYVGTPY 167
Cdd:cd05572  81 WT-ILRDRG-LFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKKLGSG-RKTWTFCGTPE 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 168 YVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWK-----NLILKVcqgcISPL--PSHYSYELQFLVKQMFKR 240
Cdd:cd05572 158 YVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFGGDDEDpmkiyNIILKG----IDKIefPKYIDKNAKNLIKQLLRR 233

                ....*
gi 23510391 241 NPSHR 245
Cdd:cd05572 234 NPEER 238
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
3-252 4.78e-46

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: 161.49  E-value: 4.78e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHESSNQMFAMKEI---RLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVM 79
Cdd:cd14098   1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIvkrKVAGNDKNLQLFQREINILKSLEHPGIVRLIDWYEDDQHIYLVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  80 EYCDGGDLMQKIKQQKGklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGK--VKLGDFGSARLLSNPmA 157
Cdd:cd14098  81 EYVEGGDLMDFIMAWGA--IPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDPviVKISDFGLAKVIHTG-T 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 158 FACTYVGTPYYVPPEIW----ENLP--YNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQG--CISPLPS-HYSY 228
Cdd:cd14098 158 FLVTFCGTMAYLAPEILmskeQNLQggYSNLVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIRKGryTQPPLVDfNISE 237
                       250       260
                ....*....|....*....|....
gi 23510391 229 ELQFLVKQMFKRNPSHRPSATTLL 252
Cdd:cd14098 238 EAIDFILRLLDVDPEKRMTAAQAL 261
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
2-253 1.24e-45

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: 160.64  E-value: 1.24e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKS-------FSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGH 74
Cdd:cd14084   6 KKYIMSRTLGSGACGEVKLAYDKSTCKKVAIKIINKRKFtigsrreINKPRNIETEIEILKKLSHPCIIKIEDFFDAEDD 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  75 LYIVMEYCDGGDLMQKIKqqKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGK---VKLGDFGSARL 151
Cdd:cd14084  86 YYIVLELMEGGELFDRVV--SNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEeclIKITDFGLSKI 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 152 LSNpMAFACTYVGTPYYVPPEIWEN---LPYNNKSDIWSLGCILYeLCTLKHPFQANSWKNLILK--VCQGCISPLPSHY 226
Cdd:cd14084 164 LGE-TSLMKTLCGTPTYLAPEVLRSfgtEGYTRAVDCWSLGVILF-ICLSGYPPFSEEYTQMSLKeqILSGKYTFIPKAW 241
                       250       260       270
                ....*....|....*....|....*....|
gi 23510391 227 ---SYELQFLVKQMFKRNPSHRPSATTLLS 253
Cdd:cd14084 242 knvSEEAKDLVKKMLVVDPSRRPSIEEALE 271
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
3-252 5.41e-45

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: 158.32  E-value: 5.41e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHESSNQMFAMKeiRLPKSFSNTQNSRK---EAVLLAKMK-HPNIVAFKESFEAEGHLYIV 78
Cdd:cd13997   1 HFHELEQIGSGSFSEVFKVRSKVDGCLYAVK--KSKKPFRGPKERARalrEVEAHAALGqHPNIVRYYSSWEEGGHLYIQ 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  79 MEYCDGGDLMQKIKQQ-KGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSA-RLLSNPM 156
Cdd:cd13997  79 MELCENGSLQDALEELsPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLAtRLETSGD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 157 AFActyvGTPYYVPPEIW-ENLPYNNKSDIWSLGCILYEL-CTLKHPFQANSWKNLIlkvcQGCISPLPSH-YSYELQFL 233
Cdd:cd13997 159 VEE----GDSRYLAPELLnENYTHLPKADIFSLGVTVYEAaTGEPLPRNGQQWQQLR----QGKLPLPPGLvLSQELTRL 230
                       250
                ....*....|....*....
gi 23510391 234 VKQMFKRNPSHRPSATTLL 252
Cdd:cd13997 231 LKVMLDPDPTRRPTADQLL 249
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
8-253 9.12e-45

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: 157.90  E-value: 9.12e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRK----EAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCD 83
Cdd:cd06625   6 KLLGQGAFGQVYLCYDADTGRELAVKQVEIDPINTEASKEVKalecEIQLLKNLQHERIVQYYGCLQDEKSLSIFMEYMP 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  84 GGDLMQKIKQQkGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSA-RLLSNPMAFAC-T 161
Cdd:cd06625  86 GGSVKDEIKAY-GAL-TENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASkRLQTICSSTGMkS 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 162 YVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPfqansWKNL-----ILKVCQGCISP-LPSHYSYELQFLVK 235
Cdd:cd06625 164 VTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPP-----WAEFepmaaIFKIATQPTNPqLPPHVSEDARDFLS 238
                       250
                ....*....|....*...
gi 23510391 236 QMFKRNPSHRPSATTLLS 253
Cdd:cd06625 239 LIFVRNKKQRPSAEELLS 256
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
3-245 2.28e-44

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: 156.80  E-value: 2.28e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSN--TQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVME 80
Cdd:cd14663   1 RYELGRTLGEGTFAKVKFARNTKTGESVAIKIIDKEQVAREgmVEQIKREIAIMKLLRHPNIVELHEVMATKTKIFFVME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  81 YCDGGDLMQKIKqqKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFG-SArlLSNPMA-- 157
Cdd:cd14663  81 LVTGGELFSKIA--KNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGlSA--LSEQFRqd 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 158 -FACTYVGTPYYVPPEIWENLPYNN-KSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCIsPLPSHYSYELQFLVK 235
Cdd:cd14663 157 gLLHTTCGTPNYVAPEVLARRGYDGaKADIWSCGVILFVLLAGYLPFDDENLMALYRKIMKGEF-EYPRWFSPGAKSLIK 235
                       250
                ....*....|
gi 23510391 236 QMFKRNPSHR 245
Cdd:cd14663 236 RILDPNPSTR 245
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
10-247 3.99e-44

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: 156.26  E-value: 3.99e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFA---MKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESF--EAEGHLYIVMEYCDG 84
Cdd:cd14119   1 LGEGSYGKVKEVLDTETLCRRAvkiLKKRKLRRIPNGEANVKREIQILRRLNHRNVIKLVDVLynEEKQKLYMVMEYCVG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  85 GdLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSnpmAFA----- 159
Cdd:cd14119  81 G-LQEMLDSAPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAEALD---LFAeddtc 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 160 CTYVGTPYYVPPEIWENLPYNN--KSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISpLPSHYSYELQFLVKQM 237
Cdd:cd14119 157 TTSQGSPAFQPPEIANGQDSFSgfKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKGEYT-IPDDVDPDLQDLLRGM 235
                       250
                ....*....|
gi 23510391 238 FKRNPSHRPS 247
Cdd:cd14119 236 LEKDPEKRFT 245
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
10-245 4.13e-44

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: 155.99  E-value: 4.13e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQH-ESSNQMFAMKEIrLPKSFSNTQN-SRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDL 87
Cdd:cd14120   1 IGHGAFAVVFKGRHrKKPDLPVAIKCI-TKKNLSKSQNlLGKEIKILKELSHENVVALLDCQETSSSVYLVMEYCNGGDL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  88 MQKIkQQKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGK---------VKLGDFGSARLLSNPMaF 158
Cdd:cd14120  80 ADYL-QAKGTL-SEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSGrkpspndirLKIADFGFARFLQDGM-M 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 159 ACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANS---WKNLILKvcQGCISP-LPSHYSYELQFLV 234
Cdd:cd14120 157 AATLCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQAQTpqeLKAFYEK--NANLRPnIPSGTSPALKDLL 234
                       250
                ....*....|.
gi 23510391 235 KQMFKRNPSHR 245
Cdd:cd14120 235 LGLLKRNPKDR 245
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
8-254 5.15e-44

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: 156.16  E-value: 5.15e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFG---RALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDG 84
Cdd:cd00192   1 KKLGEGAFGevyKGKLKGGDGKTVDVAVKTLKEDASESERKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYMEG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  85 GDLMQKIKQQKGKL-------FPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNpma 157
Cdd:cd00192  81 GDLLDFLRKSRPVFpspepstLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSRDIYD--- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 158 factyvgTPYYV------------PPEIWENLPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQGCISPLPS 224
Cdd:cd00192 158 -------DDYYRkktggklpirwmAPESLKDGIFTSKSDVWSFGVLLWEIFTLgATPYPGLSNEEVLEYLRKGYRLPKPE 230
                       250       260       270
                ....*....|....*....|....*....|
gi 23510391 225 HYSYELQFLVKQMFKRNPSHRPSATTLLSR 254
Cdd:cd00192 231 NCPDELYELMLSCWQLDPEDRPTFSELVER 260
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
2-206 5.55e-44

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: 158.60  E-value: 5.55e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRlpKS----FSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYI 77
Cdd:cd05573   1 DDFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILR--KSdmlkREQIAHVRAERDILADADSPWIVRLHYAFQDEDHLYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  78 VMEYCDGGDLMQK-IKQQKgklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSA------- 149
Cdd:cd05573  79 VMEYMPGGDLMNLlIKYDV---FPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCtkmnksg 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23510391 150 ----------------------RLLSNPMAFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANS 206
Cdd:cd05573 156 dresylndsvntlfqdnvlarrRPHKQRRVRAYSAVGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPPFYSDS 234
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
1-391 6.01e-44

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 166.45  E-value: 6.01e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391     1 MDDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIrlpkSFSNTQNSRK-----EAVLLAKMKHPNIVAFKESF--EAEG 73
Cdd:PTZ00266   12 LNEYEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAI----SYRGLKEREKsqlviEVNVMRELKHKNIVRYIDRFlnKANQ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391    74 HLYIVMEYCDGGDL---MQKIKQQKGKLfPEDMILNWFTQMCLGVNHIHK-------KRVLHRDIKSKNIFLTQ------ 137
Cdd:PTZ00266   88 KLYILMEFCDAGDLsrnIQKCYKMFGKI-EEHAIVDITRQLLHALAYCHNlkdgpngERVLHRDLKPQNIFLSTgirhig 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   138 ---------NGK--VKLGDFG-SARLLSNPMAFACtyVGTPYYVPPEIW--ENLPYNNKSDIWSLGCILYELCTLKHPF- 202
Cdd:PTZ00266  167 kitaqannlNGRpiAKIGDFGlSKNIGIESMAHSC--VGTPYYWSPELLlhETKSYDDKSDMWALGCIIYELCSGKTPFh 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   203 QANSWKNLILKVCQGCISPLPSHySYELQFLVKQMFKRNPSHRPSATTLLSRGIvarlVQKCLPPEIIMEYGEEVleeik 282
Cdd:PTZ00266  245 KANNFSQLISELKRGPDLPIKGK-SKELNILIKNLLNLSAKERPSALQCLGYQI----IKNVGPPVGAAGGGAGV----- 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   283 NSKHNTPRKKTNPSRirialgnEASTVQEEEQDrKGSHTdlESINENLVESALRRVNREEKgnksvHLRKASSPNlhRRQ 362
Cdd:PTZ00266  315 AAAPGAVVARRNPSK-------EHPGLQLAAME-KAKHA--EAANYGISPNTLINQRNEEQ-----HGRRSSSCA--SRQ 377
                         410       420       430
                  ....*....|....*....|....*....|..
gi 23510391   363 WEKNVPN-TALTALENASILTS--SLTAEDDR 391
Cdd:PTZ00266  378 SANNVTNiTSITSVTSVASVASvaSVPSKDDR 409
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
4-252 8.56e-44

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: 155.09  E-value: 8.56e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTqnSRKEAVLLAKMK----HPNIVAFKESFE--AEGHLYI 77
Cdd:cd05118   1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDFRHPKA--ALREIKLLKHLNdvegHPNIVKLLDVFEhrGGNHLCL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  78 VMEYCdGGDLMQKIKQQkGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQ-NGKVKLGDFGSARLLSNPM 156
Cdd:cd05118  79 VFELM-GMNLYELIKDY-PRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLeLGQLKLADFGLARSFTSPP 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 157 AFacTYVGTPYYVPPE-IWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQ--GcisplpshySYELQFL 233
Cdd:cd05118 157 YT--PYVATRWYRAPEvLLGAKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIVRllG---------TPEALDL 225
                       250
                ....*....|....*....
gi 23510391 234 VKQMFKRNPSHRPSATTLL 252
Cdd:cd05118 226 LSKMLKYDPAKRITASQAL 244
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
4-238 8.96e-44

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: 155.15  E-value: 8.96e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEI---RLPKSFSNTQNSRkEAVLLAKMKHPNIVAFKESFEAEGHLYIVME 80
Cdd:cd14162   2 YIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVskkKAPEDYLQKFLPR-EIEVIKGLKHPNLICFYEAIETTSRVYIIME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  81 YCDGGDLMQKIKQQKgkLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSAR-LLSNPMAFA 159
Cdd:cd14162  81 LAENGDLLDYIRKNG--ALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFARgVMKTKDGKP 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 160 C---TYVGTPYYVPPEIWENLPYNNK-SDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVK 235
Cdd:cd14162 159 KlseTYCGSYAYASPEILRGIPYDPFlSDIWSMGVVLYTMVYGRLPFDDSNLKVLLKQVQRRVVFPKNPTVSEECKDLIL 238

                ...
gi 23510391 236 QMF 238
Cdd:cd14162 239 RML 241
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
4-254 3.83e-43

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: 154.05  E-value: 3.83e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRlpKSFSNTQNS--------RKEAVLLAKM-KHPNIVAFKESFEAEGH 74
Cdd:cd13993   2 YQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLY--KSGPNSKDGndfqklpqLREIDLHRRVsRHPNIITLHDVFETEVA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  75 LYIVMEYCDGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQN-GKVKLGDFGSARLLS 153
Cdd:cd13993  80 IYIVLEYCPNGDLFEAITENRIYVGKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDeGTVKLCDFGLATTEK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 154 NPMAFACtyvGTPYYVPPEIWENLPYNNKS------DIWSLGCILYELCTLKHPF-QANSWKNL----------ILKVcq 216
Cdd:cd13993 160 ISMDFGV---GSEFYMAPECFDEVGRSLKGypcaagDIWSLGIILLNLTFGRNPWkIASESDPIfydyylnspnLFDV-- 234
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 23510391 217 gcISPLpshySYELQFLVKQMFKRNPSHRPSATTLLSR 254
Cdd:cd13993 235 --ILPM----SDDFYNLLRQIFTVNPNNRILLPELQLL 266
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
7-254 4.15e-43

Protein tyrosine kinase;


Pssm-ID: 429616 [Multi-domain]  Cd Length: 258  Bit Score: 153.42  E-value: 4.15e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391     7 LRMIGEGSFG---RALLV-QHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYC 82
Cdd:pfam07714   4 GEKLGEGAFGevyKGTLKgEGENTKIKVAVKTLKEGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVTEYM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391    83 DGGDLMQKIKQQKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNpmafacty 162
Cdd:pfam07714  84 PGGDLLDFLRKHKRKL-TLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDIYD-------- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   163 vgTPYYV------------PPEIWENLPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQGCISPLPSHYSYE 229
Cdd:pfam07714 155 --DDYYRkrgggklpikwmAPESLKDGKFTSKSDVWSFGVLLWEIFTLgEQPYPGMSNEEVLEYLEDGYRLPQPENCPDE 232
                         250       260
                  ....*....|....*....|....*
gi 23510391   230 LQFLVKQMFKRNPSHRPSATTLLSR 254
Cdd:pfam07714 233 LYDLMKQCWAYDPEDRPTFSELVED 257
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
2-245 8.59e-43

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: 153.50  E-value: 8.59e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKE------IRLpKSFSNTQNSRKeavLLAKMKHPNIVAFKESFEAEGHL 75
Cdd:cd05580   1 DDFEFLKTLGTGSFGRVRLVKHKDSGKYYALKIlkkakiIKL-KQVEHVLNEKR---ILSEVRHPFIVNLLGSFQDDRNL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  76 YIVMEYCDGGDLMQKIKqqKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNP 155
Cdd:cd05580  77 YMVMEYVPGGELFSLLR--RSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKRVKDR 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 156 mafACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISpLPSHYSYELQFLVK 235
Cdd:cd05580 155 ---TYTLCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGKIR-FPSFFDPDAKDLIK 230
                       250
                ....*....|
gi 23510391 236 QMFKRNPSHR 245
Cdd:cd05580 231 RLLVVDLTKR 240
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
10-247 1.02e-42

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: 152.49  E-value: 1.02e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQN--SRkEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDL 87
Cdd:cd14075  10 LGSGNFSQVKLGIHQLTKEKVAIKILDKTKLDQKTQRllSR-EISSMEKLHHPNIIRLYEVVETLSKLHLVMEYASGGEL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  88 MQKIKQQkGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFAcTYVGTPY 167
Cdd:cd14075  89 YTKISTE-GKL-SESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFSTHAKRGETLN-TFCGSPP 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 168 YVPPEIWENLPYNNKS-DIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISpLPSHYSYELQFLVKQMFKRNPSHRP 246
Cdd:cd14075 166 YAAPELFKDEHYIGIYvDIWALGVLLYFMVTGVMPFRAETVAKLKKCILEGTYT-IPSYVSEPCQELIRGILQPVPSDRY 244

                .
gi 23510391 247 S 247
Cdd:cd14075 245 S 245
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
8-253 1.41e-42

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: 152.30  E-value: 1.41e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRK--------EAVLLAKMKHPNIVAFKESFEAEGHLYIVM 79
Cdd:cd06628   6 ALIGSGSFGSVYLGMNASSGELMAVKQVELPSVSAENKDRKKsmldalqrEIALLRELQHENIVQYLGSSSDANHLNIFL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  80 EYCDGGDLmQKIKQQKGKlFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFG-SARLLSNPMAF 158
Cdd:cd06628  86 EYVPGGSV-ATLLNNYGA-FEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGiSKKLEANSLST 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 159 AC-----TYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLPSHYSYELQFL 233
Cdd:cd06628 164 KNngarpSLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFPDCTQMQAIFKIGENASPTIPSNISSEARDF 243
                       250       260
                ....*....|....*....|
gi 23510391 234 VKQMFKRNPSHRPSATTLLS 253
Cdd:cd06628 244 LEKTFEIDHNKRPTADELLK 263
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
4-254 2.18e-42

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: 152.45  E-value: 2.18e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPkSFSNTQNSRKEAVLLAKMKHPNI---VAFKESFEAEGH--LYIV 78
Cdd:cd13986   2 YRIQRLLGEGGFSFVYLVEDLSTGRLYALKKILCH-SKEDVKEAMREIENYRLFNHPNIlrlLDSQIVKEAGGKkeVYLL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  79 MEYCDGGDLMQKIK--QQKGKLFPEDMILNWFTQMCLGVNHIHK---KRVLHRDIKSKNIFLTQNGKVKLGDFGS---AR 150
Cdd:cd13986  81 LPYYKRGSLQDEIErrLVKGTFFPEDRILHIFLGICRGLKAMHEpelVPYAHRDIKPGNVLLSEDDEPILMDLGSmnpAR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 151 LLSNPMAFA------CTYVGTPYYVPPEIWeNLPYN----NKSDIWSLGCILYELCTLKHPFQANSWK--NLILKVCQGC 218
Cdd:cd13986 161 IEIEGRREAlalqdwAAEHCTMPYRAPELF-DVKSHctidEKTDIWSLGCTLYALMYGESPFERIFQKgdSLALAVLSGN 239
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 23510391 219 IS-PLPSHYSYELQFLVKQMFKRNPSHRPSATTLLSR 254
Cdd:cd13986 240 YSfPDNSRYSEELHQLVKSMLVVNPAERPSIDDLLSR 276
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
4-245 3.21e-42

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: 151.00  E-value: 3.21e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKsFSNTQNS---RKEAVLLAKMKHPNIVAFKESFEAEGHLYIVME 80
Cdd:cd14073   3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKKDK-IEDEQDMvriRREIEIMSSLNHPHIIRIYEVFENKDKIVIVME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  81 YCDGGDLMQKIkQQKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGsarlLSNPMA--- 157
Cdd:cd14073  82 YASGGELYDYI-SERRRL-PEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFG----LSNLYSkdk 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 158 FACTYVGTPYYVPPEIWENLPYNN-KSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPlPSHYSyELQFLVKQ 236
Cdd:cd14073 156 LLQTFCGSPLYASPEIVNGTPYQGpEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISSGDYRE-PTQPS-DASGLIRW 233

                ....*....
gi 23510391 237 MFKRNPSHR 245
Cdd:cd14073 234 MLTVNPKRR 242
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
8-245 3.55e-42

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: 152.75  E-value: 3.55e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFGRALLVQHESSNQMFAMKEirLPKSFSN-------TQNSRKeaVLLAKMKHPNIVAFKESFEAEGHLYIVME 80
Cdd:cd05570   1 KVLGKGSFGKVMLAERKKTDELYAIKV--LKKEVIIedddvecTMTEKR--VLALANRHPFLTGLHACFQTEDRLYFVME 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  81 YCDGGDLMQKIkQQKGKlFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFAC 160
Cdd:cd05570  77 YVNGGDLMFHI-QRARR-FTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCKEGIWGGNTTS 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 161 TYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLIlkvcqGCIS----PLPSHYSYELQFLVKQ 236
Cdd:cd05570 155 TFCGTPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDELF-----EAILndevLYPRWLSREAVSILKG 229

                ....*....
gi 23510391 237 MFKRNPSHR 245
Cdd:cd05570 230 LLTKDPARR 238
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
53-245 4.53e-42

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: 150.91  E-value: 4.53e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  53 LLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDLMQKIKQQKGklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKN 132
Cdd:cd14010  47 LTHELKHPNVLKFYEWYETSNHLWLVVEYCTGGDLETLLRQDGN--LPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSN 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 133 IFLTQNGKVKLGDFGSARLL----------------SNPMAFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELC 196
Cdd:cd14010 125 ILLDGNGTLKLSDFGLARREgeilkelfgqfsdegnVNKVSKKQAKRGTPYYMAPELFQGGVHSFASDLWALGCVLYEMF 204
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 23510391 197 TLKHPFQANSWKNLILKVCQGCISPLPSHY----SYELQFLVKQMFKRNPSHR 245
Cdd:cd14010 205 TGKPPFVAESFTELVEKILNEDPPPPPPKVsskpSPDFKSLLKGLLEKDPAKR 257
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
2-252 6.10e-42

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: 150.40  E-value: 6.10e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEI--RLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVM 79
Cdd:cd14186   1 EDFKVLNLLGKGSFACVYRARSLHTGLEVAIKMIdkKAMQKAGMVQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  80 EYCDGGDLMQKIKQQKgKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFA 159
Cdd:cd14186  81 EMCHNGEMSRYLKNRK-KPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKMPHEKH 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 160 CTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISpLPSHYSYELQFLVKQMFK 239
Cdd:cd14186 160 FTMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLADYE-MPAFLSREAQDLIHQLLR 238
                       250
                ....*....|...
gi 23510391 240 RNPSHRPSATTLL 252
Cdd:cd14186 239 KNPADRLSLSSVL 251
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
3-252 6.49e-42

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: 150.98  E-value: 6.49e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYC 82
Cdd:cd14046   7 DFEELQVLGKGAFGQVVKVRNKLDGRYYAIKKIKLRSESKNNSRILREVMLLSRLNHQHVVRYYQAWIERANLYIQMEYC 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  83 DGGDLMQKIKQqkGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARllSNPMAFACTY 162
Cdd:cd14046  87 EKSTLRDLIDS--GLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLAT--SNKLNVELAT 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 163 --------------------VGTPYYVPPEIWENLP--YNNKSDIWSLGCILYELCtlkHPFQANSWKNLILKVCQGCIS 220
Cdd:cd14046 163 qdinkstsaalgssgdltgnVGTALYVAPEVQSGTKstYNEKVDMYSLGIIFFEMC---YPFSTGMERVQILTALRSVSI 239
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 23510391 221 PLPSHY---SYELQF-LVKQMFKRNPSHRPSATTLL 252
Cdd:cd14046 240 EFPPDFddnKHSKQAkLIRWLLNHDPAKRPSAQELL 275
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
2-252 7.17e-42

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: 150.59  E-value: 7.17e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd06610   1 DDYELIEVIGSGATAVVYAAYCLPKKEKVAIKRIDLEKCQTSMDELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMPL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDLMQKIKQQ-KGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFAC 160
Cdd:cd06610  81 LSGGSLLDIMKSSyPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVSASLATGGDRTR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 161 ----TYVGTPYYVPPEIWENLP-YNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLPSH-----YSYEL 230
Cdd:cd06610 161 kvrkTFVGTPCWMAPEVMEQVRgYDFKADIWSFGITAIELATGAAPYSKYPPMKVLMLTLQNDPPSLETGadykkYSKSF 240
                       250       260
                ....*....|....*....|..
gi 23510391 231 QFLVKQMFKRNPSHRPSATTLL 252
Cdd:cd06610 241 RKMISLCLQKDPSKRPTAEELL 262
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
4-242 1.58e-41

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: 150.16  E-value: 1.58e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIrlpKSFSNTQNSRKEAV----LLAKMKHPNIVAFKESFEAEGHLYIVM 79
Cdd:cd07833   3 YEVLGVVGEGAYGVVLKCRNKATGEIVAIKKF---KESEDDEDVKKTALrevkVLRQLRHENIVNLKEAFRRKGRLYLVF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  80 EYCDGgDLMQKIKQQKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFA 159
Cdd:cd07833  80 EYVER-TLLELLEASPGGL-PPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARALTARPASP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 160 CT-YVGTPYYVPPEIW-ENLPYNNKSDIWSLGCILYELCTLKHPFQANS-----WknLILKvcqgCISPL-PSHysyelq 231
Cdd:cd07833 158 LTdYVATRWYRAPELLvGDTNYGKPVDVWAIGCIMAELLDGEPLFPGDSdidqlY--LIQK----CLGPLpPSH------ 225
                       250
                ....*....|.
gi 23510391 232 flvKQMFKRNP 242
Cdd:cd07833 226 ---QELFSSNP 233
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
4-245 2.49e-41

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: 148.57  E-value: 2.49e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEI--RLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd14079   4 YILGKTLGVGSFGKVKLAEHELTGHKVAVKILnrQKIKSLDMEEKIRREIQILKLFRHPHIIRLYEVIETPTDIFMVMEY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDLMQKIkQQKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGsarlLSNPM---AF 158
Cdd:cd14079  84 VSGGELFDYI-VQKGRL-SEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFG----LSNIMrdgEF 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 159 ACTYVGTPYYVPPEIWENLPYNN-KSDIWSLGCILYELCTLKHPFQANSWKNLILKVcQGCISPLPSHYSYELQFLVKQM 237
Cdd:cd14079 158 LKTSCGSPNYAAPEVISGKLYAGpEVDVWSCGVILYALLCGSLPFDDEHIPNLFKKI-KSGIYTIPSHLSPGARDLIKRM 236

                ....*...
gi 23510391 238 FKRNPSHR 245
Cdd:cd14079 237 LVVDPLKR 244
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
7-245 3.60e-41

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: 150.25  E-value: 3.60e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   7 LRMIGEGSFGRALLVQH---ESSNQMFAMKEIRLPKSFSN---TQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVME 80
Cdd:cd05584   1 LKVLGKGGYGKVFQVRKttgSDKGKIFAMKVLKKASIVRNqkdTAHTKAERNILEAVKHPFIVDLHYAFQTGGKLYLILE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  81 YCDGGDLMQKIkQQKGkLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFG--SARLLSNPMAF 158
Cdd:cd05584  81 YLSGGELFMHL-EREG-IFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGlcKESIHDGTVTH 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 159 acTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISpLPSHYSYELQFLVKQMF 238
Cdd:cd05584 159 --TFCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGKLN-LPPYLTNEARDLLKKLL 235

                ....*..
gi 23510391 239 KRNPSHR 245
Cdd:cd05584 236 KRNVSSR 242
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
4-248 5.17e-41

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: 147.70  E-value: 5.17e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEI---RLPKSFSNTQNSRKEAVLlAKMKHPNIVAFKESFE-AEGHLYIVM 79
Cdd:cd14164   2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIKIVdrrRASPDFVQKFLPRELSIL-RRVNHPNIVQMFECIEvANGRLYIVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  80 EYCDGgDLMQKIkqQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNG-KVKLGDFGSARLLSNPMAF 158
Cdd:cd14164  81 EAAAT-DLLQKI--QEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDrKIKIADFGFARFVEDYPEL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 159 ACTYVGTPYYVPPEIWENLPYNNKS-DIWSLGCILYELCTLKHPFQANSwKNLILKVCQGCISPLPSHYSYELQFLVKQM 237
Cdd:cd14164 158 STTFCGSRAYTPPEVILGTPYDPKKyDVWSLGVVLYVMVTGTMPFDETN-VRRLRLQQRGVLYPSGVALEEPCRALIRTL 236
                       250
                ....*....|.
gi 23510391 238 FKRNPSHRPSA 248
Cdd:cd14164 237 LQFNPSTRPSI 247
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
4-253 1.47e-40

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: 146.70  E-value: 1.47e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCD 83
Cdd:cd14095   2 YDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGKEHMIENEVAILRRVKHPNIVQLIEEYDTDTELYLVMELVK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  84 GGDLMQKIkQQKGKlFPE----DMILNwftqMCLGVNHIHKKRVLHRDIKSKNIFLTQNG----KVKLGDFGSARLLSNP 155
Cdd:cd14095  82 GGDLFDAI-TSSTK-FTErdasRMVTD----LAQALKYLHSLSIVHRDIKPENLLVVEHEdgskSLKLADFGLATEVKEP 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 156 MAFACtyvGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQA--NSWKNLILKVCQG---CISPLPSHYSYEL 230
Cdd:cd14095 156 LFTVC---GTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRSpdRDQEELFDLILAGefeFLSPYWDNISDSA 232
                       250       260
                ....*....|....*....|...
gi 23510391 231 QFLVKQMFKRNPSHRPSATTLLS 253
Cdd:cd14095 233 KDLISRMLVVDPEKRYSAGQVLD 255
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
4-249 1.71e-40

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: 147.33  E-value: 1.71e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKS---FSNTqnSRKEAVLLAKMKHPNIVAFKE------SFEAEGH 74
Cdd:cd07840   1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRMENEkegFPIT--AIREIKLLQKLDHPNVVRLKEivtskgSAKYKGS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  75 LYIVMEYCDGgDLmQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSN 154
Cdd:cd07840  79 IYMVFEYMDH-DL-TGLLDNPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLARPYTK 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 155 PMAFACTY-VGTPYYVPPEIwenL----PYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLPSHYSY- 228
Cdd:cd07840 157 ENNADYTNrVITLWYRPPEL---LlgatRYGPEVDMWSVGCILAELFTGKPIFQGKTELEQLEKIFELCGSPTEENWPGv 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 23510391 229 -ELQF----------------------------LVKQMFKRNPSHRPSAT 249
Cdd:cd07840 234 sDLPWfenlkpkkpykrrlrevfknvidpsaldLLDKLLTLDPKKRISAD 283
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
4-248 4.86e-40

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: 146.27  E-value: 4.86e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNT-QNSRKEAVLLAKMK---HPNIVAFKESF-----EAEGH 74
Cdd:cd07838   1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKVRVPLSEEGIpLSTIREIALLKQLEsfeHPNVVRLLDVChgprtDRELK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  75 LYIVMEYCDGgDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSN 154
Cdd:cd07838  81 LTLVFEHVDQ-DLATYLDKCPKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFGLARIYSF 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 155 PMAFaCTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKN---LILKV----------------- 214
Cdd:cd07838 160 EMAL-TSVVVTLWYRAPEVLLQSSYATPVDMWSVGCIFAELFNRRPLFRGSSEADqlgKIFDViglpseeewprnsalpr 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 23510391 215 ---CQGCISP----LPSHYSYELQFLvKQMFKRNPSHRPSA 248
Cdd:cd07838 239 ssfPSYTPRPfksfVPEIDEEGLDLL-KKMLTFNPHKRISA 278
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
10-277 5.00e-40

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: 146.33  E-value: 5.00e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKEIRlPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGdLMQ 89
Cdd:cd06644  20 LGDGAFGKVYKAKNKETGALAAAKVIE-TKSEEELEDYMVEIEILATCNHPYIVKLLGAFYWDGKLWIMIEFCPGG-AVD 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  90 KIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTYVGTPYYV 169
Cdd:cd06644  98 AIMLELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSAKNVKTLQRRDSFIGTPYWM 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 170 PPEI-----WENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPL--PSHYSYELQFLVKQMFKRNP 242
Cdd:cd06644 178 APEVvmcetMKDTPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSEPPTLsqPSKWSMEFRDFLKTALDKHP 257
                       250       260       270
                ....*....|....*....|....*....|....*
gi 23510391 243 SHRPSATTLLSRGIVARLVQKCLPPEIIMEYGEEV 277
Cdd:cd06644 258 ETRPSAAQLLEHPFVSSVTSNRPLRELVAEAKAEV 292
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
4-259 6.71e-40

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: 144.90  E-value: 6.71e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIrlpkSFSNTQNSRK------EAVLLAKMKHPNIVAFKESFEAEGHLYI 77
Cdd:cd06607   3 FEDLREIGHGSFGAVYYARNKRTSEVVAIKKM----SYSGKQSTEKwqdiikEVKFLRQLRHPNTIEYKGCYLREHTAWL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  78 VMEYCDG--GDLMQKIKqqkgKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSnP 155
Cdd:cd06607  79 VMEYCLGsaSDIVEVHK----KPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFGSASLVC-P 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 156 mafACTYVGTPYYVPPEI---WENLPYNNKSDIWSLGCILYELCTLKHP-FQANSWKNLiLKVCQGCISPLPS-HYSYEL 230
Cdd:cd06607 154 ---ANSFVGTPYWMAPEVilaMDEGQYDGKVDVWSLGITCIELAERKPPlFNMNAMSAL-YHIAQNDSPTLSSgEWSDDF 229
                       250       260
                ....*....|....*....|....*....
gi 23510391 231 QFLVKQMFKRNPSHRPSATTLLSRGIVAR 259
Cdd:cd06607 230 RNFVDSCLQKIPQDRPSAEDLLKHPFVTR 258
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
2-195 7.22e-40

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: 146.61  E-value: 7.22e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNS--RKEAVLLAKMKHPNIVAFKESFEAEGHLYIVM 79
Cdd:cd05599   1 EDFEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSEMLEKEQVAhvRAERDILAEADNPWVVKLYYSFQDEENLYLIM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  80 EYCDGGDLM-QKIKQQkgkLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFG-SARLLSNPMA 157
Cdd:cd05599  81 EFLPGGDMMtLLMKKD---TLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGlCTGLKKSHLA 157
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 23510391 158 FACtyVGTPYYVPPEIWENLPYNNKSDIWSLGCILYEL 195
Cdd:cd05599 158 YST--VGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEM 193
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
6-252 1.90e-39

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: 144.57  E-value: 1.90e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   6 VLRMIGEGSFGRALLVQHESSNQMFAMKEIrLPKSFSNTQNSRKEAVLLAKMK-HPNIVAF--------KESFEAEGHLY 76
Cdd:cd14036   4 IKRVIAEGGFAFVYEAQDVGTGKEYALKRL-LSNEEEKNKAIIQEINFMKKLSgHPNIVQFcsaasigkEESDQGQAEYL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEYCDGG--DLMQKIKQqkGKLFPEDMILNWFTQMCLGVNHIHKKR--VLHRDIKSKNIFLTQNGKVKLGDFGSARLL 152
Cdd:cd14036  83 LLTELCKGQlvDFVKKVEA--PGPFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQIKLCDFGSATTE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 153 SNPMAFA------------CTYVGTPYYVPPEI---WENLPYNNKSDIWSLGCILYELCTLKHPFQaNSWKnliLKVCQG 217
Cdd:cd14036 161 AHYPDYSwsaqkrslvedeITRNTTPMYRTPEMidlYSNYPIGEKQDIWALGCILYLLCFRKHPFE-DGAK---LRIINA 236
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 23510391 218 --CISPLPSHYSYeLQFLVKQMFKRNPSHRPSATTLL 252
Cdd:cd14036 237 kyTIPPNDTQYTV-FHDLIRSTLKVNPEERLSITEIV 272
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
3-253 2.30e-39

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: 143.89  E-value: 2.30e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQhESSNQMFAMKEIRLPKSFSNTQNS-RKEAVLLAKMKH-PNIVAFK--ESFEAEGHLYIV 78
Cdd:cd14131   2 PYEILKQLGKGGSSKVYKVL-NPKKKIYALKRVDLEGADEQTLQSyKNEIELLKKLKGsDRIIQLYdyEVTDEDDYLYMV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  79 MEYCDGgDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNiFLTQNGKVKLGDFGSARLL----SN 154
Cdd:cd14131  81 MECGEI-DLATILKKKRPKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPAN-FLLVKGRLKLIDFGIAKAIqndtTS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 155 PMAFacTYVGTPYYVPPEIWENLPYNN----------KSDIWSLGCILYELCTLKHPFQanSWKNLILKVCQGC----IS 220
Cdd:cd14131 159 IVRD--SQVGTLNYMSPEAIKDTSASGegkpkskigrPSDVWSLGCILYQMVYGKTPFQ--HITNPIAKLQAIIdpnhEI 234
                       250       260       270
                ....*....|....*....|....*....|...
gi 23510391 221 PLPSHYSYELQFLVKQMFKRNPSHRPSATTLLS 253
Cdd:cd14131 235 EFPDIPNPDLIDVMKRCLQRDPKKRPSIPELLN 267
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
2-245 3.35e-39

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: 144.08  E-value: 3.35e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKE------IRLpKSFSNTQNSRKeavLLAKMKHPNIVAFKESFEAEGHL 75
Cdd:cd14209   1 DDFDRIKTLGTGSFGRVMLVRHKETGNYYAMKIldkqkvVKL-KQVEHTLNEKR---ILQAINFPFLVKLEYSFKDNSNL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  76 YIVMEYCDGGDLMQKIkqQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNP 155
Cdd:cd14209  77 YMVMEYVPGGEMFSHL--RRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRVKGR 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 156 MAFACtyvGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISpLPSHYSYELQFLVK 235
Cdd:cd14209 155 TWTLC---GTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVR-FPSHFSSDLKDLLR 230
                       250
                ....*....|
gi 23510391 236 QMFKRNPSHR 245
Cdd:cd14209 231 NLLQVDLTKR 240
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
1-246 5.04e-39

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: 142.40  E-value: 5.04e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   1 MDDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEI---RLPKSFSNTQnSRKEAVLLAKMKHPNIVAFKESFEAEGHLYI 77
Cdd:cd14116   4 LEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLfkaQLEKAGVEHQ-LRREVEIQSHLRHPNILRLYGYFHDATRVYL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  78 VMEYCDGGDLMQKIkqQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSArlLSNPMA 157
Cdd:cd14116  83 ILEYAPLGTVYREL--QKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWS--VHAPSS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 158 FACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISpLPSHYSYELQFLVKQM 237
Cdd:cd14116 159 RRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFT-FPDFVTEGARDLISRL 237

                ....*....
gi 23510391 238 FKRNPSHRP 246
Cdd:cd14116 238 LKHNPSQRP 246
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
7-211 9.44e-39

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: 141.85  E-value: 9.44e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   7 LRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQ--NSRKE-AVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCD 83
Cdd:cd05611   1 LKPISKGAFGSVYLAKKRSTGDYFAIKVLKKSDMIAKNQvtNVKAErAIMMIQGESPYVAKLYYSFQSKDYLYLVMEYLN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  84 GGDLMQKIKQQKGklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSAR---LLSNPMAFac 160
Cdd:cd05611  81 GGDCASLIKTLGG--LPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSRnglEKRHNKKF-- 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 23510391 161 tyVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANS----WKNLI 211
Cdd:cd05611 157 --VGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETpdavFDNIL 209
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
8-245 1.06e-38

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: 143.29  E-value: 1.06e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSN-----TQNSRKeaVLLAKMKHPNIVAFKESFEAEGHLYIVMEYC 82
Cdd:cd05592   1 KVLGKGSFGKVMLAELKGTNQYFAIKALKKDVVLEDddvecTMIERR--VLALASQHPFLTHLFCTFQTESHLFFVMEYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  83 DGGDLMQKIkQQKGKlFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTY 162
Cdd:cd05592  79 NGGDLMFHI-QQSGR-FDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCKENIYGENKASTF 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 163 VGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGcISPLPSHYSYELQFLVKQMFKRNP 242
Cdd:cd05592 157 CGTPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICND-TPHYPRWLTKEAASCLSLLLERNP 235

                ...
gi 23510391 243 SHR 245
Cdd:cd05592 236 EKR 238
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
2-253 2.57e-38

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: 141.29  E-value: 2.57e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMK--------------EIRLPKSFSNtqnsrkeavllakmkHPNIVAFKE 67
Cdd:cd06608   6 GIFELVEVIGEGTYGKVYKARHKKTGQLAAIKimdiiedeeeeiklEINILRKFSN---------------HPNIATFYG 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  68 SFEAEGH------LYIVMEYCDGG---DLMQKIKQqKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQN 138
Cdd:cd06608  71 AFIKKDPpggddqLWLVMEYCGGGsvtDLVKGLRK-KGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEE 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 139 GKVKLGDFGSARLLSNPMAFACTYVGTPYYVPPEIW---ENL--PYNNKSDIWSLGCILYE-------LCTLkHPFQAns 206
Cdd:cd06608 150 AEVKLVDFGVSAQLDSTLGRRNTFIGTPYWMAPEVIacdQQPdaSYDARCDVWSLGITAIEladgkppLCDM-HPMRA-- 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 23510391 207 wknlILKVCQGCISPL--PSHYSYELQFLVKQMFKRNPSHRPSATTLLS 253
Cdd:cd06608 227 ----LFKIPRNPPPTLksPEKWSKEFNDFISECLIKNYEQRPFTEELLE 271
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
8-245 3.31e-38

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: 142.15  E-value: 3.31e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFGRALLVQH---ESSNQMFAMKEirLPKS---FSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd05582   1 KVLGQGSFGKVFLVRKitgPDAGTLYAMKV--LKKAtlkVRDRVRTKMERDILADVNHPFIVKLHYAFQTEGKLYLILDF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDLMQKIkqQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACT 161
Cdd:cd05582  79 LRGGDLFTRL--SKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKESIDHEKKAYS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 162 YVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWK---NLILKVCQGcispLPSHYSYELQFLVKQMF 238
Cdd:cd05582 157 FCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKetmTMILKAKLG----MPQFLSPEAQSLLRALF 232

                ....*..
gi 23510391 239 KRNPSHR 245
Cdd:cd05582 233 KRNPANR 239
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
9-245 6.59e-38

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: 139.76  E-value: 6.59e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   9 MIGEGSFGRALLVQH-ESSNQMFAMKEIRlPKSFSNTQNSR-KEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGD 86
Cdd:cd14202   9 LIGHGAFAVVFKGRHkEKHDLEVAVKCIN-KKNLAKSQTLLgKEIKILKELKHENIVALYDFQEIANSVYLVMEYCNGGD 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  87 LMQKIKQQKgkLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNG---------KVKLGDFGSARLLSNPMa 157
Cdd:cd14202  88 LADYLHTMR--TLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGgrksnpnniRIKIADFGFARYLQNNM- 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 158 FACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLIL--KVCQGCISPLPSHYSYELQFLVK 235
Cdd:cd14202 165 MAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQDLRLfyEKNKSLSPNIPRETSSHLRQLLL 244
                       250
                ....*....|
gi 23510391 236 QMFKRNPSHR 245
Cdd:cd14202 245 GLLQRNQKDR 254
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
3-252 1.69e-37

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: 138.78  E-value: 1.69e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLpksfsNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGH-------- 74
Cdd:cd14047   7 DFKEIELIGSGGFGQVFKAKHRIDGKTYAIKRVKL-----NNEKAEREVKALAKLDHPNIVRYNGCWDGFDYdpetsssn 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  75 --------LYIVMEYCDGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDF 146
Cdd:cd14047  82 ssrsktkcLFIQMEFCEKGTLESWIEKRNGEKLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGKVKIGDF 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 147 GSARLLSNPMAFACTYvGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCtlkHPFQANSWKNLILKVCQGCISPLPSHY 226
Cdd:cd14047 162 GLVTSLKNDGKRTKSK-GTLSYMSPEQISSQDYGKEVDIYALGLILFELL---HVCDSAFEKSKFWTDLRNGILPDIFDK 237
                       250       260
                ....*....|....*....|....*..
gi 23510391 227 SYELQF-LVKQMFKRNPSHRPSATTLL 252
Cdd:cd14047 238 RYKIEKtIIKKMLSKKPEDRPNASEIL 264
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
4-254 2.82e-37

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: 137.44  E-value: 2.82e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLP-KSFSNTQNSRKEAVLLAKMK-HPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd14050   3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKRSRSRfRGEKDRKRKLEEVERHEKLGeHPNCVRFIKAWEEKGILYIQTEL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGdlMQKIKQQKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGsarLLSNPMAFACT 161
Cdd:cd14050  83 CDTS--LQQYCEETHSL-PESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFG---LVVELDKEDIH 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 162 YV--GTPYYVPPEIWENLpYNNKSDIWSLGCILYEL-CTLKHPFQANSWKNLIlkvcQG-----CISPLPShysyELQFL 233
Cdd:cd14050 157 DAqeGDPRYMAPELLQGS-FTKAADIFSLGITILELaCNLELPSGGDGWHQLR----QGylpeeFTAGLSP----ELRSI 227
                       250       260
                ....*....|....*....|.
gi 23510391 234 VKQMFKRNPSHRPSATTLLSR 254
Cdd:cd14050 228 IKLMMDPDPERRPTAEDLLAL 248
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
9-253 3.14e-37

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: 137.95  E-value: 3.14e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   9 MIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNS-----RKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCD 83
Cdd:cd06630   7 LLGTGAFSSCYQARDVKTGTLMAVKQVSFCRNSSSEQEEvveaiREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEWMA 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  84 GGDLMQKIKQQKGklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGK-VKLGDFGSARLLSNPMA----F 158
Cdd:cd06630  87 GGSVASLLSKYGA--FSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGQrLRIADFGAAARLASKGTgageF 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 159 ACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKN---LILKV-CQGCISPLPSHYSYELQFLV 234
Cdd:cd06630 165 QGQLLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEKISNhlaLIFKIaSATTPPPIPEHLSPGLRDVT 244
                       250
                ....*....|....*....
gi 23510391 235 KQMFKRNPSHRPSATTLLS 253
Cdd:cd06630 245 LRCLELQPEDRPPARELLK 263
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
3-197 3.60e-37

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: 137.46  E-value: 3.60e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPK-SFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd14069   2 DWDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRaPGDCPENIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFLEY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDLMQKIKQQKGklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSA---------RLL 152
Cdd:cd14069  82 ASGGELFDKIEPDVG--MPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLAtvfrykgkeRLL 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 23510391 153 SNPmafactyVGTPYYVPPEIWENLPYN-NKSDIWSLGCILYELCT 197
Cdd:cd14069 160 NKM-------CGTLPYVAPELLAKKKYRaEPVDVWSCGIVLFAMLA 198
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
2-206 4.76e-37

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: 139.40  E-value: 4.76e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKeiRLPK----SFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYI 77
Cdd:cd05597   1 DDFEILKVIGRGAFGEVAVVKLKSTEKVYAMK--ILNKwemlKRAETACFREERDVLVNGDRRWITKLHYAFQDENYLYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  78 VMEYCDGGDLMQKIKQQKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSA-RLLSNPM 156
Cdd:cd05597  79 VMDYYCGGDLLTLLSKFEDRL-PEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFGSClKLREDGT 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 23510391 157 AFACTYVGTPYYVPPEIWENLP-----YNNKSDIWSLGCILYELCTLKHPFQANS 206
Cdd:cd05597 158 VQSSVAVGTPDYISPEILQAMEdgkgrYGPECDWWSLGVCMYEMLYGETPFYAES 212
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
2-252 5.07e-37

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: 138.44  E-value: 5.07e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSN----TQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYI 77
Cdd:cd14094   3 DVYELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFTSSpglsTEDLKREASICHMLKHPHIVELLETYSSDGMLYM 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  78 VMEYCDGGDLMQKIKQQ--KGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLT---QNGKVKLGDFGSARLL 152
Cdd:cd14094  83 VFEFMDGADLCFEIVKRadAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskeNSAPVKLGGFGVAIQL 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 153 SNPMAFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFqANSWKNLILKVCQGCIS---PLPSHYSYE 229
Cdd:cd14094 163 GESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF-YGTKERLFEGIIKGKYKmnpRQWSHISES 241
                       250       260
                ....*....|....*....|...
gi 23510391 230 LQFLVKQMFKRNPSHRPSATTLL 252
Cdd:cd14094 242 AKDLVRRMLMLDPAERITVYEAL 264
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
4-253 5.12e-37

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: 137.82  E-value: 5.12e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTqNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCD 83
Cdd:cd14166   5 FIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRDS-SLENEIAVLKRIKHENIVTLEDIYESTTHYYLVMQLVS 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  84 GGDLMQKIKQQkgKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKN-IFLT--QNGKVKLGDFGSARLLSNP-MAFA 159
Cdd:cd14166  84 GGELFDRILER--GVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENlLYLTpdENSKIMITDFGLSKMEQNGiMSTA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 160 CtyvGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCI---SPLPSHYSYELQFLVKQ 236
Cdd:cd14166 162 C---GTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGYYefeSPFWDDISESAKDFIRH 238
                       250
                ....*....|....*..
gi 23510391 237 MFKRNPSHRPSATTLLS 253
Cdd:cd14166 239 LLEKNPSKRYTCEKALS 255
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
4-252 6.27e-37

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: 137.00  E-value: 6.27e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCD 83
Cdd:cd14185   2 YEIGRTIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGKEDMIESEILIIKSLSHPNIVKLFEVYETEKEIYLILEYVR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  84 GGDLMQKIKQQKGklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNG----KVKLGDFGSARLLSNPMAFA 159
Cdd:cd14185  82 GGDLFDAIIESVK--FTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHNPdkstTLKLADFGLAKYVTGPIFTV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 160 CtyvGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSW-KNLILKVCQG----CISPLPSHYSYELQFLV 234
Cdd:cd14185 160 C---GTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRSPERdQEELFQIIQLghyeFLPPYWDNISEAAKDLI 236
                       250
                ....*....|....*...
gi 23510391 235 KQMFKRNPSHRPSATTLL 252
Cdd:cd14185 237 SRLLVVDPEKRYTAKQVL 254
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
4-249 6.64e-37

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: 138.09  E-value: 6.64e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKsFSNTQN-----SRKEAVLLAKMKHPNIVAFKESFEAEGHLYIV 78
Cdd:cd07841   2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGE-RKEAKDginftALREIKLLQELKHPNIIGLLDVFGHKSNINLV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  79 MEYCDGgDLMQKIKQQKGKLFPEDmILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAF 158
Cdd:cd07841  81 FEFMET-DLEKVIKDKSIVLTPAD-IKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLARSFGSPNRK 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 159 ACTYVGTPYYVPPEIwenL----PYNNKSDIWSLGCILYELCT-------------LKHPFQA------NSW---KNLIL 212
Cdd:cd07841 159 MTHQVVTRWYRAPEL---LfgarHYGVGVDMWSVGCIFAELLLrvpflpgdsdidqLGKIFEAlgtpteENWpgvTSLPD 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 23510391 213 KVCQGCISPLP-----SHYSYELQFLVKQMFKRNPSHRPSAT 249
Cdd:cd07841 236 YVEFKPFPPTPlkqifPAASDDALDLLQRLLTLNPNKRITAR 277
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
1-253 7.12e-37

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: 136.99  E-value: 7.12e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   1 MDDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIrlPKSFSNTQNSRK----EAVLLAKMKHPNIVAFKESFEAEGHLY 76
Cdd:cd14187   6 RRRYVRGRFLGKGGFAKCYEITDADTKEVFAGKIV--PKSLLLKPHQKEkmsmEIAIHRSLAHQHVVGFHGFFEDNDFVY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEYCDGGDLMQKIKQQKGKLFPEdmILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPM 156
Cdd:cd14187  84 VVLELCRRRSLLELHKRRKALTEPE--ARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKVEYDG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 157 AFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISpLPSHYSYELQFLVKQ 236
Cdd:cd14187 162 ERKKTLCGTPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYS-IPKHINPVAASLIQK 240
                       250
                ....*....|....*..
gi 23510391 237 MFKRNPSHRPSATTLLS 253
Cdd:cd14187 241 MLQTDPTARPTINELLN 257
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
10-253 7.57e-37

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: 136.24  E-value: 7.57e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKEIrlPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDLMQ 89
Cdd:cd14006   1 LGRGRFGVVKRCIEKATGREFAAKFI--PKRDKKKEAVLREISILNQLQHPRIIQLHEAYESPTELVLILELCSGGELLD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  90 KIKqQKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGK--VKLGDFGSARLLSNPMAFACTYvGTPY 167
Cdd:cd14006  79 RLA-ERGSL-SEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPSpqIKIIDFGLARKLNPGEELKEIF-GTPE 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 168 YVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCIS---PLPSHYSYELQFLVKQMFKRNPSH 244
Cdd:cd14006 156 FVAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVDfseEYFSSVSQEAKDFIRKLLVKEPRK 235

                ....*....
gi 23510391 245 RPSATTLLS 253
Cdd:cd14006 236 RPTAQEALQ 244
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
4-247 8.33e-37

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: 136.49  E-value: 8.33e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSN---TQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVME 80
Cdd:cd14070   4 YLIGRKLGEGSFAKVREGLHAVTGEKVAIKVIDKKKAKKDsyvTKNLRREGRIQQMIRHPNITQLLDILETENSYYLVME 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  81 YCDGGDLMQKIKQQkgKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFG---SARLL--SNP 155
Cdd:cd14070  84 LCPGGNLMHRIYDK--KRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGlsnCAGILgySDP 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 156 MAFACtyvGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQAN--SWKNLILKVCQGCISPLPSHYSYELQFL 233
Cdd:cd14070 162 FSTQC---GSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPFTVEpfSLRALHQKMVDKEMNPLPTDLSPGAISF 238
                       250
                ....*....|....
gi 23510391 234 VKQMFKRNPSHRPS 247
Cdd:cd14070 239 LRSLLEPDPLKRPN 252
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
2-253 1.64e-36

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: 136.40  E-value: 1.64e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEI-RLPKSFSNTQNSRkEAVLLAKMKHPNIVAFKESF--EAEGHLYIV 78
Cdd:cd06621   1 DKIVELSSLGEGAGGSVTKCRLRNTKTIFALKTItTDPNPDVQKQILR-ELEINKSCASPYIVKYYGAFldEQDSSIGIA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  79 MEYCDGGDL---MQKIKQQKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNp 155
Cdd:cd06621  80 MEYCEGGSLdsiYKKVKKKGGRI-GEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVSGELVN- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 156 mAFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLPS----------- 224
Cdd:cd06621 158 -SLAGTFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFPPEGEPPLGPIELLSYIVNMPNpelkdepengi 236
                       250       260
                ....*....|....*....|....*....
gi 23510391 225 HYSYELQFLVKQMFKRNPSHRPSATTLLS 253
Cdd:cd06621 237 KWSESFKDFIEKCLEKDGTRRPGPWQMLA 265
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
4-245 2.08e-36

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: 135.28  E-value: 2.08e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIrlPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCD 83
Cdd:cd14662   2 YELVKDIGSGNFGVARLMRNKETKELVAVKYI--ERGLKIDENVQREIINHRSLRHPNIIRFKEVVLTPTHLAIVMEYAA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  84 GGDLMQKIkQQKGKlFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQN--GKVKLGDFG---SARLLSNPMaf 158
Cdd:cd14662  80 GGELFERI-CNAGR-FSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSpaPRLKICDFGyskSSVLHSQPK-- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 159 acTYVGTPYYVPPEIWENLPYNNK-SDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCIS-----PLPSHYSYELQF 232
Cdd:cd14662 156 --STVGTPAYIAPEVLSRKEYDGKvADVWSCGVTLYVMLVGAYPFEDPDDPKNFRKTIQRIMSvqykiPDYVRVSQDCRH 233
                       250
                ....*....|...
gi 23510391 233 LVKQMFKRNPSHR 245
Cdd:cd14662 234 LLSRIFVANPAKR 246
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
4-247 2.09e-36

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: 135.47  E-value: 2.09e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQhESSNQMFAMKEIRLP--KSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd14161   5 YEFLETLGKGTYGRVKKAR-DSSGRLVAIKSIRKDriKDEQDLLHIRREIEIMSSLNHPHIISVYEVFENSSKIVIVMEY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDLMQKIKQQKGklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLsNPMAFACT 161
Cdd:cd14161  84 ASRGDLYDYISERQR--LSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSNLY-NQDKFLQT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 162 YVGTPYYVPPEIWENLPYNN-KSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPlPSHYSyELQFLVKQMFKR 240
Cdd:cd14161 161 YCGSPLYASPEIVNGRPYIGpEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISSGAYRE-PTKPS-DACGLIRWLLMV 238

                ....*..
gi 23510391 241 NPSHRPS 247
Cdd:cd14161 239 NPERRAT 245
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
7-291 3.32e-36

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: 136.31  E-value: 3.32e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   7 LRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNT--QNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDG 84
Cdd:cd06634  20 LREIGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNEkwQDIIKEVKFLQKLRHPNTIEYRGCYLREHTAWLVMEYCLG 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  85 G--DLMQKIKQQKgklfpEDMILNWFTQMCL-GVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLlsnpMAFACT 161
Cdd:cd06634 100 SasDLLEVHKKPL-----QEVEIAAITHGALqGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGSASI----MAPANS 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 162 YVGTPYYVPPEI---WENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLPS-HYSYELQFLVKQM 237
Cdd:cd06634 171 FVGTPYWMAPEVilaMDEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESPALQSgHWSEYFRNFVDSC 250
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 23510391 238 FKRNPSHRPSATTLLSRgivaRLVQKCLPPEIIMEY---GEEVLEEIKNSKHNTPRK 291
Cdd:cd06634 251 LQKIPQDRPTSDVLLKH----RFLLRERPPTVIMDLiqrTKDAVRELDNLQYRKMKK 303
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
4-253 3.61e-36

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: 134.91  E-value: 3.61e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEI---RLPKSFSNTQNSRkEAVLLAKMKHPNIVAFKESFEA-EGHLYIVM 79
Cdd:cd14165   3 YILGINLGEGSYAKVKSAYSERLKCNVAIKIIdkkKAPDDFVEKFLPR-ELEILARLNHKSIIKTYEIFETsDGKVYIVM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  80 EYCDGGDLMQKIKQQkGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLL----SNP 155
Cdd:cd14165  82 ELGVQGDLLEFIKLR-GAL-PEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRClrdeNGR 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 156 MAFACTYVGTPYYVPPEIWENLPYNNK-SDIWSLGCILYELCTLKHPF-QANSWKNLILKVCQGCISPLPSHYSYELQFL 233
Cdd:cd14165 160 IVLSKTFCGSAAYAAPEVLQGIPYDPRiYDIWSLGVILYIMVCGSMPYdDSNVKKMLKIQKEHRVRFPRSKNLTSECKDL 239
                       250       260
                ....*....|....*....|
gi 23510391 234 VKQMFKRNPSHRPSATTLLS 253
Cdd:cd14165 240 IYRLLQPDVSQRLCIDEVLS 259
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
2-206 3.69e-36

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: 138.60  E-value: 3.69e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNS--RKEAVLLAKMKHPNIVAFKESFEAEGHLYIVM 79
Cdd:cd05624  72 DDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRAETAcfREERNVLVNGDCQWITTLHYAFQDENYLYLVM 151
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  80 EYCDGGDLMQKIKQQKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSA-RLLSNPMAF 158
Cdd:cd05624 152 DYYVGGDLLTLLSKFEDKL-PEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFGSClKMNDDGTVQ 230
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 23510391 159 ACTYVGTPYYVPPEIWENL-----PYNNKSDIWSLGCILYELCTLKHPFQANS 206
Cdd:cd05624 231 SSVAVGTPDYISPEILQAMedgmgKYGPECDWWSLGVCMYEMLYGETPFYAES 283
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
10-245 3.80e-36

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: 135.18  E-value: 3.80e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKEI-------------RLPKSFSNTQNSR---------KEAVLLAKMKHPNIVAFKE 67
Cdd:cd14118   2 IGKGSYGIVKLAYNEEDNTLYAMKILskkkllkqagffrRPPPRRKPGALGKpldpldrvyREIAILKKLDHPNVVKLVE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  68 SFE--AEGHLYIVMEYCDGGDLMQKIKQqkgKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGD 145
Cdd:cd14118  82 VLDdpNEDNLYMVFELVDKGAVMEVPTD---NPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIAD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 146 FGSARLLSNPMAFACTYVGTPYYVPPE--IWENLPYNNKS-DIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPL 222
Cdd:cd14118 159 FGVSNEFEGDDALLSSTAGTPAFMAPEalSESRKKFSGKAlDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIKTDPVVFP 238
                       250       260
                ....*....|....*....|....
gi 23510391 223 PSHY-SYELQFLVKQMFKRNPSHR 245
Cdd:cd14118 239 DDPVvSEQLKDLILRMLDKNPSER 262
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
4-252 4.51e-36

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: 134.91  E-value: 4.51e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKH---PNIVAFKESFEAEGHLYIVME 80
Cdd:cd06917   3 YRRLELVGRGSYGAVYRGYHVKTGRVVALKVLNLDTDDDDVSDIQKEVALLSQLKLgqpKNIIKYYGSYLKGPSLWIIMD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  81 YCDGGDLMQKIKQQKGKlfpEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFAC 160
Cdd:cd06917  83 YCEGGSIRTLMRAGPIA---ERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQNSSKRS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 161 TYVGTPYYVPPE-IWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLP-SHYSYELQFLVKQMF 238
Cdd:cd06917 160 TFVGTPYWMAPEvITEGKYYDTKADIWSLGITTYEMATGNPPYSDVDALRAVMLIPKSKPPRLEgNGYSPLLKEFVAACL 239
                       250
                ....*....|....
gi 23510391 239 KRNPSHRPSATTLL 252
Cdd:cd06917 240 DEEPKDRLSADELL 253
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
10-253 4.53e-36

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: 134.74  E-value: 4.53e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHES--SNQMFAMKEIRLPKSFSNTQNSR----KEAVLLAKMKHPNIVafkESFE----AEGHLYIVM 79
Cdd:cd13994   1 IGKGATSVVRIVTKKNprSGVLYAVKEYRRRDDESKRKDYVkrltSEYIISSKLHHPNIV---KVLDlcqdLHGKWCLVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  80 EYCDGGDLMQKIKqqKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNP---- 155
Cdd:cd13994  78 EYCPGGDLFTLIE--KADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAEVFGMPaeke 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 156 MAFACTYVGTPYYVPPEIWENLPYNNKS-DIWSLGCILYELCTLKHPFQANSWKNLILKVCQG-----CISPLPSHYS-- 227
Cdd:cd13994 156 SPMSAGLCGSEPYMAPEVFTSGSYDGRAvDVWSCGIVLFALFTGRFPWRSAKKSDSAYKAYEKsgdftNGPYEPIENLlp 235
                       250       260
                ....*....|....*....|....*.
gi 23510391 228 YELQFLVKQMFKRNPSHRPSATTLLS 253
Cdd:cd13994 236 SECRRLIYRMLHPDPEKRITIDEALN 261
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
54-253 5.00e-36

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: 133.77  E-value: 5.00e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  54 LAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDLMQKIKQqkGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNI 133
Cdd:cd14059  35 LRKLNHPNIIKFKGVCTQAPCYCILMEYCPYGQLYEVLRA--GREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNV 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 134 FLTQNGKVKLGDFGSARLL---SNPMAFActyvGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNL 210
Cdd:cd14059 113 LVTYNDVLKISDFGTSKELsekSTKMSFA----GTVAWMAPEVIRNEPCSEKVDIWSFGVVLWELLTGEIPYKDVDSSAI 188
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 23510391 211 ILKVCQGCIS-PLPSHYSYELQFLVKQMFKRNPSHRPSATTLLS 253
Cdd:cd14059 189 IWGVGSNSLQlPVPSTCPDGFKLLMKQCWNSKPRNRPSFRQILM 232
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
2-206 6.65e-36

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: 135.90  E-value: 6.65e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNS--RKEAVLLAKMKHPNIVAFKESFEAEGHLYIVM 79
Cdd:cd05601   1 KDFEVKNVIGRGHFGEVQVVKEKATGDIYAMKVLKKSETLAQEEVSffEEERDIMAKANSPWITKLQYAFQDSENLYLVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  80 EYCDGGDLMQKIKQQKGkLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGS-ARLLSNPMAF 158
Cdd:cd05601  81 EYHPGGDLLSLLSRYDD-IFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSaAKLSSDKTVT 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 23510391 159 ACTYVGTPYYVPPEIWENLPYNNKS------DIWSLGCILYELCTLKHPFQANS 206
Cdd:cd05601 160 SKMPVGTPDYIAPEVLTSMNGGSKGtygvecDWWSLGIVAYEMLYGKTPFTEDT 213
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
4-253 8.23e-36

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: 134.94  E-value: 8.23e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNtqnsrKEAVLLAKMKHPNIVAFKESFEAEG------HLYI 77
Cdd:cd14137   6 YTIEKVIGSGSFGVVYQAKLLETGEVVAIKKVLQDKRYKN-----RELQIMRRLKHPNIVKLKYFFYSSGekkdevYLNL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  78 VMEYC--DGGDLMQKIKQQKGKLfpeDMIL--NWFTQMCLGVNHIHKKRVLHRDIKSKNIFL-TQNGKVKLGDFGSARLL 152
Cdd:cd14137  81 VMEYMpeTLYRVIRHYSKNKQTI---PIIYvkLYSYQLFRGLAYLHSLGICHRDIKPQNLLVdPETGVLKLCDFGSAKRL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 153 -----SNPmafactYVGTPYYVPPE-IWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKN---LILKV--------- 214
Cdd:cd14137 158 vpgepNVS------YICSRYYRAPElIFGATDYTTAIDIWSAGCVLAELLLGQPLFPGESSVDqlvEIIKVlgtptreqi 231
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 23510391 215 ---CQGCISP-------------LPSHYSYELQFLVKQMFKRNPSHRPSATTLLS 253
Cdd:cd14137 232 kamNPNYTEFkfpqikphpwekvFPKRTPPDAIDLLSKILVYNPSKRLTALEALA 286
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
4-252 8.23e-36

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: 133.80  E-value: 8.23e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEI-RLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYC 82
Cdd:cd14072   2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKIIdKTQLNPSSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEYA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  83 DGGDLMQ--------KIKQQKGKlfpedmilnwFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGsarlLSN 154
Cdd:cd14072  82 SGGEVFDylvahgrmKEKEARAK----------FRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFG----FSN 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 155 PMAFAC---TYVGTPYYVPPEIWENLPYNN-KSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISpLPSHYSYEL 230
Cdd:cd14072 148 EFTPGNkldTFCGSPPYAAPELFQGKKYDGpEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYR-IPFYMSTDC 226
                       250       260
                ....*....|....*....|..
gi 23510391 231 QFLVKQMFKRNPSHRPSATTLL 252
Cdd:cd14072 227 ENLLKKFLVLNPSKRGTLEQIM 248
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
4-252 8.67e-36

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: 133.51  E-value: 8.67e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIrlPKSFSNTQNSRKEAV----LLAKMKHPNIVAFKESFEAEGHLYIVM 79
Cdd:cd14189   3 YCKGRLLGKGGFARCYEMTDLATNKTYAVKVI--PHSRVAKPHQREKIVneieLHRDLHHKHVVKFSHHFEDAENIYIFL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  80 EYCDGGDLMQKIKQQKGKLFPEdmILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFA 159
Cdd:cd14189  81 ELCSRKSLAHIWKARHTLLEPE--VRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAARLEPPEQRK 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 160 CTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQanswkNLILKVCQGCISP----LPSHYSYELQFLVK 235
Cdd:cd14189 159 KTICGTPNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFE-----TLDLKETYRCIKQvkytLPASLSLPARHLLA 233
                       250
                ....*....|....*..
gi 23510391 236 QMFKRNPSHRPSATTLL 252
Cdd:cd14189 234 GILKRNPGDRLTLDQIL 250
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
10-253 8.78e-36

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: 135.12  E-value: 8.78e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKEIrlpksfSNTQNSRKEAVLLAKMK-HPNIVAFKESFEAEGHLYIVMEYCDGGDLM 88
Cdd:cd14092  14 LGDGSFSVCRKCVHKKTGQEFAVKIV------SRRLDTSREVQLLRLCQgHPNIVKLHEVFQDELHTYLVMELLRGGELL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  89 QKIKQQkgKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGK---VKLGDFGSARLL--SNPMAFACTyv 163
Cdd:cd14092  88 ERIRKK--KRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDDdaeIKIVDFGFARLKpeNQPLKTPCF-- 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 164 gTPYYVPPEIWENLP----YNNKSDIWSLGCILYELCTLKHPFQANSWKN----LILKVCQGCIS---PLPSHYSYELQF 232
Cdd:cd14092 164 -TLPYAAPEVLKQALstqgYDESCDLWSLGVILYTMLSGQVPFQSPSRNEsaaeIMKRIKSGDFSfdgEEWKNVSSEAKS 242
                       250       260
                ....*....|....*....|.
gi 23510391 233 LVKQMFKRNPSHRPSATTLLS 253
Cdd:cd14092 243 LIQGLLTVDPSKRLTMSELRN 263
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
3-257 9.04e-36

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: 134.00  E-value: 9.04e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPK--SFSNTQnsrKEAVLLAKMKHPNIVAFKESFEAEGHLYIVME 80
Cdd:cd06646  10 DYELIQRVGSGTYGDVYKARNLHTGELAAVKIIKLEPgdDFSLIQ---QEIFMVKECKHCNIVAYFGSYLSREKLWICME 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  81 YCDGGDLmQKIKQQKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFAC 160
Cdd:cd06646  87 YCGGGSL-QDIYHVTGPL-SELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAAKITATIAKRK 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 161 TYVGTPYYVPPEIW---ENLPYNNKSDIWSLGCILYELCTLKHP-FQANSWKNLILKVCQGCISPL---PSHYSYELQFL 233
Cdd:cd06646 165 SFIGTPYWMAPEVAaveKNGGYNQLCDIWAVGITAIELAELQPPmFDLHPMRALFLMSKSNFQPPKlkdKTKWSSTFHNF 244
                       250       260
                ....*....|....*....|....
gi 23510391 234 VKQMFKRNPSHRPSATTLLSRGIV 257
Cdd:cd06646 245 VKISLTKNPKKRPTAERLLTHLFV 268
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
4-253 9.73e-36

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: 133.55  E-value: 9.73e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNtqNSRKEAVLLAKMK------HPNIVAFKESFEAEGHLYI 77
Cdd:cd14133   1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKIIKNNKDYLD--QSLDEIRLLELLNkkdkadKYHIVRLKDVFYFKNHLCI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  78 VMEYCdGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGK--VKLGDFGSARLLSNP 155
Cdd:cd14133  79 VFELL-SQNLYEFLKQNKFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSRcqIKIIDFGSSCFLTQR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 156 MafaCTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVcQGCISPLPSHY-------SY 228
Cdd:cd14133 158 L---YSYIQSRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARI-IGTIGIPPAHMldqgkadDE 233
                       250       260
                ....*....|....*....|....*
gi 23510391 229 ELQFLVKQMFKRNPSHRPSATTLLS 253
Cdd:cd14133 234 LFVDFLKKLLEIDPKERPTASQALS 258
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
9-253 1.01e-35

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: 134.05  E-value: 1.01e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   9 MIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAV---------LLAKMKHPNIVAFKESFEAEGHLYIVM 79
Cdd:cd06629   8 LIGKGTYGRVYLAMNATTGEMLAVKQVELPKTSSDRADSRQKTVvdalkseidTLKDLDHPNIVQYLGFEETEDYFSIFL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  80 EYCDGGDLMQKIKQQkGKlFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMA-- 157
Cdd:cd06629  88 EYVPGGSIGSCLRKY-GK-FEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISKKSDDIYGnn 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 158 FACTYVGTPYYVPPEIWENLP--YNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKV-CQGCISPLPS--HYSYE-LQ 231
Cdd:cd06629 166 GATSMQGSVFWMAPEVIHSQGqgYSAKVDIWSLGCVVLEMLAGRRPWSDDEAIAAMFKLgNKRSAPPVPEdvNLSPEaLD 245
                       250       260
                ....*....|....*....|..
gi 23510391 232 FLVKqMFKRNPSHRPSATTLLS 253
Cdd:cd06629 246 FLNA-CFAIDPRDRPTAAELLS 266
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
7-245 1.10e-35

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: 135.21  E-value: 1.10e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   7 LRMIGEGSFGRALLVQHESSNQMFAmkeIRLPKSFSNTQNSRKEAVLLAKM------KHPNIVAFKESFEAEGHLYIVME 80
Cdd:cd05587   1 LMVLGKGSFGKVMLAERKGTDELYA---IKILKKDVIIQDDDVECTMVEKRvlalsgKPPFLTQLHSCFQTMDRLYFVME 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  81 YCDGGDLMQKIkQQKGKlFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFAC 160
Cdd:cd05587  78 YVNGGDLMYHI-QQVGK-FKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKEGIFGGKTTR 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 161 TYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISpLPSHYSYELQFLVKQMFKR 240
Cdd:cd05587 156 TFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVS-YPKSLSKEAVSICKGLLTK 234

                ....*
gi 23510391 241 NPSHR 245
Cdd:cd05587 235 HPAKR 239
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
3-245 1.31e-35

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: 133.34  E-value: 1.31e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHESSNQMFAMK--------------EIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKES 68
Cdd:cd14077   2 NWEFVKTIGAGSMGKVKLAKHIRTGEKCAIKiiprasnaglkkerEKRLEKEISRDIRTIREAALSSLLNHPHICRLRDF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  69 FEAEGHLYIVMEYCDGGDLMQKIKQQkGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGS 148
Cdd:cd14077  82 LRTPNHYYMLFEYVDGGQLLDYIISH-GKL-KEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 149 ARLLSNPMAFAcTYVGTPYYVPPEIWENLPYNN-KSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISpLPSHYS 227
Cdd:cd14077 160 SNLYDPRRLLR-TFCGSLYFAAPELLQAQPYTGpEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKIKKGKVE-YPSYLS 237
                       250
                ....*....|....*...
gi 23510391 228 YELQFLVKQMFKRNPSHR 245
Cdd:cd14077 238 SECKSLISRMLVVDPKKR 255
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
6-247 2.16e-35

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: 133.18  E-value: 2.16e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   6 VLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSfSNTQNSRKEAVLLAKMK-HPNIVAFKES---------FEaeghL 75
Cdd:cd14037   7 IEKYLAEGGFAHVYLVKTSNGGNRAALKRVYVNDE-HDLNVCKREIEIMKRLSgHKNIVGYIDSsanrsgngvYE----V 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  76 YIVMEYCDGG---DLMQKIKQQKgklFPEDMILNWFTQMCLGVNHIH--KKRVLHRDIKSKNIFLTQNGKVKLGDFGSA- 149
Cdd:cd14037  82 LLLMEYCKGGgviDLMNQRLQTG---LTESEILKIFCDVCEAVAAMHylKPPLIHRDLKVENVLISDSGNYKLCDFGSAt 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 150 RLLSNPMAFA-CTYV-------GTPYYVPPEI---WENLPYNNKSDIWSLGCILYELCTLKHPFQanswKNLILKVCQGC 218
Cdd:cd14037 159 TKILPPQTKQgVTYVeedikkyTTLQYRAPEMidlYRGKPITEKSDIWALGCLLYKLCFYTTPFE----ESGQLAILNGN 234
                       250       260       270
                ....*....|....*....|....*....|
gi 23510391 219 IS-PLPSHYSYELQFLVKQMFKRNPSHRPS 247
Cdd:cd14037 235 FTfPDNSRYSKRLHKLIRYMLEEDPEKRPN 264
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
7-291 2.64e-35

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: 134.01  E-value: 2.64e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   7 LRMIGEGSFGRALLVQHESSNQMFAMKEIrlpkSFSNTQNSRK------EAVLLAKMKHPNIVAFKESFEAEGHLYIVME 80
Cdd:cd06633  26 LHEIGHGSFGAVYFATNSHTNEVVAIKKM----SYSGKQTNEKwqdiikEVKFLQQLKHPNTIEYKGCYLKDHTAWLVME 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  81 YCDGG--DLMQKIKqqkgKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNpmaf 158
Cdd:cd06633 102 YCLGSasDLLEVHK----KPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIASP---- 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 159 ACTYVGTPYYVPPEI---WENLPYNNKSDIWSLGCILYELCTLKHP-FQANSWKNLiLKVCQGCISPLPSH-YSYELQFL 233
Cdd:cd06633 174 ANSFVGTPYWMAPEVilaMDEGQYDGKVDIWSLGITCIELAERKPPlFNMNAMSAL-YHIAQNDSPTLQSNeWTDSFRGF 252
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23510391 234 VKQMFKRNPSHRPSATTLLSRGIVARLvqkcLPPEIIMEY---GEEVLEEIKNSKHNTPRK 291
Cdd:cd06633 253 VDYCLQKIPQERPSSAELLRHDFVRRE----RPPRVLIDLiqrTKDAVRELDNLQYRKMKK 309
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
10-272 3.74e-35

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: 132.84  E-value: 3.74e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKEIRlPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGdLMQ 89
Cdd:cd06643  13 LGDGAFGKVYKAQNKETGILAAAKVID-TKSEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILIEFCAGG-AVD 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  90 KIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTYVGTPYYV 169
Cdd:cd06643  91 AVMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTRTLQRRDSFIGTPYWM 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 170 PPEI-----WENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPL--PSHYSYELQFLVKQMFKRNP 242
Cdd:cd06643 171 APEVvmcetSKDRPYDYKADVWSLGVTLIEMAQIEPPHHELNPMRVLLKIAKSEPPTLaqPSRWSPEFKDFLRKCLEKNV 250
                       250       260       270
                ....*....|....*....|....*....|
gi 23510391 243 SHRPSATTLLSRGIVARLVQKCLPPEIIME 272
Cdd:cd06643 251 DARWTTSQLLQHPFVSVLVSNKPLRELIAE 280
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
9-253 3.84e-35

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: 132.17  E-value: 3.84e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   9 MIGEGSFGRAL--LVqheSSNQMFAMKEIRLPKSFSNT-----QNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd06631   8 VLGKGAYGTVYcgLT---STGQLIAVKQVELDTSDKEKaekeyEKLQEEVDLLKTLKHVNIVGYLGTCLEDNVVSIFMEF 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDLMQkIKQQKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFAC- 160
Cdd:cd06631  85 VPGGSIAS-ILARFGAL-EEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGCAKRLCINLSSGSq 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 161 -----TYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVC--QGCISPLPSHYSYELQFL 233
Cdd:cd06631 163 sqllkSMRGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPWADMNPMAAIFAIGsgRKPVPRLPDKFSPEARDF 242
                       250       260
                ....*....|....*....|
gi 23510391 234 VKQMFKRNPSHRPSATTLLS 253
Cdd:cd06631 243 VHACLTRDQDERPSAEQLLK 262
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
4-245 5.56e-35

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: 131.65  E-value: 5.56e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSntQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCD 83
Cdd:cd14665   2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIERGEKID--ENVQREIINHRSLRHPNIVRFKEVILTPTHLAIVMEYAA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  84 GGDLMQKIkQQKGKlFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFL--TQNGKVKLGDFG---SARLLSNPMaf 158
Cdd:cd14665  80 GGELFERI-CNAGR-FSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLdgSPAPRLKICDFGyskSSVLHSQPK-- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 159 acTYVGTPYYVPPEIWENLPYNNK-SDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCIS-----PLPSHYSYELQF 232
Cdd:cd14665 156 --STVGTPAYIAPEVLLKKEYDGKiADVWSCGVTLYVMLVGAYPFEDPEEPRNFRKTIQRILSvqysiPDYVHISPECRH 233
                       250
                ....*....|...
gi 23510391 233 LVKQMFKRNPSHR 245
Cdd:cd14665 234 LISRIFVADPATR 246
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
1-252 7.16e-35

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: 131.41  E-value: 7.16e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   1 MDDYMvlrMIGEGSFGRALLVQHESSNQMFAMKEIRLPKsfsntQNSRK----EAVLLAKMKHPNIVAFKESFEAEGHLY 76
Cdd:cd06648   9 LDNFV---KIGEGSTGIVCIATDKSTGRQVAVKKMDLRK-----QQRREllfnEVVIMRDYQHPNIVEMYSSYLVGDELW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEYCDGGDLMQKIKQQKgklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPM 156
Cdd:cd06648  81 VVMEFLEGGALTDIVTHTR---MNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQVSKEV 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 157 AFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCT------LKHPFQAnswknliLKVCQGCISPLPSHY---S 227
Cdd:cd06648 158 PRRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDgeppyfNEPPLQA-------MKRIRDNEPPKLKNLhkvS 230
                       250       260
                ....*....|....*....|....*
gi 23510391 228 YELQFLVKQMFKRNPSHRPSATTLL 252
Cdd:cd06648 231 PRLRSFLDRMLVRDPAQRATAAELL 255
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
4-245 9.01e-35

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: 132.18  E-value: 9.01e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMF-AMKEIR------LPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLY 76
Cdd:cd14096   3 YRLINKIGEGAFSNVYKAVPLRNTGKPvAIKVVRkadlssDNLKGSSRANILKEVQIMKRLSHPNIVKLLDFQESDEYYY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEYCDGGDLMQKIKQQkgKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKN-----IFLTQN------------- 138
Cdd:cd14096  83 IVLELADGGEIFHQIVRL--TYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENllfepIPFIPSivklrkadddetk 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 139 ---------------GKVKLGDFGSARLLSNpmAFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQ 203
Cdd:cd14096 161 vdegefipgvggggiGIVKLADFGLSKQVWD--SNTKTPCGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFPPFY 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 23510391 204 ANSWKNLILKVCQG---CISPLPSHYSYELQFLVKQMFKRNPSHR 245
Cdd:cd14096 239 DESIETLTEKISRGdytFLSPWWDEISKSAKDLISHLLTVDPAKR 283
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
9-252 1.00e-34

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: 130.99  E-value: 1.00e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   9 MIGEGSFGRALLVQHESSNQMFAMKEIrlP-KSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDL 87
Cdd:cd06624  15 VLGKGTFGVVYAARDLSTQVRIAIKEI--PeRDSREVQPLHEEIALHSRLSHKNIVQYLGSVSEDGFFKIFMEQVPGGSL 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  88 MQKIKQQKGKLFPEDMILNWFTQMCL-GVNHIHKKRVLHRDIKSKNIFL-TQNGKVKLGDFGSARLLS--NPMafACTYV 163
Cdd:cd06624  93 SALLRSKWGPLKDNENTIGYYTKQILeGLKYLHDNKIVHRDIKGDNVLVnTYSGVVKISDFGTSKRLAgiNPC--TETFT 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 164 GTPYYVPPEIWENLP--YNNKSDIWSLGCILYELCTLKHPF------QANSWKNLILKvcqgcISP-LPSHYSYELQFLV 234
Cdd:cd06624 171 GTLQYMAPEVIDKGQrgYGPPADIWSLGCTIIEMATGKPPFielgepQAAMFKVGMFK-----IHPeIPESLSEEAKSFI 245
                       250
                ....*....|....*...
gi 23510391 235 KQMFKRNPSHRPSATTLL 252
Cdd:cd06624 246 LRCFEPDPDKRATASDLL 263
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
9-245 1.46e-34

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: 130.90  E-value: 1.46e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   9 MIGEGSFGRALLVQH-ESSNQMFAMKEIRlPKSFSNTQNSR-KEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGD 86
Cdd:cd14201  13 LVGHGAFAVVFKGRHrKKTDWEVAIKSIN-KKNLSKSQILLgKEIKILKELQHENIVALYDVQEMPNSVFLVMEYCNGGD 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  87 LMQKIkQQKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGK---------VKLGDFGSARLLSNPMa 157
Cdd:cd14201  92 LADYL-QAKGTL-SEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASRkkssvsgirIKIADFGFARYLQSNM- 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 158 FACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLIL--KVCQGCISPLPSHYSYELQFLVK 235
Cdd:cd14201 169 MAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQDLRMfyEKNKNLQPSIPRETSPYLADLLL 248
                       250
                ....*....|
gi 23510391 236 QMFKRNPSHR 245
Cdd:cd14201 249 GLLQRNQKDR 258
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
10-249 1.92e-34

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: 131.92  E-value: 1.92e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMK-----EIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDG 84
Cdd:cd05586   1 IGKGTFGQVYQVRKKDTRRIYAMKvlskkVIVAKKEVAHTIGERNILVRTALDESPFIVGLKFSFQTPTDLYLVTDYMSG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  85 GDLMQKIkQQKGKlFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTYVG 164
Cdd:cd05586  81 GELFWHL-QKEGR-FSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSKADLTDNKTTNTFCG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 165 TPYYVPPEI-WENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQMFKRNPS 243
Cdd:cd05586 159 TTEYLAPEVlLDEKGYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKVRFPKDVLSDEGRSFVKGLLNRNPK 238

                ....*.
gi 23510391 244 HRPSAT 249
Cdd:cd05586 239 HRLGAH 244
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
4-245 2.09e-34

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: 129.82  E-value: 2.09e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEI---RLPKSfsNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVME 80
Cdd:cd14071   2 YDIERTIGKGNFAVVKLARHRITKTEVAIKIIdksQLDEE--NLKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  81 YCDGGDLMQKIKQQkGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFAc 160
Cdd:cd14071  80 YASNGEIFDYLAQH-GRM-SEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSNFFKPGELLK- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 161 TYVGTPYYVPPEIWENLPYNN-KSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISpLPSHYSYELQFLVKQMFK 239
Cdd:cd14071 157 TWCGSPPYAAPEVFEGKEYEGpQLDIWSLGVVLYVLVCGALPFDGSTLQTLRDRVLSGRFR-IPFFMSTDCEHLIRRMLV 235

                ....*.
gi 23510391 240 RNPSHR 245
Cdd:cd14071 236 LDPSKR 241
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
3-252 2.26e-34

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: 129.81  E-value: 2.26e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNT-QNSRK------EAVLLAKMK---HPNIVAFKESFEAE 72
Cdd:cd14004   1 DYTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERILVDTwVRDRKlgtvplEIHILDTLNkrsHPNIVKLLDFFEDD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  73 GHLYIVME-YCDGGDLMQKIKQQKGKLFPEDMILnwFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARL 151
Cdd:cd14004  81 EFYYLVMEkHGSGMDLFDFIERKPNMDEKEAKYI--FRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFGSAAY 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 152 L-SNPMAfacTYVGTPYYVPPEIWENLPYNNKS-DIWSLGCILYELCTLKHPFQAnswknlILKVCQGCISPlPSHYSYE 229
Cdd:cd14004 159 IkSGPFD---TFVGTIDYAAPEVLRGNPYGGKEqDIWALGVLLYTLVFKENPFYN------IEEILEADLRI-PYAVSED 228
                       250       260
                ....*....|....*....|...
gi 23510391 230 LQFLVKQMFKRNPSHRPSATTLL 252
Cdd:cd14004 229 LIDLISRMLNRDVGDRPTIEELL 251
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
4-252 4.46e-34

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: 129.70  E-value: 4.46e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKeiRLPKSFSNTQ--NSRKEAVLLAKMK-HPNIVAFKES-FEAE-GHLYIV 78
Cdd:cd07831   1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIK--CMKKHFKSLEqvNNLREIQALRRLSpHPNILRLIEVlFDRKtGRLALV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  79 MEYCDGG--DLMQKIKQqkgkLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNgKVKLGDFGSARLLSNPM 156
Cdd:cd07831  79 FELMDMNlyELIKGRKR----PLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDD-ILKLADFGSCRGIYSKP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 157 AFAcTYVGTPYYVPPE-IWENLPYNNKSDIWSLGCILYELCTLkHP----------------------------FQANSW 207
Cdd:cd07831 154 PYT-EYISTRWYRAPEcLLTDGYYGPKMDIWAVGCVFFEILSL-FPlfpgtneldqiakihdvlgtpdaevlkkFRKSRH 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 23510391 208 KNLIL--KVCQGcISPLPSHYSYELQFLVKQMFKRNPSHRPSATTLL 252
Cdd:cd07831 232 MNYNFpsKKGTG-LRKLLPNASAEGLDLLKKLLAYDPDERITAKQAL 277
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
2-259 5.49e-34

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: 129.39  E-value: 5.49e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLP--KSFSNTQnsrKEAVLLAKMKHPNIVAFKESFEAEGHLYIVM 79
Cdd:cd06645  11 EDFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEpgEDFAVVQ---QEIIMMKDCKHSNIVAYFGSYLRRDKLWICM 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  80 EYCDGGDLmQKIKQQKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFA 159
Cdd:cd06645  88 EFCGGGSL-QDIYHVTGPL-SESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITATIAKR 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 160 CTYVGTPYYVPPEIW---ENLPYNNKSDIWSLGCILYELCTLKHP-FQANSWKNLILKVCQGCISPL---PSHYSYELQF 232
Cdd:cd06645 166 KSFIGTPYWMAPEVAaveRKGGYNQLCDIWAVGITAIELAELQPPmFDLHPMRALFLMTKSNFQPPKlkdKMKWSNSFHH 245
                       250       260
                ....*....|....*....|....*..
gi 23510391 233 LVKQMFKRNPSHRPSATTLLSRGIVAR 259
Cdd:cd06645 246 FVKMALTKNPKKRPTAEKLLQHPFVTQ 272
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
7-263 6.50e-34

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: 129.04  E-value: 6.50e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   7 LRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGD 86
Cdd:cd06641   9 LEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLGGGS 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  87 LMQKIkqQKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTYVGTP 166
Cdd:cd06641  89 ALDLL--EPGPL-DETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIKRN*FVGTP 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 167 YYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQMFKRNPSHRP 246
Cdd:cd06641 166 FWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIPKNNPPTLEGNYSKPLKEFVEACLNKEPSFRP 245
                       250
                ....*....|....*..
gi 23510391 247 SATTLLSRGIVARLVQK 263
Cdd:cd06641 246 TAKELLKHKFILRNAKK 262
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
4-206 7.09e-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: 129.33  E-value: 7.09e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLpksfsntqNSRKEAV---------LLAKMKHPNIVAFKESFEAEGH 74
Cdd:cd07835   1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKIRL--------ETEDEGVpstaireisLLKELNHPNIVRLLDVVHSENK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  75 LYIVMEYCDGgDL---MQKIKQQKgklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARL 151
Cdd:cd07835  73 LYLVFEFLDL-DLkkyMDSSPLTG---LDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLARA 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 23510391 152 LSNPMAfacTY---VGTPYYVPPEIWENLP-YNNKSDIWSLGCILYELCTLKHPFQANS 206
Cdd:cd07835 149 FGVPVR---TYtheVVTLWYRAPEILLGSKhYSTPVDIWSVGCIFAEMVTRRPLFPGDS 204
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
8-245 7.78e-34

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: 130.13  E-value: 7.78e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQ--NSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGG 85
Cdd:cd05595   1 KLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEvaHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  86 DLMQKIKQQKgkLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTYVGT 165
Cdd:cd05595  81 ELFFHLSRER--VFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGITDGATMKTFCGT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 166 PYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISpLPSHYSYELQFLVKQMFKRNPSHR 245
Cdd:cd05595 159 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIR-FPRTLSPEAKSLLAGLLKKDPKQR 237
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
2-291 9.94e-34

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: 129.08  E-value: 9.94e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPK-SFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVME 80
Cdd:cd14086   1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKlSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  81 YCDGGDLMQKIKQQkgKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFL---TQNGKVKLGDFGSARLLSNPMA 157
Cdd:cd14086  81 LVTGGELFEDIVAR--EFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLaskSKGAAVKLADFGLAIEVQGDQQ 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 158 FACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCI---SPLPSHYSYELQFLV 234
Cdd:cd14086 159 AWFGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYdypSPEWDTVTPEAKDLI 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 23510391 235 KQMFKRNPSHRPSATTLLSRGIVARLVQKClppeiIMEYGEEVLEEIKnsKHNTPRK 291
Cdd:cd14086 239 NQMLTVNPAKRITAAEALKHPWICQRDRVA-----SMVHRQETVDCLK--KFNARRK 288
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
48-206 1.53e-33

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 411126 [Multi-domain]  Cd Length: 563  Bit Score: 133.77  E-value: 1.53e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   48 RKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDLMQKIkQQKGKLFPEDmILNWFTQMCLGVNHIHKKRVLHRD 127
Cdd:NF033483  55 RREAQSAASLSHPNIVSVYDVGEDGGIPYIVMEYVDGRTLKDYI-REHGPLSPEE-AVEIMIQILSALEHAHRNGIVHRD 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  128 IKSKNIFLTQNGKVKLGDFGSARLLSN-PMAFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANS 206
Cdd:NF033483 133 IKPQNILITKDGRVKVTDFGIARALSStTMTQTNSVLGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFDGDS 212
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
4-253 1.55e-33

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: 127.70  E-value: 1.55e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLpKSFSNTQnSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCD 83
Cdd:cd14107   4 YEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIPL-RSSTRAR-AFQERDILARLSHRRLTCLLDQFETRKTLILILELCS 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  84 GGDLMQKIkQQKGKLFPEDMILnWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGK--VKLGDFGSARLLSnPMAFACT 161
Cdd:cd14107  82 SEELLDRL-FLKGVVTEAEVKL-YIQQVLEGIGYLHGMNILHLDIKPDNILMVSPTRedIKICDFGFAQEIT-PSEHQFS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 162 YVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCIS---PLPSHYSYELQFLVKQMF 238
Cdd:cd14107 159 KYGSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVVSwdtPEITHLSEDAKDFIKRVL 238
                       250
                ....*....|....*
gi 23510391 239 KRNPSHRPSATTLLS 253
Cdd:cd14107 239 QPDPEKRPSASECLS 253
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
7-263 1.61e-33

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: 128.25  E-value: 1.61e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   7 LRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGD 86
Cdd:cd06642   9 LERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIMEYLGGGS 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  87 LMQKIKqqKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTYVGTP 166
Cdd:cd06642  89 ALDLLK--PGPL-EETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRNTFVGTP 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 167 YYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQMFKRNPSHRP 246
Cdd:cd06642 166 FWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDLHPMRVLFLIPKNSPPTLEGQHSKPFKEFVEACLNKDPRFRP 245
                       250
                ....*....|....*..
gi 23510391 247 SATTLLSRGIVARLVQK 263
Cdd:cd06642 246 TAKELLKHKFITRYTKK 262
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
2-197 1.85e-33

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: 128.26  E-value: 1.85e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEirlpksFSNTQNS---RKEAV----LLAKMKHPNIVAFKESFEAEGH 74
Cdd:cd07847   1 EKYEKLSKIGEGSYGVVFKCRNRETGQIVAIKK------FVESEDDpviKKIALreirMLKQLKHPNLVNLIEVFRRKRK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  75 LYIVMEYCDGGDLMQKIKQQKGklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSN 154
Cdd:cd07847  75 LHLVFEYCDHTVLNELEKNPRG--VPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARILTG 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 23510391 155 PMAFACTYVGTPYYVPPE-IWENLPYNNKSDIWSLGCILYELCT 197
Cdd:cd07847 153 PGDDYTDYVATRWYRAPElLVGDTQYGPPVDVWAIGCVFAELLT 196
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
10-247 1.97e-33

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: 127.02  E-value: 1.97e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSN-QMFAMKEI---RLPKSfsNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGG 85
Cdd:cd14121   3 LGSGTYATVYKAYRKSGArEVVAVKCVsksSLNKA--STENLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYCSGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  86 DLMQKIKQQkgKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKV--KLGDFGSARLLSnPMAFACTYV 163
Cdd:cd14121  81 DLSRFIRSR--RTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYNPvlKLADFGFAQHLK-PNDEAHSLR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 164 GTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLPS--HYSYELQFLVKQMFKRN 241
Cdd:cd14121 158 GSPLYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFASRSFEELEEKIRSSKPIEIPTrpELSADCRDLLLRLLQRD 237

                ....*.
gi 23510391 242 PSHRPS 247
Cdd:cd14121 238 PDRRIS 243
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
4-214 2.23e-33

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: 129.18  E-value: 2.23e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKeiRLPKSFSNTQNSRK---EAVLLAKMKHPNIVAFK-----ESFEAEGHL 75
Cdd:cd07834   2 YELLKPIGSGAYGVVCSAYDKRTGRKVAIK--KISNVFDDLIDAKRilrEIKILRHLKHENIIGLLdilrpPSPEEFNDV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  76 YIVMEYCDGgDLMQKIKQQKgKLFPEDMilNWFT-QMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLL-S 153
Cdd:cd07834  80 YIVTELMET-DLHKVIKSPQ-PLTDDHI--QYFLyQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGLARGVdP 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23510391 154 NPMAFACT-YVGTPYYVPPEI---WENlpYNNKSDIWSLGCILYELCTLKHPFQANSWK---NLILKV 214
Cdd:cd07834 156 DEDKGFLTeYVVTRWYRAPELllsSKK--YTKAIDIWSVGCIFAELLTRKPLFPGRDYIdqlNLIVEV 221
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
2-206 2.41e-33

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: 129.42  E-value: 2.41e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKeiRLPKsFSNTQNSR-----KEAVLLAKMKHPNIVAFKESFEAEGHLY 76
Cdd:cd05596  26 EDFDVIKVIGRGAFGEVQLVRHKSTKKVYAMK--LLSK-FEMIKRSDsaffwEERDIMAHANSEWIVQLHYAFQDDKYLY 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEYCDGGDLMQKIKQQKgklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSA-RLLSNP 155
Cdd:cd05596 103 MVMDYMPGGDLVNLMSNYD---VPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFGTCmKMDKDG 179
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 23510391 156 MAFACTYVGTPYYVPPEIWENLP----YNNKSDIWSLGCILYELCTLKHPFQANS 206
Cdd:cd05596 180 LVRSDTAVGTPDYISPEVLKSQGgdgvYGRECDWWSVGVFLYEMLVGDTPFYADS 234
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
2-206 3.01e-33

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: 130.52  E-value: 3.01e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNS--RKEAVLLAKMKHPNIVAFKESFEAEGHLYIVM 79
Cdd:cd05623  72 EDFEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAETAcfREERDVLVNGDSQWITTLHYAFQDDNNLYLVM 151
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  80 EYCDGGDLMQKIKQQKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSA-RLLSNPMAF 158
Cdd:cd05623 152 DYYVGGDLLTLLSKFEDRL-PEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGSClKLMEDGTVQ 230
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 23510391 159 ACTYVGTPYYVPPEIWENLP-----YNNKSDIWSLGCILYELCTLKHPFQANS 206
Cdd:cd05623 231 SSVAVGTPDYISPEILQAMEdgkgkYGPECDWWSLGVCMYEMLYGETPFYAES 283
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
8-252 3.29e-33

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: 126.67  E-value: 3.29e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFGRALLVQHESSNQMFAMKEIrlPKSFSNTQNSR----KEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCD 83
Cdd:cd14188   7 KVLGKGGFAKCYEMTDLTTNKVYAAKII--PHSRVSKPHQRekidKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  84 GGDLMQKIKQQKGKLFPEdmILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTYV 163
Cdd:cd14188  85 RRSMAHILKARKVLTEPE--VRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLEPLEHRRRTIC 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 164 GTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSwknliLKVCQGCIS----PLPSHYSYELQFLVKQMFK 239
Cdd:cd14188 163 GTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTN-----LKETYRCIRearySLPSSLLAPAKHLIASMLS 237
                       250
                ....*....|...
gi 23510391 240 RNPSHRPSATTLL 252
Cdd:cd14188 238 KNPEDRPSLDEII 250
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
4-252 3.73e-33

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: 126.49  E-value: 3.73e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRlpKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCD 83
Cdd:cd14087   3 YDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIE--TKCRGREVCESELNVLRRVRHTNIIQLIEVFETKERVYMVMELAT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  84 GGDLMQKIKQqKGKLFPEDMilNWFTQMCL-GVNHIHKKRVLHRDIKSKNIFLTQNG---KVKLGDFG--SARLlSNPMA 157
Cdd:cd14087  81 GGELFDRIIA-KGSFTERDA--TRVLQMVLdGVKYLHGLGITHRDLKPENLLYYHPGpdsKIMITDFGlaSTRK-KGPNC 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 158 FACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLPSHYSyELQFLVKQM 237
Cdd:cd14087 157 LMKTTCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSYSGEPWP-SVSNLAKDF 235
                       250
                ....*....|....*....
gi 23510391 238 FKR----NPSHRPSATTLL 252
Cdd:cd14087 236 IDRlltvNPGERLSATQAL 254
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
2-254 6.46e-33

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: 126.79  E-value: 6.46e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRL-PKSFSNTQNSRkEAVLLAKMKHPNIVAFKESFEAE-GHLYIVM 79
Cdd:cd06620   5 QDLETLKDLGAGNGGSVSKVLHIPTGTIMAKKVIHIdAKSSVRKQILR-ELQILHECHSPYIVSFYGAFLNEnNNIIICM 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  80 EYCDGGDLmQKIKQQKGKlFPEDMILNWFTQMCLGVNHIHKK-RVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNpmAF 158
Cdd:cd06620  84 EYMDCGSL-DKILKKKGP-FPEEVLGKIAVAVLEGLTYLYNVhRIIHRDIKPSNILVNSKGQIKLCDFGVSGELIN--SI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 159 ACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNL-------ILKVCQgCI----SP-LPS-- 224
Cdd:cd06620 160 ADTFVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFAGSNDDDDgyngpmgILDLLQ-RIvnepPPrLPKdr 238
                       250       260       270
                ....*....|....*....|....*....|
gi 23510391 225 HYSYELQFLVKQMFKRNPSHRPSATTLLSR 254
Cdd:cd06620 239 IFPKDLRDFVDRCLLKDPRERPSPQLLLDH 268
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
1-245 7.16e-33

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: 128.27  E-value: 7.16e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   1 MDDYMVLRMIGEGSFGRALLVQHESSNQMFAMK----EIRLPKSfsNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLY 76
Cdd:cd05593  14 MNDFDYLKLLGKGTFGKVILVREKASGKYYAMKilkkEVIIAKD--EVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLC 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEYCDGGDLMQKIKQQKgkLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPM 156
Cdd:cd05593  92 FVMEYVNGGELFFHLSRER--VFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDA 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 157 AFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISpLPSHYSYELQFLVKQ 236
Cdd:cd05593 170 ATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIK-FPRTLSADAKSLLSG 248

                ....*....
gi 23510391 237 MFKRNPSHR 245
Cdd:cd05593 249 LLIKDPNKR 257
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
3-252 7.18e-33

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: 126.59  E-value: 7.18e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKsfsntQNSRKEA-VLLAKMKHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd14091   1 EYEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDKSK-----RDPSEEIeILLRYGQHPNIITLRDVYDDGNSVYLVTEL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDLMQKIKQQkgKLFPED---MILNWFTQMclgVNHIHKKRVLHRDIKSKNI-FLTQNGK---VKLGDFGSARLL-- 152
Cdd:cd14091  76 LRGGELLDRILRQ--KFFSEReasAVMKTLTKT---VEYLHSQGVVHRDLKPSNIlYADESGDpesLRICDFGFAKQLra 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 153 SNPMAFACTYvgTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQA--NSWKNLILK-VCQGCI---SPLPSHY 226
Cdd:cd14091 151 ENGLLMTPCY--TANFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPFASgpNDTPEVILArIGSGKIdlsGGNWDHV 228
                       250       260
                ....*....|....*....|....*.
gi 23510391 227 SYELQFLVKQMFKRNPSHRPSATTLL 252
Cdd:cd14091 229 SDSAKDLVRKMLHVDPSQRPTAAQVL 254
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
2-206 8.16e-33

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: 127.43  E-value: 8.16e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQ--NSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVM 79
Cdd:cd05598   1 SMFEKIKTIGVGAFGEVSLVRKKDTNALYAMKTLRKKDVLKRNQvaHVKAERDILAEADNEWVVKLYYSFQDKENLYFVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  80 EYCDGGDLMQK-IKqqKGkLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFG----------S 148
Cdd:cd05598  81 DYIPGGDLMSLlIK--KG-IFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGlctgfrwthdS 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 23510391 149 ARLLsnpmafACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANS 206
Cdd:cd05598 158 KYYL------AHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAQT 209
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
1-245 1.18e-32

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: 126.96  E-value: 1.18e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   1 MDDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIR-----LPKSFSNTQNSRKeaVLLAKMKHPNIVAFKESFEAEGHL 75
Cdd:cd05619   4 IEDFVLHKMLGKGSFGKVFLAELKGTNQFFAIKALKkdvvlMDDDVECTMVEKR--VLSLAWEHPFLTHLFCTFQTKENL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  76 YIVMEYCDGGDLMQKIkqQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNP 155
Cdd:cd05619  82 FFVMEYLNGGDLMFHI--QSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKENMLG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 156 MAFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGciSPL-PSHYSYELQFLV 234
Cdd:cd05619 160 DAKTSTFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSIRMD--NPFyPRWLEKEAKDIL 237
                       250
                ....*....|.
gi 23510391 235 KQMFKRNPSHR 245
Cdd:cd05619 238 VKLFVREPERR 248
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
1-249 1.71e-32

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: 125.37  E-value: 1.71e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   1 MDDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEA--------- 71
Cdd:cd14048   5 LTDFEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRIRLPNNELAREKVLREVRALAKLDHPGIVRYFNAWLErppegwqek 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  72 --EGHLYIVMEYCDGGDLMQKIKQQKG-KLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGS 148
Cdd:cd14048  85 mdEVYLYIQMQLCRKENLKDWMNRRCTmESRELFVCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVGDFGL 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 149 A----------RLLSNPMAFA--CTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCtlkHPFQANSWKNLILK-VC 215
Cdd:cd14048 165 VtamdqgepeqTVLTPMPAYAkhTGQVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELI---YSFSTQMERIRTLTdVR 241
                       250       260       270
                ....*....|....*....|....*....|....
gi 23510391 216 QGCISPLPSHYSYELQFLVKQMFKRNPSHRPSAT 249
Cdd:cd14048 242 KLKFPALFTNKYPEERDMVQQMLSPSPSERPEAH 275
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
2-245 1.84e-32

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: 124.75  E-value: 1.84e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRlPKSFSNTQNS-RKEAVLLAKMKHPNIVAFKESFEAEGHLYIVME 80
Cdd:cd14167   3 DIYDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIA-KKALEGKETSiENEIAVLHKIKHPNIVALDDIYESGGHLYLIMQ 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  81 YCDGGDLMQKIkQQKGkLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIF---LTQNGKVKLGDFGSARlLSNPMA 157
Cdd:cd14167  82 LVSGGELFDRI-VEKG-FYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGLSK-IEGSGS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 158 FACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNL---ILKVCQGCISPLPSHYSYELQFLV 234
Cdd:cd14167 159 VMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLfeqILKAEYEFDSPYWDDISDSAKDFI 238
                       250
                ....*....|.
gi 23510391 235 KQMFKRNPSHR 245
Cdd:cd14167 239 QHLMEKDPEKR 249
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
2-280 1.85e-32

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: 125.35  E-value: 1.85e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd06622   1 DEIEVLDELGKGNYGSVYKVLHRPTGVTMAMKEIRLELDESKFNQIIMELDILHKAVSPYIVDFYGAFFIEGAVYMCMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDlMQKI--KQQKGKLFPEDMILNWFTQMCLGVNHIHKK-RVLHRDIKSKNIFLTQNGKVKLGDFG-SARLLSnpmA 157
Cdd:cd06622  81 MDAGS-LDKLyaGGVATEGIPEDVLRRITYAVVKGLKFLKEEhNIIHRDVKPTNVLVNGNGQVKLCDFGvSGNLVA---S 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 158 FACTYVGTPYYVPPE------IWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILK---VCQGCISPLPSHYSY 228
Cdd:cd06622 157 LAKTNIGCQSYMAPEriksggPNQNPTYTVQSDVWSLGLSILEMALGRYPYPPETYANIFAQlsaIVDGDPPTLPSGYSD 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 23510391 229 ELQFLVKQMFKRNPSHRPSATTLLSRGIVARLVQkclpPEIIM-EYGEEVLEE 280
Cdd:cd06622 237 DAQDFVAKCLNKIPNRRPTYAQLLEHPWLVKYKN----ADVDMaEWVTGALKR 285
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
7-263 2.49e-32

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: 124.78  E-value: 2.49e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   7 LRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGD 86
Cdd:cd06640   9 LERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIMEYLGGGS 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  87 LMQKIKQQKgklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTYVGTP 166
Cdd:cd06640  89 ALDLLRAGP---FDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRNTFVGTP 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 167 YYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQMFKRNPSHRP 246
Cdd:cd06640 166 FWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPPNSDMHPMRVLFLIPKNNPPTLVGDFSKPFKEFIDACLNKDPSFRP 245
                       250
                ....*....|....*..
gi 23510391 247 SATTLLSRGIVARLVQK 263
Cdd:cd06640 246 TAKELLKHKFIVKNAKK 262
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
3-206 3.42e-32

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: 124.45  E-value: 3.42e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSR-KEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd07861   1 DYTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIRLESEEEGVPSTAiREISLLKELQHPNIVCLEDVLMQENRLYLVFEF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 --CDGGDLMQKIKqqKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFA 159
Cdd:cd07861  81 lsMDLKKYLDSLP--KGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARAFGIPVRVY 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 23510391 160 CTYVGTPYYVPPEIWENLP-YNNKSDIWSLGCILYELCTLKHPFQANS 206
Cdd:cd07861 159 THEVVTLWYRAPEVLLGSPrYSTPVDIWSIGTIFAEMATKKPLFHGDS 206
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
1-245 4.05e-32

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: 125.88  E-value: 4.05e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   1 MDDYMVLRMIGEGSFGRALLVQHESSNQMFAmkeIRLPKSFSNTQNSRKEAVLLAKM------KHPNIVAFKESFEAEGH 74
Cdd:cd05615   9 LTDFNFLMVLGKGSFGKVMLAERKGSDELYA---IKILKKDVVIQDDDVECTMVEKRvlalqdKPPFLTQLHSCFQTVDR 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  75 LYIVMEYCDGGDLMQKIkQQKGKlFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSN 154
Cdd:cd05615  86 LYFVMEYVNGGDLMYHI-QQVGK-FKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMV 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 155 PMAFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISpLPSHYSYELQFLV 234
Cdd:cd05615 164 EGVTTRTFCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVS-YPKSLSKEAVSIC 242
                       250
                ....*....|.
gi 23510391 235 KQMFKRNPSHR 245
Cdd:cd05615 243 KGLMTKHPAKR 253
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
3-245 4.47e-32

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: 125.50  E-value: 4.47e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHESSNQMFAMKeirLPKSFSNTQNSRKEAVLLAKM------KHPNIVAFKESFEAEGHLY 76
Cdd:cd05616   1 DFNFLMVLGKGSFGKVMLAERKGTDELYAVK---ILKKDVVIQDDDVECTMVEKRvlalsgKPPFLTQLHSCFQTMDRLY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEYCDGGDLMQKIkQQKGKlFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPM 156
Cdd:cd05616  78 FVMEYVNGGDLMYHI-QQVGR-FKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 157 AFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISpLPSHYSYELQFLVKQ 236
Cdd:cd05616 156 VTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVA-YPKSMSKEAVAICKG 234

                ....*....
gi 23510391 237 MFKRNPSHR 245
Cdd:cd05616 235 LMTKHPGKR 243
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
8-245 4.83e-32

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: 125.30  E-value: 4.83e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFGRALLVQHESSNQMFAMK----EIRLPKSFSNTQNSRKEAVLLAKmKHPNIVAFKESFEAEGHLYIVMEYCD 83
Cdd:cd05591   1 KVLGKGSFGKVMLAERKGTDEVYAIKvlkkDVILQDDDVDCTMTEKRILALAA-KHPFLTALHSCFQTKDRLFFVMEYVN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  84 GGDLMQKIkqQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTYV 163
Cdd:cd05591  80 GGDLMFQI--QRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGKTTTTFC 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 164 GTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISpLPSHYSYELQFLVKQMFKRNPS 243
Cdd:cd05591 158 GTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVL-YPVWLSKEAVSILKAFMTKNPA 236

                ..
gi 23510391 244 HR 245
Cdd:cd05591 237 KR 238
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
3-245 6.37e-32

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: 125.03  E-value: 6.37e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHES---SNQMFAMKEIR---LPKSFSNTQNSRKEAVLLAKMKH-PNIVAFKESFEAEGHL 75
Cdd:cd05614   1 NFELLKVLGTGAYGKVFLVRKVSghdANKLYAMKVLRkaaLVQKAKTVEHTRTERNVLEHVRQsPFLVTLHYAFQTDAKL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  76 YIVMEYCDGGDLMQKIKQQKGklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFG-SARLLSN 154
Cdd:cd05614  81 HLILDYVSGGELFTHLYQRDH--FSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGlSKEFLTE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 155 PMAFACTYVGTPYYVPPEIWENLPYNNKS-DIWSLGCILYELCTLKHPFQANSWKNLILKVCQ---GCISPLPSHYSYEL 230
Cdd:cd05614 159 EKERTYSFCGTIEYMAPEIIRGKSGHGKAvDWWSLGILMFELLTGASPFTLEGEKNTQSEVSRrilKCDPPFPSFIGPVA 238
                       250
                ....*....|....*
gi 23510391 231 QFLVKQMFKRNPSHR 245
Cdd:cd05614 239 RDLLQKLLCKDPKKR 253
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
10-219 6.82e-32

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: 124.10  E-value: 6.82e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKE--IRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKE-----SFEAEGHLYIV-MEY 81
Cdd:cd13989   1 LGSGGFGYVTLWKHQDTGEYVAIKKcrQELSPSDKNRERWCLEVQIMKKLNHPNVVSARDvppelEKLSPNDLPLLaMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDLMQKIKQQKGKL-FPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQ-NGKV--KLGDFGSARLLSNpmA 157
Cdd:cd13989  81 CSGGDLRKVLNQPENCCgLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQgGGRViyKLIDLGYAKELDQ--G 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23510391 158 FACT-YVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANS----WKNLILKVCQGCI 219
Cdd:cd13989 159 SLCTsFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPFLPNWqpvqWHGKVKQKKPEHI 225
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
8-251 7.45e-32

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: 124.63  E-value: 7.45e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFGRALLVQHESSNQMFAMKEIR----LPKSFSNTQNSRKEAVLLAKmKHPNIVAFKESFEAEGHLYIVMEYCD 83
Cdd:cd05590   1 RVLGKGSFGKVMLARLKESGRLYAVKVLKkdviLQDDDVECTMTEKRILSLAR-NHPFLTQLYCCFQTPDRLFFVMEFVN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  84 GGDLMQKIkqQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTYV 163
Cdd:cd05590  80 GGDLMFHI--QKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGIFNGKTTSTFC 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 164 GTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISpLPSHYSYELQFLVKQMFKRNPS 243
Cdd:cd05590 158 GTPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVV-YPTWLSQDAVDILKAFMTKNPT 236

                ....*...
gi 23510391 244 HRPSATTL 251
Cdd:cd05590 237 MRLGSLTL 244
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
2-252 8.44e-32

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: 123.69  E-value: 8.44e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLpksfsnTQNSRKEAVLLAKMK-------HPNIVAFKESFEAEGH 74
Cdd:cd06617   1 DDLEVIEELGRGAYGVVDKMRHVPTGTIMAVKRIRA------TVNSQEQKRLLMDLDismrsvdCPYTVTFYGALFREGD 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  75 LYIVMEYCDGG-DLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKK-RVLHRDIKSKNIFLTQNGKVKLGDFGSARLL 152
Cdd:cd06617  75 VWICMEVMDTSlDKFYKKVYDKGLTIPEDILGKIAVSIVKALEYLHSKlSVIHRDVKPSNVLINRNGQVKLCDFGISGYL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 153 SNPMAFACTYVGTPYYVPPEI---WENLPYNNKSDIWSLGCILYELCTLKHPFqaNSWKNL---ILKVCQGCISPLPSH- 225
Cdd:cd06617 155 VDSVAKTIDAGCKPYMAPERInpeLNQKGYDVKSDVWSLGITMIELATGRFPY--DSWKTPfqqLKQVVEEPSPQLPAEk 232
                       250       260
                ....*....|....*....|....*..
gi 23510391 226 YSYELQFLVKQMFKRNPSHRPSATTLL 252
Cdd:cd06617 233 FSPEFQDFVNKCLKKNYKERPNYPELL 259
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
2-224 8.75e-32

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: 123.57  E-value: 8.75e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSR-KEAVLLAKMKHPNIVAFKESFEAEGHLYIVME 80
Cdd:cd07848   1 NKFEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFKDSEENEEVKETTlRELKMLRTLKQENIVELKEAFRRRGKLYLVFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  81 YCDGGdlMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPM-AFA 159
Cdd:cd07848  81 YVEKN--MLELLEEMPNGVPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLSEGSnANY 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23510391 160 CTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVcQGCISPLPS 224
Cdd:cd07848 159 TEYVATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQPLFPGESEIDQLFTI-QKVLGPLPA 222
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
7-259 1.00e-31

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: 124.39  E-value: 1.00e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   7 LRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNT--QNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDG 84
Cdd:cd06635  30 LREIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEkwQDIIKEVKFLQRIKHPNSIEYKGCYLREHTAWLVMEYCLG 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  85 G--DLMQKIKQQKgklfpEDMILNWFTQMCL-GVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNpmafACT 161
Cdd:cd06635 110 SasDLLEVHKKPL-----QEIEIAAITHGALqGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIASP----ANS 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 162 YVGTPYYVPPEI---WENLPYNNKSDIWSLGCILYELCTLKHP-FQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQM 237
Cdd:cd06635 181 FVGTPYWMAPEVilaMDEGQYDGKVDVWSLGITCIELAERKPPlFNMNAMSALYHIAQNESPTLQSNEWSDYFRNFVDSC 260
                       250       260
                ....*....|....*....|..
gi 23510391 238 FKRNPSHRPSATTLLSRGIVAR 259
Cdd:cd06635 261 LQKIPQDRPTSEELLKHMFVLR 282
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
2-245 1.03e-31

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: 123.31  E-value: 1.03e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPK--SFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVM 79
Cdd:cd05612   1 DDFERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEviRLKQEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYMLM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  80 EYCDGGDLMQKIKQQKGklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFA 159
Cdd:cd05612  81 EYVPGGELFSYLRNSGR--FSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKKLRDRTWTL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 160 CtyvGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISpLPSHYSYELQFLVKQMFK 239
Cdd:cd05612 159 C---GTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGKLE-FPRHLDLYAKDLIKKLLV 234

                ....*.
gi 23510391 240 RNPSHR 245
Cdd:cd05612 235 VDRTRR 240
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
9-252 1.51e-31

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: 122.46  E-value: 1.51e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   9 MIGEGSFG---RALLVQHEssnqmFAMKEIRLP--KSFSNT-QNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYC 82
Cdd:cd14145  13 IIGIGGFGkvyRAIWIGDE-----VAVKAARHDpdEDISQTiENVRQEAKLFAMLKHPNIIALRGVCLKEPNLCLVMEFA 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  83 DGGDLMQKIkqqKGKLFPEDMILNWFTQMCLGVNHIHKKR---VLHRDIKSKNIFLTQ--------NGKVKLGDFGSARL 151
Cdd:cd14145  88 RGGPLNRVL---SGKRIPPDILVNWAVQIARGMNYLHCEAivpVIHRDLKSSNILILEkvengdlsNKILKITDFGLARE 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 152 L--SNPMAFACTYVgtpyYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCIS-PLPSHYSY 228
Cdd:cd14145 165 WhrTTKMSAAGTYA----WMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPFRGIDGLAVAYGVAMNKLSlPIPSTCPE 240
                       250       260
                ....*....|....*....|....
gi 23510391 229 ELQFLVKQMFKRNPSHRPSATTLL 252
Cdd:cd14145 241 PFARLMEDCWNPDPHSRPPFTNIL 264
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
8-252 1.54e-31

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: 122.46  E-value: 1.54e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFGRALLVQHESSNQMFAMKEIRL-PKSFSNTQNSRK---EAVLLAKMKHPNIVAFKESFE--AEGHLYIVMEY 81
Cdd:cd06652   8 KLLGQGAFGRVYLCYDADTGRELAVKQVQFdPESPETSKEVNAlecEIQLLKNLLHERIVQYYGCLRdpQERTLSIFMEY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDLMQKIKQQkGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNpMAFACT 161
Cdd:cd06652  88 MPGGSIKDQLKSY-GAL-TENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGASKRLQT-ICLSGT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 162 ----YVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISP-LPSHYSYELQFLVKQ 236
Cdd:cd06652 165 gmksVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPWAEFEAMAAIFKIATQPTNPqLPAHVSDHCRDFLKR 244
                       250
                ....*....|....*.
gi 23510391 237 MFKRnPSHRPSATTLL 252
Cdd:cd06652 245 IFVE-AKLRPSADELL 259
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
3-216 1.70e-31

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: 123.97  E-value: 1.70e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIR---LPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVM 79
Cdd:cd05602   8 DFHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQkkaILKKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQTTDKLYFVL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  80 EYCDGGDLMQKIkqQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFA 159
Cdd:cd05602  88 DYINGGELFYHL--QRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIEPNGTT 165
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23510391 160 CTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPF----QANSWKNLILKVCQ 216
Cdd:cd05602 166 STFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFysrnTAEMYDNILNKPLQ 226
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
10-251 1.72e-31

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: 123.23  E-value: 1.72e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKEIRlPKSFSNTQnsRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDLMQ 89
Cdd:cd14179  15 LGEGSFSICRKCLHKKTNQEYAVKIVS-KRMEANTQ--REIAALKLCEGHPNIVKLHEVYHDQLHTFLVMELLKGGELLE 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  90 KIKqqKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLT---QNGKVKLGDFGSARLL---SNPMAFACTyv 163
Cdd:cd14179  92 RIK--KKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTdesDNSEIKIIDFGFARLKppdNQPLKTPCF-- 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 164 gTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQAN-------SWKNLILKVCQG---CISPLPSHYSYELQFL 233
Cdd:cd14179 168 -TLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQCHdksltctSAEEIMKKIKQGdfsFEGEAWKNVSQEAKDL 246
                       250
                ....*....|....*...
gi 23510391 234 VKQMFKRNPSHRPSATTL 251
Cdd:cd14179 247 IQGLLTVDPNKRIKMSGL 264
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
10-263 1.73e-31

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: 122.64  E-value: 1.73e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKEI---RLPKSfSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGD 86
Cdd:cd05577   1 LGRGGFGEVCACQVKATGKMYACKKLdkkRIKKK-KGETMALNEKIILEKVSSPFIVSLAYAFETKDKLCLVLTLMNGGD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  87 LMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFAcTYVGTP 166
Cdd:cd05577  80 LKYHIYNVGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVEFKGGKKIK-GRVGTH 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 167 YYVPPEIWEN-LPYNNKSDIWSLGCILYELCTLKHPFQAN----SWKNLILKVCQGCISpLPSHYSYELQFLVKQMFKRN 241
Cdd:cd05577 159 GYMAPEVLQKeVAYDFSVDWFALGCMLYEMIAGRSPFRQRkekvDKEELKRRTLEMAVE-YPDSFSPEARSLCEGLLQKD 237
                       250       260
                ....*....|....*....|..
gi 23510391 242 PSHRpsattLLSRGIVARLVQK 263
Cdd:cd05577 238 PERR-----LGCRGGSADEVKE 254
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
4-247 1.88e-31

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: 121.75  E-value: 1.88e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPK-SFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYC 82
Cdd:cd14074   5 YDLEETLGRGHFAVVKLARHVFTGEKVAVKVIDKTKlDDVSKAHLFQEVRCMKLVQHPNVVRLYEVIDTQTKLYLILELG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  83 DGGDLMQKIKQQKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKN-IFLTQNGKVKLGDFGSARLLsNPMAFACT 161
Cdd:cd14074  85 DGGDMYDYIMKHENGL-NEDLARKYFRQIVSAISYCHKLHVVHRDLKPENvVFFEKQGLVKLTDFGFSNKF-QPGEKLET 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 162 YVGTPYYVPPEIWENLPYNN-KSDIWSLGCILYELCTLKHPFQ-ANSWKNLILkvCQGCISPLPSHYSYELQFLVKQMFK 239
Cdd:cd14074 163 SCGSLAYSAPEILLGDEYDApAVDIWSLGVILYMLVCGQPPFQeANDSETLTM--IMDCKYTVPAHVSPECKDLIRRMLI 240

                ....*...
gi 23510391 240 RNPSHRPS 247
Cdd:cd14074 241 RDPKKRAS 248
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
1-202 2.02e-31

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: 124.36  E-value: 2.02e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   1 MDDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRlpKSFSNTQN-----SRKEAVLLAKMKHPNIVAFKESFEAEGHL 75
Cdd:cd05617  14 LQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVK--KELVHDDEdidwvQTEKHVFEQASSNPFLVGLHSCFQTTSRL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  76 YIVMEYCDGGDLMQKIKQQKGklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNP 155
Cdd:cd05617  92 FLVIEYVNGGDLMFHMQRQRK--LPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGP 169
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 23510391 156 MAFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPF 202
Cdd:cd05617 170 GDTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPF 216
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
1-224 2.82e-31

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: 122.60  E-value: 2.82e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   1 MDDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRL---PKSFSNTqnSRKEAVLLAKMKHPNIVAFKE---------S 68
Cdd:cd07864   6 VDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLdneKEGFPIT--AIREIKILRQLNHRSVVNLKEivtdkqdalD 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  69 FEAE-GHLYIVMEYCDGgDLMqKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFG 147
Cdd:cd07864  84 FKKDkGAFYLVFEYMDH-DLM-GLLESGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADFG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 148 SARLLSNPMAFACT-YVGTPYYVPPE-IWENLPYNNKSDIWSLGCILYELCTLKHPFQAN---SWKNLILKVCQgciSPL 222
Cdd:cd07864 162 LARLYNSEESRPYTnKVITLWYRPPElLLGEERYGPAIDVWSCGCILGELFTKKPIFQANqelAQLELISRLCG---SPC 238

                ..
gi 23510391 223 PS 224
Cdd:cd07864 239 PA 240
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
1-269 3.13e-31

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: 122.40  E-value: 3.13e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   1 MDDYMvlrMIGEGSFGRALLVQHESSNQMFAMKEIRLPKsfsntQNSRK----EAVLLAKMKHPNIVAFKESFEAEGHLY 76
Cdd:cd06659  23 LENYV---KIGEGSTGVVCIAREKHSGRQVAVKMMDLRK-----QQRREllfnEVVIMRDYQHPNVVEMYKSYLVGEELW 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEYCDGGDLMQKIKQQKgklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPM 156
Cdd:cd06659  95 VLMEYLQGGALTDIVSQTR---LNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFCAQISKDV 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 157 AFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQgciSPLP-----SHYSYELQ 231
Cdd:cd06659 172 PKRKSLVGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRD---SPPPklknsHKASPVLR 248
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 23510391 232 FLVKQMFKRNPSHRPSATTLLSRGIVARL-VQKCLPPEI 269
Cdd:cd06659 249 DFLERMLVRDPQERATAQELLDHPFLLQTgLPECLVPLI 287
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
2-202 3.47e-31

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: 120.94  E-value: 3.47e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRlPKSFSNTQNS-RKEAVLLAKMKHPNIVAFKESFEAEGHLYIVME 80
Cdd:cd14083   3 DKYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCID-KKALKGKEDSlENEIAVLRKIKHPNIVQLLDIYESKSHLYLVME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  81 YCDGGDLMQKIkQQKGKLFPED---MIlnwfTQMCLGVNHIHKKRVLHRDIKSKN-IFLTQ--NGKVKLGDFGSARLL-S 153
Cdd:cd14083  82 LVTGGELFDRI-VEKGSYTEKDashLI----RQVLEAVDYLHSLGIVHRDLKPENlLYYSPdeDSKIMISDFGLSKMEdS 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 23510391 154 NPMAFACtyvGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPF 202
Cdd:cd14083 157 GVMSTAC---GTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPF 202
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
2-253 3.68e-31

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: 121.29  E-value: 3.68e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd14184   1 EKYKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKEHLIENEVSILRRVKHPNIIMLIEEMDTPAELYLVMEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDLMQKIKQQKgKLFPED---MILNwftqMCLGVNHIHKKRVLHRDIKSKNIFLTQ--NG--KVKLGDFGSARLLSN 154
Cdd:cd14184  81 VKGGDLFDAITSST-KYTERDasaMVYN----LASALKYLHGLCIVHRDIKPENLLVCEypDGtkSLKLGDFGLATVVEG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 155 PMAFACtyvGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQA--NSWKNLILKVCQGCI---SPLPSHYSYE 229
Cdd:cd14184 156 PLYTVC---GTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSenNLQEDLFDQILLGKLefpSPYWDNITDS 232
                       250       260
                ....*....|....*....|....
gi 23510391 230 LQFLVKQMFKRNPSHRPSATTLLS 253
Cdd:cd14184 233 AKELISHMLQVNVEARYTAEQILS 256
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
1-245 4.85e-31

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: 123.22  E-value: 4.85e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   1 MDDYMVLRMIGEGSFGRALLVQHESSNQMFAMK----EIRLPKSfsNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLY 76
Cdd:cd05594  24 MNDFEYLKLLGKGTFGKVILVKEKATGRYYAMKilkkEVIVAKD--EVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLC 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEYCDGGDLMQKIKQQKgkLFPEDMILNWFTQMCLGVNHIHKKR-VLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNP 155
Cdd:cd05594 102 FVMEYANGGELFFHLSRER--VFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKD 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 156 MAFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISpLPSHYSYELQFLVK 235
Cdd:cd05594 180 GATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIR-FPRTLSPEAKSLLS 258
                       250
                ....*....|
gi 23510391 236 QMFKRNPSHR 245
Cdd:cd05594 259 GLLKKDPKQR 268
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
8-245 5.13e-31

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: 122.36  E-value: 5.13e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFGRALLVQHESSNQMFAMKEIR-----LPKSFSNTQNSRKeaVLLAKMKHPNIVAFKESFEAEGHLYIVMEYC 82
Cdd:cd05620   1 KVLGKGSFGKVLLAELKGKGEYFAVKALKkdvvlIDDDVECTMVEKR--VLALAWENPFLTHLYCTFQTKEHLFFVMEFL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  83 DGGDLMQKIkQQKGKLfpeDMILNWF--TQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFAC 160
Cdd:cd05620  79 NGGDLMFHI-QDKGRF---DLYRATFyaAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKENVFGDNRAS 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 161 TYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGciSP-LPSHYSYELQFLVKQMFK 239
Cdd:cd05620 155 TFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVD--TPhYPRWITKESKDILEKLFE 232

                ....*.
gi 23510391 240 RNPSHR 245
Cdd:cd05620 233 RDPTRR 238
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
8-253 5.78e-31

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: 120.96  E-value: 5.78e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFGRALLVQHESSNQMFAMKEIRL----PKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFE--AEGHLYIVMEY 81
Cdd:cd06651  13 KLLGQGAFGRVYLCYDVDTGRELAAKQVQFdpesPETSKEVSALECEIQLLKNLQHERIVQYYGCLRdrAEKTLTIFMEY 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDLMQKIKQQKGklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFAC- 160
Cdd:cd06651  93 MPGGSVKDQLKAYGA--LTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICMSGTg 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 161 --TYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVC-QGCISPLPSHYSYELQFLVKQM 237
Cdd:cd06651 171 irSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIAtQPTNPQLPSHISEHARDFLGCI 250
                       250
                ....*....|....*.
gi 23510391 238 FKRnPSHRPSATTLLS 253
Cdd:cd06651 251 FVE-ARHRPSAEELLR 265
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
4-257 5.78e-31

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: 121.27  E-value: 5.78e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSfsNTQNSRKEAVLLAKMKH-PNIVAFKESF---EAEGH---LY 76
Cdd:cd06636  18 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTED--EEEEIKLEINMLKKYSHhRNIATYYGAFikkSPPGHddqLW 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEYCDGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPM 156
Cdd:cd06636  96 LVMEFCGAGSVTDLVKNTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTV 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 157 AFACTYVGTPYYVPPEIW---EN--LPYNNKSDIWSLGCILYE-------LCTLkHPFQA--------------NSWKNL 210
Cdd:cd06636 176 GRRNTFIGTPYWMAPEVIacdENpdATYDYRSDIWSLGITAIEmaegappLCDM-HPMRAlfliprnpppklksKKWSKK 254
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 23510391 211 ILKVCQGCisplpshysyelqfLVKqmfkrNPSHRPSATTLLSRGIV 257
Cdd:cd06636 255 FIDFIEGC--------------LVK-----NYLSRPSTEQLLKHPFI 282
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
4-252 6.60e-31

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: 120.73  E-value: 6.60e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSN-TQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYC 82
Cdd:cd14097   3 YTFGRKLGQGSFGVVIEATHKETQTKWAIKKINREKAGSSaVKLLEREVDILKHVNHAHIIHLEEVFETPKRMYLVMELC 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  83 DGGDLmQKIKQQKGkLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNG-------KVKLGDFG-SARLLSN 154
Cdd:cd14097  83 EDGEL-KELLLRKG-FFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSIidnndklNIKVTDFGlSVQKYGL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 155 PMAFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLPSHY---SYELQ 231
Cdd:cd14097 161 GEDMLQETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDLTFTQSVWqsvSDAAK 240
                       250       260
                ....*....|....*....|.
gi 23510391 232 FLVKQMFKRNPSHRPSATTLL 252
Cdd:cd14097 241 NVLQQLLKVDPAHRMTASELL 261
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
1-245 8.75e-31

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 121.85  E-value: 8.75e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391    1 MDDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPK--SFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIV 78
Cdd:PTZ00263  17 LSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREilKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   79 MEYCDGGDLMQKIKQqKGKlFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAF 158
Cdd:PTZ00263  97 LEFVVGGELFTHLRK-AGR-FPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVPDRTFT 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  159 ACtyvGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISpLPSHYSYELQFLVKQMF 238
Cdd:PTZ00263 175 LC---GTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLK-FPNWFDGRARDLVKGLL 250

                 ....*..
gi 23510391  239 KRNPSHR 245
Cdd:PTZ00263 251 QTDHTKR 257
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
3-245 9.81e-31

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: 120.59  E-value: 9.81e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRlpKSFSNTQNSRKEAV----LLAKMKHPNIVAFKESFEAEGHLYIV 78
Cdd:cd05609   1 DFETIKLISNGAYGAVYLVRHRETRQRFAMKKIN--KQNLILRNQIQQVFverdILTFAENPFVVSMYCSFETKRHLCMV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  79 MEYCDGGDLMQKIKQQkGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSAR--LLS--- 153
Cdd:cd05609  79 MEYVEGGDCATLLKNI-GPL-PVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSKigLMSltt 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 154 ---------NPMAFACTYV-GTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCI---- 219
Cdd:cd05609 157 nlyeghiekDTREFLDKQVcGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIewpe 236
                       250       260
                ....*....|....*....|....*...
gi 23510391 220 --SPLPShysyELQFLVKQMFKRNPSHR 245
Cdd:cd05609 237 gdDALPD----DAQDLITRLLQQNPLER 260
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
10-219 1.06e-30

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: 120.79  E-value: 1.06e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHL-----YIVMEYCDG 84
Cdd:cd14039   1 LGTGGFGNVCLYQNQETGEKIAIKSCRLELSVKNKDRWCHEIQIMKKLNHPNVVKACDVPEEMNFLvndvpLLAMEYCSG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  85 GDLMQKI-KQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQ-NGKV--KLGDFGSARLLSNPmAFAC 160
Cdd:cd14039  81 GDLRKLLnKPENCCGLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEiNGKIvhKIIDLGYAKDLDQG-SLCT 159
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23510391 161 TYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPF----QANSWKNLILKVCQGCI 219
Cdd:cd14039 160 SFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPFlhnlQPFTWHEKIKKKDPKHI 222
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
7-202 1.12e-30

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: 121.61  E-value: 1.12e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   7 LRMIGEGSFGRALLVQHESSNQMFAMKEIRlPKSFSNTQNSR----KEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYC 82
Cdd:cd05604   1 LKVIGKGSFGKVLLAKRKRDGKYYAVKVLQ-KKVILNRKEQKhimaERNVLLKNVKHPFLVGLHYSFQTTDKLYFVLDFV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  83 DGGDLMQKIkqQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTY 162
Cdd:cd05604  80 NGGELFFHL--QRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKEGISNSDTTTTF 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 23510391 163 VGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPF 202
Cdd:cd05604 158 CGTPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPF 197
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
4-245 1.36e-30

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: 120.00  E-value: 1.36e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCD 83
Cdd:cd14169   5 YELKEKLGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKEAMVENEIAVLRRINHENIVSLEDIYESPTHLYLAMELVT 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  84 GGDLMQKIKQQKGklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKN-IFLT--QNGKVKLGDFGSARL-LSNPMAFA 159
Cdd:cd14169  85 GGELFDRIIERGS--YTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENlLYATpfEDSKIMISDFGLSKIeAQGMLSTA 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 160 CtyvGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANS---WKNLILKVCQGCISPLPSHYSYELQFLVKQ 236
Cdd:cd14169 163 C---GTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENdseLFNQILKAEYEFDSPYWDDISESAKDFIRH 239

                ....*....
gi 23510391 237 MFKRNPSHR 245
Cdd:cd14169 240 LLERDPEKR 248
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
8-263 1.43e-30

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: 121.23  E-value: 1.43e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSR---KEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDG 84
Cdd:cd05603   1 KVIGKGSFGKVLLAKRKCDGKFYAVKVLQKKTILKKKEQNHimaERNVLLKNLKHPFLVGLHYSFQTSEKLYFVLDYVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  85 GDLMQKIkqQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTYVG 164
Cdd:cd05603  81 GELFFHL--QRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEGMEPEETTSTFCG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 165 TPYYVPPEIWENLPYNNKSDIWSLGCILYELctlkhpfqanswknlilkvcqgcISPLPSHYSYElqflVKQMFK---RN 241
Cdd:cd05603 159 TPEYLAPEVLRKEPYDRTVDWWCLGAVLYEM-----------------------LYGLPPFYSRD----VSQMYDnilHK 211
                       250       260
                ....*....|....*....|..
gi 23510391 242 PSHRPSATTLLSRGIVARLVQK 263
Cdd:cd05603 212 PLHLPGGKTVAACDLLQGLLHK 233
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
10-206 1.49e-30

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: 119.92  E-value: 1.49e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSR-KEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGgDLM 88
Cdd:cd07860   8 IGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAiREISLLKELNHPNIVKLLDVIHTENKLYLVFEFLHQ-DLK 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  89 QKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTYVGTPYY 168
Cdd:cd07860  87 KFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEVVTLWY 166
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 23510391 169 VPPEIWENLP-YNNKSDIWSLGCILYELCTLKHPFQANS 206
Cdd:cd07860 167 RAPEILLGCKyYSTAVDIWSLGCIFAEMVTRRALFPGDS 205
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
2-283 1.63e-30

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: 121.32  E-value: 1.63e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIrlPKSFSNTQNSRK---EAVLLAKMKHPNIVAFKESFEAEG----- 73
Cdd:cd07855   5 DRYEPIETIGSGAYGVVCSAIDTKSGQKVAIKKI--PNAFDVVTTAKRtlrELKILRHFKHDNIIAIRDILRPKVpyadf 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  74 -HLYIVMEYCDGgDLMQKIKQQKGklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLL 152
Cdd:cd07855  83 kDVYVVLDLMES-DLHHIIHSDQP--LTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMARGL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 153 SNPMA----FACTYVGTPYYVPPEIWENLP-YNNKSDIWSLGCILYELCTLKHPFQANSWKN---LILKV----CQG--- 217
Cdd:cd07855 160 CTSPEehkyFMTEYVATRWYRAPELMLSLPeYTQAIDMWSVGCIFAEMLGRRQLFPGKNYVHqlqLILTVlgtpSQAvin 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 218 ---------CISPLPSHYSYELQF-----------LVKQMFKRNPSHRPSATTLLSRGIVARLV-----QKCLPP----- 267
Cdd:cd07855 240 aigadrvrrYIQNLPNKQPVPWETlypkadqqaldLLSQMLRFDPSERITVAEALQHPFLAKYHdpddePDCAPPfdfdf 319
                       330
                ....*....|....*.
gi 23510391 268 EIIMEYGEEVLEEIKN 283
Cdd:cd07855 320 DAEALTREALKEAIVN 335
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
2-206 2.48e-30

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: 121.64  E-value: 2.48e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKeirLPKSFSNTQNSR-----KEAVLLAKMKHPNIVAFKESFEAEGHLY 76
Cdd:cd05621  52 EDYDVVKVIGRGAFGEVQLVRHKASQKVYAMK---LLSKFEMIKRSDsaffwEERDIMAFANSPWVVQLFCAFQDDKYLY 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEYCDGGDLMQKIKQQKgklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPM 156
Cdd:cd05621 129 MVMEYMPGGDLVNLMSNYD---VPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGTCMKMDETG 205
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 23510391 157 AFAC-TYVGTPYYVPPEIWENLP----YNNKSDIWSLGCILYELCTLKHPFQANS 206
Cdd:cd05621 206 MVHCdTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLFEMLVGDTPFYADS 260
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
4-221 3.13e-30

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: 119.78  E-value: 3.13e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRL---PKSFSNTqnSRKEAVLLAKMKHPNIVAFKESFEAE-------- 72
Cdd:cd07865  14 YEKLAKIGQGTFGEVFKARHRKTGQIVALKKVLMeneKEGFPIT--ALREIKILQLLKHENVVNLIEICRTKatpynryk 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  73 GHLYIVMEYCDGgDLMQKIKQQKGKlFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLL 152
Cdd:cd07865  92 GSIYLVFEFCEH-DLAGLLSNKNVK-FTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVLKLADFGLARAF 169
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23510391 153 SNPMAFA----CTYVGTPYYVPPEIWEN-LPYNNKSDIWSLGCILYELCTlKHP-FQANSWK---NLILKVCqGCISP 221
Cdd:cd07865 170 SLAKNSQpnryTNRVVTLWYRPPELLLGeRDYGPPIDMWGAGCIMAEMWT-RSPiMQGNTEQhqlTLISQLC-GSITP 245
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
8-195 3.16e-30

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: 120.11  E-value: 3.16e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFGRALLVQHESSNQMFAMKEirLPKSFSNTQNSRKE-----AVLLAKMKHPNIVAFKESFEAEGHLYIVMEYC 82
Cdd:cd05575   1 KVIGKGSFGKVLLARHKAEGKLYAVKV--LQKKAILKRNEVKHimaerNVLLKNVKHPFLVGLHYSFQTKDKLYFVLDYV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  83 DGGDLMQKIkqQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTY 162
Cdd:cd05575  79 NGGELFFHL--QRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKEGIEPSDTTSTF 156
                       170       180       190
                ....*....|....*....|....*....|...
gi 23510391 163 VGTPYYVPPEIWENLPYNNKSDIWSLGCILYEL 195
Cdd:cd05575 157 CGTPEYLAPEVLRKQPYDRTVDWWCLGAVLYEM 189
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
4-253 3.35e-30

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: 118.25  E-value: 3.35e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCD 83
Cdd:cd14078   5 YELHETIGSGGFAKVKLATHILTGEKVAIKIMDKKALGDDLPRVKTEIEALKNLSHQHICRLYHVIETDNKIFMVLEYCP 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  84 GGDLMQKIkQQKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGsarLLSNP---MAFAC 160
Cdd:cd14078  85 GGELFDYI-VAKDRL-SEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFG---LCAKPkggMDHHL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 161 -TYVGTPYYVPPEIWENLPY-NNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISpLPSHYSYELQFLVKQMF 238
Cdd:cd14078 160 eTCCGSPAYAAPELIQGKPYiGSEADVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSGKYE-EPEWLSPSSKLLLDQML 238
                       250
                ....*....|....*
gi 23510391 239 KRNPSHRPSATTLLS 253
Cdd:cd14078 239 QVDPKKRITVKELLN 253
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
8-202 3.72e-30

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: 120.22  E-value: 3.72e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFGRALLVQHESSNQMFAMKEIRlpKSFSNTQN-----SRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYC 82
Cdd:cd05588   1 RVIGRGSYAKVLMVELKKTKRIYAMKVIK--KELVNDDEdidwvQTEKHVFETASNHPFLVGLHSCFQTESRLFFVIEFV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  83 DGGDLMQKIKQQKgKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTY 162
Cdd:cd05588  79 NGGDLMFHMQRQR-RL-PEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTF 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 23510391 163 VGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPF 202
Cdd:cd05588 157 CGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPF 196
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
1-208 4.36e-30

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: 118.96  E-value: 4.36e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   1 MDDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVME 80
Cdd:cd07871   4 LETYVKLDKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTAIREVSLLKNLKHANIVTLHDIIHTERCLTLVFE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  81 YCDGgDLMQKIkQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFAC 160
Cdd:cd07871  84 YLDS-DLKQYL-DNCGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLARAKSVPTKTYS 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 23510391 161 TYVGTPYYVPPEI-WENLPYNNKSDIWSLGCILYELCTLKHPFQANSWK 208
Cdd:cd07871 162 NEVVTLWYRPPDVlLGSTEYSTPIDMWGVGCILYEMATGRPMFPGSTVK 210
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
9-245 5.14e-30

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: 119.21  E-value: 5.14e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   9 MIGEGSFGRALLVQHESSNQMFAMKEIRLPK--SFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGD 86
Cdd:cd05585   1 VIGKGSFGKVMQVRKKDTSRIYALKTIRKAHivSRSEVTHTLAERTVLAQVDCPFIVPLKFSFQSPEKLYLVLAFINGGE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  87 LMQKIkQQKGKlFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTYVGTP 166
Cdd:cd05585  81 LFHHL-QREGR-FDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKLNMKDDDKTNTFCGTP 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 167 YYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQgciSPL--PSHYSYELQFLVKQMFKRNPSH 244
Cdd:cd05585 159 EYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQ---EPLrfPDGFDRDAKDLLIGLLNRDPTK 235

                .
gi 23510391 245 R 245
Cdd:cd05585 236 R 236
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
1-202 5.50e-30

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: 120.52  E-value: 5.50e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   1 MDDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRlpKSFSNTQN-----SRKEAVLLAKMKHPNIVAFKESFEAEGHL 75
Cdd:cd05618  19 LQDFDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVK--KELVNDDEdidwvQTEKHVFEQASNHPFLVGLHSCFQTESRL 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  76 YIVMEYCDGGDLMQKIKQQKGklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNP 155
Cdd:cd05618  97 FFVIEYVNGGDLMFHMQRQRK--LPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRP 174
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 23510391 156 MAFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPF 202
Cdd:cd05618 175 GDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPF 221
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
10-245 6.19e-30

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: 117.88  E-value: 6.19e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHES---SNQMFAMKE------IRLPKSFSNTQNSRKeaVLLAKMKHPNIVAFKESFEAEGHLYIVME 80
Cdd:cd05583   2 LGTGAYGKVFLVRKVGghdAGKLYAMKVlkkatiVQKAKTAEHTMTERQ--VLEAVRQSPFLVTLHYAFQTDAKLHLILD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  81 YCDGGDLMQKIKQQKGklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFG-SARLLSNPMAFA 159
Cdd:cd05583  80 YVNGGELFTHLYQREH--FTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGlSKEFLPGENDRA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 160 CTYVGTPYYVPPEIWENLP--YNNKSDIWSLGCILYELCTLKHPFQANSWKNL---ILKVCQGCISPLPSHYSYELQFLV 234
Cdd:cd05583 158 YSFCGTIEYMAPEVVRGGSdgHDKAVDWWSLGVLTYELLTGASPFTVDGERNSqseISKRILKSHPPIPKTFSAEAKDFI 237
                       250
                ....*....|.
gi 23510391 235 KQMFKRNPSHR 245
Cdd:cd05583 238 LKLLEKDPKKR 248
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
1-197 6.22e-30

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: 118.57  E-value: 6.22e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   1 MDDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVME 80
Cdd:cd07873   1 LETYIKLDKLGEGTYATVYKGRSKLTDNLVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIIHTEKSLTLVFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  81 YCDGgDLMQKIKQQKGKLFPEDMILNWFtQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFAC 160
Cdd:cd07873  81 YLDK-DLKQYLDDCGNSINMHNVKLFLF-QLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSIPTKTYS 158
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 23510391 161 TYVGTPYYVPPEI-WENLPYNNKSDIWSLGCILYELCT 197
Cdd:cd07873 159 NEVVTLWYRPPDIlLGSTDYSTQIDMWGVGCIFYEMST 196
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
3-253 6.25e-30

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: 117.77  E-value: 6.25e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLR-MIGEGSFGRALLVQHESSNQMFAMKEIRlpksfsNTQNSRKEAVLLAKM-KHPNIVAFKESFEAEGH----LY 76
Cdd:cd14089   1 DYTISKqVLGLGINGKVLECFHKKTGEKFALKVLR------DNPKARREVELHWRAsGCPHIVRIIDVYENTYQgrkcLL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEYCDGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQ---NGKVKLGDFGSARLL- 152
Cdd:cd14089  75 VVMECMEGGELFSRIQERADSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSkgpNAILKLTDFGFAKETt 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 153 -SNPMAFACtYvgTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQAN-------SWKNLILKVCQGCISPLPS 224
Cdd:cd14089 155 tKKSLQTPC-Y--TPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNhglaispGMKKRIRNGQYEFPNPEWS 231
                       250       260
                ....*....|....*....|....*....
gi 23510391 225 HYSYELQFLVKQMFKRNPSHRPSATTLLS 253
Cdd:cd14089 232 NVSEEAKDLIRGLLKTDPSERLTIEEVMN 260
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
2-206 6.32e-30

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: 120.88  E-value: 6.32e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKeirLPKSFSNTQNSR-----KEAVLLAKMKHPNIVAFKESFEAEGHLY 76
Cdd:cd05622  73 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMK---LLSKFEMIKRSDsaffwEERDIMAFANSPWVVQLFYAFQDDRYLY 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEYCDGGDLMQKIKQQKgklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPM 156
Cdd:cd05622 150 MVMEYMPGGDLVNLMSNYD---VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEG 226
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 23510391 157 AFAC-TYVGTPYYVPPEIWENLP----YNNKSDIWSLGCILYELCTLKHPFQANS 206
Cdd:cd05622 227 MVRCdTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADS 281
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
2-201 6.82e-30

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: 120.34  E-value: 6.82e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQ--NSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVM 79
Cdd:cd05629   1 EDFHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMFKKDQlaHVKAERDVLAESDSPWVVSLYYSFQDAQYLYLIM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  80 EYCDGGDLMQK-IKQQkgkLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSA--------- 149
Cdd:cd05629  81 EFLPGGDLMTMlIKYD---TFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGLStgfhkqhds 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 150 ----RLLS-----------NPMA-----------------------FACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCI 191
Cdd:cd05629 158 ayyqKLLQgksnknridnrNSVAvdsinltmsskdqiatwkknrrlMAYSTVGTPDYIAPEIFLQQGYGQECDWWSLGAI 237
                       250
                ....*....|
gi 23510391 192 LYElCTLKHP 201
Cdd:cd05629 238 MFE-CLIGWP 246
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
3-245 7.38e-30

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


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 118.18  E-value: 7.38e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHES---SNQMFAMKEIR---LPKSFSNTQNSRKEAVLLAKMKH-PNIVAFKESFEAEGHL 75
Cdd:cd05613   1 NFELLKVLGTGAYGKVFLVRKVSghdAGKLYAMKVLKkatIVQKAKTAEHTRTERQVLEHIRQsPFLVTLHYAFQTDTKL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  76 YIVMEYCDGGDLMQKIKQQKGklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFG-SARLLSN 154
Cdd:cd05613  81 HLILDYINGGELFTHLSQRER--FTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGlSKEFLLD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 155 PMAFACTYVGTPYYVPPEIWE--NLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCIS---PLPSHYSYE 229
Cdd:cd05613 159 ENERAYSFCGTIEYMAPEIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKsepPYPQEMSAL 238
                       250
                ....*....|....*.
gi 23510391 230 LQFLVKQMFKRNPSHR 245
Cdd:cd05613 239 AKDIIQRLLMKDPKKR 254
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
2-245 7.44e-30

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


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 118.88  E-value: 7.44e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEirLPKSFSNTQNSRK----EAVLLAKMKHPNIVAFKESFEAEGHLYI 77
Cdd:cd05574   1 DHFKKIKLLGKGDVGRVYLVRLKGTGKLFAMKV--LDKEEMIKRNKVKrvltEREILATLDHPFLPTLYASFQTSTHLCF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  78 VMEYCDGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDF----------- 146
Cdd:cd05574  79 VMDYCPGGELFRLLQKQPGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFdlskqssvtpp 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 147 --------GSARLLSN----------PMAFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWK 208
Cdd:cd05574 159 pvrkslrkGSRRSSVKsieketfvaePSARSNSFVGTEEYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTTPFKGSNRD 238
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 23510391 209 NLILKVCQGCISpLPSHY--SYELQFLVKQMFKRNPSHR 245
Cdd:cd05574 239 ETFSNILKKELT-FPESPpvSSEAKDLIRKLLVKDPSKR 276
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
3-195 8.91e-30

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: 117.82  E-value: 8.91e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNS--RKEAVLLAKMKHPNIVAFKESFEAEGHLYIVME 80
Cdd:cd07832   1 RYKILGRIGEGAHGIVFKAKDRETGETVALKKVALRKLEGGIPNQalREIKALQACQGHPYVVKLRDVFPHGTGFVLVFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  81 YCDGgDLMQKIKQQKgKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFAC 160
Cdd:cd07832  81 YMLS-SLSEVLRDEE-RPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLARLFSEEDPRLY 158
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 23510391 161 TY-VGTPYYVPPEI-WENLPYNNKSDIWSLGCILYEL 195
Cdd:cd07832 159 SHqVATRWYRAPELlYGSRKYDEGVDLWAVGCIFAEL 195
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
2-252 1.05e-29

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: 117.79  E-value: 1.05e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKeIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAE-----GHLY 76
Cdd:cd06639  22 DTWDIIETIGKGTYGKVYKVTNKKDGSLAAVK-ILDPISDVDEEIEAEYNILRSLPNHPNVVKFYGMFYKAdqyvgGQLW 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEYCDGGDLMQKIKQ--QKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFG------S 148
Cdd:cd06639 101 LVLELCNGGSVTELVKGllKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGvsaqltS 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 149 ARLLSNpmafacTYVGTPYYVPPEIWE-----NLPYNNKSDIWSLGCILYELCTLKHP-FQANSWKNLiLKVCQGCISPL 222
Cdd:cd06639 181 ARLRRN------TSVGTPFWMAPEVIAceqqyDYSYDARCDVWSLGITAIELADGDPPlFDMHPVKAL-FKIPRNPPPTL 253
                       250       260       270
                ....*....|....*....|....*....|..
gi 23510391 223 --PSHYSYELQFLVKQMFKRNPSHRPSATTLL 252
Cdd:cd06639 254 lnPEKWCRGFSHFISQCLIKDFEKRPSVTHLL 285
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
10-253 1.66e-29

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: 116.27  E-value: 1.66e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKEirLPKSFSNTQNSRKEAVL-LAKMKHPNIV-AFKESFEAEGHLYIVMEYCDGGDL 87
Cdd:cd13987   1 LGEGTYGKVLLAVHKGSGTKMALKF--VPKPSTKLKDFLREYNIsLELSVHPHIIkTYDVAFETEDYYVFAQEYAPYGDL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  88 MQKIKQQKGklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNG--KVKLGDFGSARLLSNPMAFACtyvGT 165
Cdd:cd13987  79 FSIIPPQVG--LPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDcrRVKLCDFGLTRRVGSTVKRVS---GT 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 166 PYYVPPEIWENLPY-----NNKSDIWSLGCILYELCTLKHPFQANSWKN----LILKVCQGCISPLPSHY---SYELQFL 233
Cdd:cd13987 154 IPYTAPEVCEAKKNegfvvDPSIDVWAFGVLLFCCLTGNFPWEKADSDDqfyeEFVRWQKRKNTAVPSQWrrfTPKALRM 233
                       250       260
                ....*....|....*....|
gi 23510391 234 VKQMFKRNPSHRPSATTLLS 253
Cdd:cd13987 234 FKKLLAPEPERRCSIKEVFK 253
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
8-245 2.07e-29

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: 117.84  E-value: 2.07e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFGRALLVQHESSNQMFAMK----EIRLPK---SFSNTQNSrkeavLLAKMKHPNIVAFKESFEAEGHLYIVME 80
Cdd:cd05571   1 KVLGKGTFGKVILCREKATGELYAIKilkkEVIIAKdevAHTLTENR-----VLQNTRHPFLTSLKYSFQTNDRLCFVME 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  81 YCDGGDLMQKIKqqKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGsarLLSNPMAFAC 160
Cdd:cd05571  76 YVNGGELFFHLS--RERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFG---LCKEEISYGA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 161 ---TYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISpLPSHYSYELQFLVKQM 237
Cdd:cd05571 151 ttkTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEVR-FPSTLSPEAKSLLAGL 229

                ....*...
gi 23510391 238 FKRNPSHR 245
Cdd:cd05571 230 LKKDPKKR 237
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
10-251 2.23e-29

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: 117.28  E-value: 2.23e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKEI--RLPksfSNTQnsRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDL 87
Cdd:cd14180  14 LGEGSFSVCRKCRHRQSGQEYAVKIIsrRME---ANTQ--REVAALRLCQSHPNIVALHEVLHDQYHTYLVMELLRGGEL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  88 MQKIKQQKgkLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFL---TQNGKVKLGDFGSARLL---SNPMAFACT 161
Cdd:cd14180  89 LDRIKKKA--RFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYadeSDGAVLKVIDFGFARLRpqgSRPLQTPCF 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 162 yvgTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQ-------ANSWKNLILKVCQGCIS---PLPSHYSYELQ 231
Cdd:cd14180 167 ---TLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQskrgkmfHNHAADIMHKIKEGDFSlegEAWKGVSEEAK 243
                       250       260
                ....*....|....*....|
gi 23510391 232 FLVKQMFKRNPSHRPSATTL 251
Cdd:cd14180 244 DLVRGLLTVDPAKRLKLSEL 263
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
6-253 2.37e-29

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: 116.29  E-value: 2.37e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   6 VLRMIGEGSFGRallVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVL-LAKMKHPNIVAFKESFEAEGHLYIVMEYCDG 84
Cdd:cd14063   4 IKEVIGKGRFGR---VHRGRWHGDVAIKLLNIDYLNEEQLEAFKEEVAaYKNTRHDNLVLFMGACMDPPHLAIVTSLCKG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  85 GDLMQKIKQQKGKlFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLtQNGKVKLGDFG--SARLLSNPMAFACTY 162
Cdd:cd14063  81 RTLYSLIHERKEK-FDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFL-ENGRVVITDFGlfSLSGLLQPGRREDTL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 163 V---GTPYYVPPEI----------WENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLPSH-YSY 228
Cdd:cd14063 159 VipnGWLCYLAPEIiralspdldfEESLPFTKASDVYAFGTVWYELLAGRWPFKEQPAESIIWQVGCGKKQSLSQLdIGR 238
                       250       260
                ....*....|....*....|....*
gi 23510391 229 ELQFLVKQMFKRNPSHRPSATTLLS 253
Cdd:cd14063 239 EVKDILMQCWAYDPEKRPTFSDLLR 263
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
10-254 3.27e-29

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: 115.57  E-value: 3.27e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRallVQHES-SNQMFAMKEIRLP--KSFSNT-QNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGG 85
Cdd:cd14061   2 IGVGGFGK---VYRGIwRGEEVAVKAARQDpdEDISVTlENVRQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEYARGG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  86 DLMQKIkqqKGKLFPEDMILNWFTQMCLGVNHIHKKR---VLHRDIKSKNIFL--------TQNGKVKLGDFGSARLLSN 154
Cdd:cd14061  79 ALNRVL---AGRKIPPHVLVDWAIQIARGMNYLHNEApvpIIHRDLKSSNILIleaienedLENKTLKITDFGLAREWHK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 155 P--MAFACTYVgtpyYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFqanswKNL-ILKVCQGCIS-----PLPSHY 226
Cdd:cd14061 156 TtrMSAAGTYA----WMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPY-----KGIdGLAVAYGVAVnkltlPIPSTC 226
                       250       260
                ....*....|....*....|....*...
gi 23510391 227 SYELQFLVKQMFKRNPSHRPSATTLLSR 254
Cdd:cd14061 227 PEPFAQLMKDCWQPDPHDRPSFADILKQ 254
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
4-252 3.47e-29

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: 116.74  E-value: 3.47e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLpkSFSNTQNSRKEAVLLAKMKH-PNIVAFKESF------EAEGHLY 76
Cdd:cd06637   8 FELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDV--TGDEEEEIKQEINMLKKYSHhRNIATYYGAFikknppGMDDQLW 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEYCDGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPM 156
Cdd:cd06637  86 LVMEFCGAGSVTDLIKNTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTV 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 157 AFACTYVGTPYYVPPEIWE-----NLPYNNKSDIWSLGCILYE-------LCTLkHPFQAnswknlILKVCQGCISPLPS 224
Cdd:cd06637 166 GRRNTFIGTPYWMAPEVIAcdenpDATYDFKSDLWSLGITAIEmaegappLCDM-HPMRA------LFLIPRNPAPRLKS 238
                       250       260
                ....*....|....*....|....*....
gi 23510391 225 -HYSYELQFLVKQMFKRNPSHRPSATTLL 252
Cdd:cd06637 239 kKWSKKFQSFIESCLVKNHSQRPSTEQLM 267
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
2-252 7.76e-29

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: 114.71  E-value: 7.76e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd14183   6 ERYKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKCRGKEHMIQNEVSILRRVKHPNIVLLIEEMDMPTELYLVMEL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDLMQKIKQQKGklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLT--QNG--KVKLGDFGSARLLSNPMA 157
Cdd:cd14183  86 VKGGDLFDAITSTNK--YTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYehQDGskSLKLGDFGLATVVDGPLY 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 158 FACtyvGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLIL--KVCQGCIS-PLP--SHYSYELQF 232
Cdd:cd14183 164 TVC---GTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGSGDDQEVLfdQILMGQVDfPSPywDNVSDSAKE 240
                       250       260
                ....*....|....*....|
gi 23510391 233 LVKQMFKRNPSHRPSATTLL 252
Cdd:cd14183 241 LITMMLQVDVDQRYSALQVL 260
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
7-259 1.08e-28

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 116.46  E-value: 1.08e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391    7 LRMIGEGSFGRALLVQHESSNQMFAMKEIrlpksFSNTQNS-----RKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:PLN00034  79 VNRIGSGAGGTVYKVIHRPTGRLYALKVI-----YGNHEDTvrrqiCREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEF 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   82 CDGGDLmqkikqQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACT 161
Cdd:PLN00034 154 MDGGSL------EGTHIADEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRILAQTMDPCNS 227
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  162 YVGTPYYVPPE-IWENL---PYNNKS-DIWSLGCILYELCTLKHPF---QANSWKNLILKVCQGCISPLPSHYSYELQFL 233
Cdd:PLN00034 228 SVGTIAYMSPErINTDLnhgAYDGYAgDIWSLGVSILEFYLGRFPFgvgRQGDWASLMCAICMSQPPEAPATASREFRHF 307
                        250       260
                 ....*....|....*....|....*.
gi 23510391  234 VKQMFKRNPSHRPSATTLLSRGIVAR 259
Cdd:PLN00034 308 ISCCLQREPAKRWSAMQLLQHPFILR 333
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
10-247 1.25e-28

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: 114.09  E-value: 1.25e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKEIR-LPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDLM 88
Cdd:cd13978   1 LGSGGFGTVSKARHVSWFGMVAIKCLHsSPNCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSLK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  89 QKIKQQKGKLfPEDMILNWFTQMCLGVNHIH--KKRVLHRDIKSKNIFLTQNGKVKLGDFGSARL-----LSNPMAFACT 161
Cdd:cd13978  81 SLLEREIQDV-PWSLRFRIIHEIALGMNFLHnmDPPLLHHDLKPENILLDNHFHVKISDFGLSKLgmksiSANRRRGTEN 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 162 YVGTPYYVPPEIWENLPY--NNKSDIWSLGCILYELCTLKHPFQANSWKNLIL-KVCQG-----------CISPLPShys 227
Cdd:cd13978 160 LGGTPIYMAPEAFDDFNKkpTSKSDVYSFAIVIWAVLTRKEPFENAINPLLIMqIVSKGdrpslddigrlKQIENVQ--- 236
                       250       260
                ....*....|....*....|
gi 23510391 228 yELQFLVKQMFKRNPSHRPS 247
Cdd:cd13978 237 -ELISLMIRCWDGNPDARPT 255
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
8-245 1.42e-28

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: 114.74  E-value: 1.42e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFGRALLVQHESSNQMFAMKEI---RLPKSFSNTQnSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDG 84
Cdd:cd05630   6 RVLGKGGFGEVCACQVRATGKMYACKKLekkRIKKRKGEAM-ALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTLMNG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  85 GDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFAcTYVG 164
Cdd:cd05630  85 GDLKFHIYHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPEGQTIK-GRVG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 165 TPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSwKNLILKVCQGCISPLPSHYSYEL----QFLVKQMFKR 240
Cdd:cd05630 164 TVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRK-KKIKREEVERLVKEVPEEYSEKFspqaRSLCSMLLCK 242

                ....*
gi 23510391 241 NPSHR 245
Cdd:cd05630 243 DPAER 247
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
4-197 1.59e-28

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: 114.40  E-value: 1.59e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCD 83
Cdd:cd07844   2 YKKLDKLGEGSYATVYKGRSKLTGQLVALKEIRLEHEEGAPFTAIREASLLKDLKHANIVTLHDIIHTKKTLTLVFEYLD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  84 GgDLMQKIKQQKGKLFPEDMILNWFtQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAfacTY- 162
Cdd:cd07844  82 T-DLKQYMDDCGGGLSMHNVRLFLF-QLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLARAKSVPSK---TYs 156
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 23510391 163 --VGTPYYVPPEI-WENLPYNNKSDIWSLGCILYELCT 197
Cdd:cd07844 157 neVVTLWYRPPDVlLGSTEYSTSLDMWGVGCIFYEMAT 194
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
2-215 1.84e-28

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: 115.47  E-value: 1.84e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPksFSNTQNSR---KEAVLLAKMKHPNIVAFKESFEAEGHL--- 75
Cdd:cd07851  15 DRYQNLSPVGSGAYGQVCSAFDTKTGRKVAIKKLSRP--FQSAIHAKrtyRELRLLKHMKHENVIGLLDVFTPASSLedf 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  76 ---YIVMEYCdGGDLMQKIKQQKgklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLL 152
Cdd:cd07851  93 qdvYLVTHLM-GADLNNIVKCQK---LSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLARHT 168
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23510391 153 SNPMAfacTYVGTPYYVPPEIWEN-LPYNNKSDIWSLGCILYELCTLKHPFQAN---SWKNLILKVC 215
Cdd:cd07851 169 DDEMT---GYVATRWYRAPEIMLNwMHYNQTVDIWSVGCIMAELLTGKTLFPGSdhiDQLKRIMNLV 232
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
4-197 2.22e-28

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: 114.56  E-value: 2.22e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRlpksfsNTQNSRKEAVLLAKM------KHP----NIVAFKESFEAEG 73
Cdd:cd14210  15 YEVLSVLGKGSFGQVVKCLDHKTGQLVAIKIIR------NKKRFHQQALVEVKIlkhlndNDPddkhNIVRYKDSFIFRG 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  74 HLYIVMEYCdGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGK--VKLGDFGSARL 151
Cdd:cd14210  89 HLCIVFELL-SINLYELLKSNNFQGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSKssIKVIDFGSSCF 167
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 23510391 152 LSNPMAfacTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCT 197
Cdd:cd14210 168 EGEKVY---TYIQSRFYRAPEVILGLPYDTAIDMWSLGCILAELYT 210
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
10-203 2.38e-28

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: 114.69  E-value: 2.38e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHE--SSNQMFAMKEIRLPKS----FSntQNSRKEAVLLAKMKHPNIVAFKESF--EAEGHLYIVMEY 81
Cdd:cd07842   8 IGRGTYGRVYKAKRKngKDGKEYAIKKFKGDKEqytgIS--QSACREIALLRELKHENVVSLVEVFleHADKSVYLLFDY 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGgDLMQKIK---QQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLT----QNGKVKLGDFGSARLLSN 154
Cdd:cd07842  86 AEH-DLWQIIKfhrQAKRVSIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVMgegpERGVVKIGDLGLARLFNA 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 23510391 155 PMAFACT---YVGTPYYVPPEIwenL----PYNNKSDIWSLGCILYELCTLKHPFQ 203
Cdd:cd07842 165 PLKPLADldpVVVTIWYRAPEL---LlgarHYTKAIDIWAIGCIFAELLTLEPIFK 217
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
4-197 2.50e-28

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: 113.73  E-value: 2.50e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCD 83
Cdd:cd07836   2 FKQLEKLGEGTYATVYKGRNRTTGEIVALKEIHLDAEEGTPSTAIREISLMKELKHENIVRLHDVIHTENKLMLVFEYMD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  84 GgDLMQ--KIKQQKGKLFPedMILNWFTQMCL-GVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFAC 160
Cdd:cd07836  82 K-DLKKymDTHGVRGALDP--NTVKSFTYQLLkGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARAFGIPVNTFS 158
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 23510391 161 TYVGTPYYVPPEI-WENLPYNNKSDIWSLGCILYELCT 197
Cdd:cd07836 159 NEVVTLWYRAPDVlLGSRTYSTSIDIWSVGCIMAEMIT 196
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
1-253 3.18e-28

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: 113.09  E-value: 3.18e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   1 MDDYMVLRMIGEGSFGR---ALLVQ--HESSNQMFAMKEIrlpKSFSNTQNSRKE-----AVLLAKMKHPNIVAFKESFE 70
Cdd:cd14198   2 MDNFNNFYILTSKELGRgkfAVVRQciSKSTGQEYAAKFL---KKRRRGQDCRAEilheiAVLELAKSNPRVVNLHEVYE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  71 AEGHLYIVMEYCDGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQN---GKVKLGDFG 147
Cdd:cd14198  79 TTSEIILILEYAAGGEIFNLCVPDLAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIyplGDIKIVDFG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 148 SARLLSNpmafACTY---VGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLPS 224
Cdd:cd14198 159 MSRKIGH----ACELreiMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNISQVNVDYSEE 234
                       250       260       270
                ....*....|....*....|....*....|..
gi 23510391 225 HYSYELQF---LVKQMFKRNPSHRPSATTLLS 253
Cdd:cd14198 235 TFSSVSQLatdFIQKLLVKNPEKRPTAEICLS 266
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
9-254 3.98e-28

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: 112.77  E-value: 3.98e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   9 MIGEGSFG---RALLVQHEssnqmFAMKEIRL--PKSFSNT-QNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYC 82
Cdd:cd14148   1 IIGVGGFGkvyKGLWRGEE-----VAVKAARQdpDEDIAVTaENVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEYA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  83 DGGDLMQKIkqqKGKLFPEDMILNWFTQMCLGVNHIHKKR---VLHRDIKSKNIFLTQ--------NGKVKLGDFGSARL 151
Cdd:cd14148  76 RGGALNRAL---AGKKVPPHVLVNWAVQIARGMNYLHNEAivpIIHRDLKSSNILILEpienddlsGKTLKITDFGLARE 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 152 L--SNPMAFACTYVgtpyYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCIS-PLPSHYSY 228
Cdd:cd14148 153 WhkTTKMSAAGTYA----WMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYREIDALAVAYGVAMNKLTlPIPSTCPE 228
                       250       260
                ....*....|....*....|....*.
gi 23510391 229 ELQFLVKQMFKRNPSHRPSATTLLSR 254
Cdd:cd14148 229 PFARLLEECWDPDPHGRPDFGSILKR 254
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
4-252 5.57e-28

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: 112.33  E-value: 5.57e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLpksfsnTQNSRKEAVL-----LAKMKHPNIVAFKESFEAEGHLYIV 78
Cdd:cd06647   9 YTRFEKIGQGASGTVYTAIDVATGQEVAIKQMNL------QQQPKKELIIneilvMRENKNPNIVNYLDSYLVGDELWVV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  79 MEYCDGGDLMQKIKQQKgklfPEDMILNWFTQMCL-GVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMA 157
Cdd:cd06647  83 MEYLAGGSLTDVVTETC----MDEGQIAAVCRECLqALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 158 FACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPF-QANSWKNLILKVCQGCIS-PLPSHYSYELQFLVK 235
Cdd:cd06647 159 KRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYlNENPLRALYLIATNGTPElQNPEKLSAIFRDFLN 238
                       250
                ....*....|....*..
gi 23510391 236 QMFKRNPSHRPSATTLL 252
Cdd:cd06647 239 RCLEMDVEKRGSAKELL 255
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
4-252 5.58e-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: 112.90  E-value: 5.58e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKE-IRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYC 82
Cdd:cd07846   3 YENLGLVGEGSYGMVMKCRHKETGQIVAIKKfLESEDDKMVKKIAMREIKMLKQLRHENLVNLIEVFRRKKRWYLVFEFV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  83 DGgDLMQKIKQQKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTY 162
Cdd:cd07846  83 DH-TVLDDLEKYPNGL-DESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDY 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 163 VGTPYYVPPEIW-ENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKV--CQGCISP----------------LP 223
Cdd:cd07846 161 VATRWYRAPELLvGDTKYGKAVDVWAVGCLVTEMLTGEPLFPGDSDIDQLYHIikCLGNLIPrhqelfqknplfagvrLP 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 23510391 224 S------------HYSYELQFLVKQMFKRNPSHRPSATTLL 252
Cdd:cd07846 241 EvkeveplerrypKLSGVVIDLAKKCLHIDPDKRPSCSELL 281
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
3-254 6.16e-28

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: 112.43  E-value: 6.16e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRM---IGEGSFGRalLVQHESSNQMFAMKEIRLP--KSFSNT-QNSRKEAVLLAKMKHPNIVAFKESFEAEGHLY 76
Cdd:cd14147   1 SFQELRLeevIGIGGFGK--VYRGSWRGELVAVKAARQDpdEDISVTaESVRQEARLFAMLAHPNIIALKAVCLEEPNLC 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEYCDGGDLMQKIkqqKGKLFPEDMILNWFTQMCLGVNHIHKKR---VLHRDIKSKNIFLTQNGK--------VKLGD 145
Cdd:cd14147  79 LVMEYAAGGPLSRAL---AGRRVPPHVLVNWAVQIARGMHYLHCEAlvpVIHRDLKSNNILLLQPIEnddmehktLKITD 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 146 FGSARLL--SNPMAFACTYVgtpyYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCIS-PL 222
Cdd:cd14147 156 FGLAREWhkTTQMSAAGTYA----WMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRGIDCLAVAYGVAVNKLTlPI 231
                       250       260       270
                ....*....|....*....|....*....|..
gi 23510391 223 PSHYSYELQFLVKQMFKRNPSHRPSATTLLSR 254
Cdd:cd14147 232 PSTCPEPFAQLMADCWAQDPHRRPDFASILQQ 263
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
2-214 9.25e-28

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: 111.53  E-value: 9.25e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIrlPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd14108   2 DYYDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFI--PVRAKKKTSARRELALLAELDHKSIVRFHDAFEKRRVVIIVTEL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CdGGDLMQKIKQQKGKLfpEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNG--KVKLGDFGSARLLSNPMAFA 159
Cdd:cd14108  80 C-HEELLERITKRPTVC--ESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKtdQVRICDFGNAQELTPNEPQY 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 23510391 160 CTYvGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKV 214
Cdd:cd14108 157 CKY-GTPEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNI 210
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
9-254 1.05e-27

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: 111.67  E-value: 1.05e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   9 MIGEGSFGRalLVQHESSNQMFAMKEIRL--PKSFSNTQNS-RKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGG 85
Cdd:cd14146   1 IIGVGGFGK--VYRATWKGQEVAVKAARQdpDEDIKATAESvRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFARGG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  86 DLMQKI-------KQQKGKLFPEDMILNWFTQMCLGVNHIHKKRV---LHRDIKSKNIFLTQ--------NGKVKLGDFG 147
Cdd:cd14146  79 TLNRALaaanaapGPRRARRIPPHILVNWAVQIARGMLYLHEEAVvpiLHRDLKSSNILLLEkiehddicNKTLKITDFG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 148 SARLL--SNPMAFACTYVgtpyYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCIS-PLPS 224
Cdd:cd14146 159 LAREWhrTTKMSAAGTYA----WMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYRGIDGLAVAYGVAVNKLTlPIPS 234
                       250       260       270
                ....*....|....*....|....*....|
gi 23510391 225 HYSYELQFLVKQMFKRNPSHRPSATTLLSR 254
Cdd:cd14146 235 TCPEPFAKLMKECWEQDPHIRPSFALILEQ 264
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
1-267 1.07e-27

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: 111.88  E-value: 1.07e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   1 MDDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEI---RLPKSFSNTQnSRKEAVLLAKMKHPNIVAFKESFEAEGHLYI 77
Cdd:cd14117   5 IDDFDIGRPLGKGKFGNVYLAREKQSKFIVALKVLfksQIEKEGVEHQ-LRREIEIQSHLRHPNILRLYNYFHDRKRIYL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  78 VMEYCDGGDLMQKIkqQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSArlLSNPMA 157
Cdd:cd14117  84 ILEYAPRGELYKEL--QKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWS--VHAPSL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 158 FACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISpLPSHYSYELQFLVKQM 237
Cdd:cd14117 160 RRRTMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVDLK-FPPFLSDGSRDLISKL 238
                       250       260       270
                ....*....|....*....|....*....|
gi 23510391 238 FKRNPSHRPSATTLLSRGIVARLVQKCLPP 267
Cdd:cd14117 239 LRYHPSERLPLKGVMEHPWVKANSRRVLPP 268
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
2-252 1.11e-27

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: 112.03  E-value: 1.11e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKeIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAF-----KESFEAEGHLY 76
Cdd:cd06638  18 DTWEIIETIGKGTYGKVFKVLNKKNGSKAAVK-ILDPIHDIDEEIEAEYNILKALSDHPNVVKFygmyyKKDVKNGDQLW 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEYCDGGDLMQKIKQ--QKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSN 154
Cdd:cd06638  97 LVLELCNGGSVTDLVKGflKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTS 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 155 PMAFACTYVGTPYYVPPEIWE-----NLPYNNKSDIWSLGCILYEL------CTLKHPFQAnswknlILKVCQGCISPL- 222
Cdd:cd06638 177 TRLRRNTSVGTPFWMAPEVIAceqqlDSTYDARCDVWSLGITAIELgdgdppLADLHPMRA------LFKIPRNPPPTLh 250
                       250       260       270
                ....*....|....*....|....*....|.
gi 23510391 223 -PSHYSYELQFLVKQMFKRNPSHRPSATTLL 252
Cdd:cd06638 251 qPELWSNEFNDFIRKCLTKDYEKRPTVSDLL 281
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
2-221 1.24e-27

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: 111.93  E-value: 1.24e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKS---FSNTqnSRKEAVLLAKMKHPNIVAFKESFEAEG--HLY 76
Cdd:cd07843   5 DEYEKLNRIEEGTYGVVYRARDKKTGEIVALKKLKMEKEkegFPIT--SLREINILLKLQHPNIVTVKEVVVGSNldKIY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEYC--DGGDLMQKIKQQkgklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSN 154
Cdd:cd07843  83 MVMEYVehDLKSLMETMKQP----FLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLAREYGS 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23510391 155 PMAFACTYVGTPYYVPPEIWENLP-YNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISP 221
Cdd:cd07843 159 PLKPYTQLVVTLWYRAPELLLGAKeYSTAIDMWSVGCIFAELLTKKPLFPGKSEIDQLNKIFKLLGTP 226
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
4-195 1.28e-27

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: 111.76  E-value: 1.28e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSR-KEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYC 82
Cdd:cd07839   2 YEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEGVPSSAlREICLLKELKHKNIVRLYDVLHSDKKLTLVFEYC 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  83 DGgDLMQKIKQQKGKLFPEdMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTY 162
Cdd:cd07839  82 DQ-DLKKYFDSCNGDIDPE-IVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARAFGIPVRCYSAE 159
                       170       180       190
                ....*....|....*....|....*....|....
gi 23510391 163 VGTPYYVPPEIWENLP-YNNKSDIWSLGCILYEL 195
Cdd:cd07839 160 VVTLWYRPPDVLFGAKlYSTSIDMWSAGCIFAEL 193
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
10-252 1.28e-27

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: 112.05  E-value: 1.28e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKEIRLPKsfsntQNSRK----EAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGG 85
Cdd:cd06658  30 IGEGSTGIVCIATEKHTGKQVAVKKMDLRK-----QQRREllfnEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGG 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  86 DLMQKIKQQKgklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTYVGT 165
Cdd:cd06658 105 ALTDIVTHTR---MNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQVSKEVPKRKSLVGT 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 166 PYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFqansWKNLILKVCQGCISPLP-----SH-YSYELQFLVKQMFK 239
Cdd:cd06658 182 PYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPY----FNEPPLQAMRRIRDNLPprvkdSHkVSSVLRGFLDLMLV 257
                       250
                ....*....|...
gi 23510391 240 RNPSHRPSATTLL 252
Cdd:cd06658 258 REPSQRATAQELL 270
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
2-253 1.30e-27

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: 111.29  E-value: 1.30e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVL-RMIGEGSFGRALLVQHESSNQMFAMKEIRLPKsfsNTQNSRKE-----AVLLAKMKHPNIVAFKESFEAEGHL 75
Cdd:cd14106   7 EVYTVEsTPLGRGKFAVVRKCIHKETGKEYAAKFLRKRR---RGQDCRNEilheiAVLELCKDCPRVVNLHEVYETRSEL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  76 YIVMEYCDGGDLMQKIKQQKgkLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQ---NGKVKLGDFGSARLL 152
Cdd:cd14106  84 ILILELAAGGELQTLLDEEE--CLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSefpLGDIKLCDFGISRVI 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 153 sNPMAFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLPSHY---SYE 229
Cdd:cd14106 162 -GEGEEIREILGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQCNLDFPEELFkdvSPL 240
                       250       260
                ....*....|....*....|....
gi 23510391 230 LQFLVKQMFKRNPSHRPSATTLLS 253
Cdd:cd14106 241 AIDFIKRLLVKDPEKRLTAKECLE 264
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
10-271 1.76e-27

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: 111.65  E-value: 1.76e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKEIRLPKsfsntQNSRK----EAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGG 85
Cdd:cd06657  28 IGEGSTGIVCIATVKSSGKLVAVKKMDLRK-----QQRREllfnEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGG 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  86 DLMQKIKQQKgklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTYVGT 165
Cdd:cd06657 103 ALTDIVTHTR---MNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGT 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 166 PYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFqansWKNLILKVCQGCISPLPSHY------SYELQFLVKQMFK 239
Cdd:cd06657 180 PYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPY----FNEPPLKAMKMIRDNLPPKLknlhkvSPSLKGFLDRLLV 255
                       250       260       270
                ....*....|....*....|....*....|..
gi 23510391 240 RNPSHRPSATTLLSRGIVArlvqKCLPPEIIM 271
Cdd:cd06657 256 RDPAQRATAAELLKHPFLA----KAGPPSCIV 283
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
4-195 1.79e-27

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: 111.59  E-value: 1.79e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCD 83
Cdd:cd07870   2 YLNLEKLGEGSYATVYKGISRINGQLVALKVISMKTEEGVPFTAIREASLLKGLKHANIVLLHDIIHTKETLTFVFEYMH 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  84 GgDLMQKIKQQKGKLFPEDMILNWFtQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTYV 163
Cdd:cd07870  82 T-DLAQYMIQHPGGLHPYNVRLFMF-QLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLARAKSIPSQTYSSEV 159
                       170       180       190
                ....*....|....*....|....*....|...
gi 23510391 164 GTPYYVPPEI-WENLPYNNKSDIWSLGCILYEL 195
Cdd:cd07870 160 VTLWYRPPDVlLGATDYSSALDIWGAGCIFIEM 192
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
4-245 1.85e-27

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: 111.04  E-value: 1.85e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALL------VQHESSNQMfAMKEIRLPKSFSNTQNSR--KEAVLLAKMKHPNIVAFKESFEAEGHL 75
Cdd:cd14076   3 YILGRTLGEGEFGKVKLgwplpkANHRSGVQV-AIKLIRRDTQQENCQTSKimREINILKGLTHPNIVRLLDVLKTKKYI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  76 YIVMEYCDGGDLMQKIkqQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARL--LS 153
Cdd:cd14076  82 GIVLEFVSGGELFDYI--LARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANTfdHF 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 154 NPMAFAcTYVGTPYYVPPE--IWENLPYNNKSDIWSLGCILYELCTLKHPFQAN----SWKNLILKVCQGCISPL--PSH 225
Cdd:cd14076 160 NGDLMS-TSCGSPCYAAPElvVSDSMYAGRKADIWSCGVILYAMLAGYLPFDDDphnpNGDNVPRLYRYICNTPLifPEY 238
                       250       260
                ....*....|....*....|
gi 23510391 226 YSYELQFLVKQMFKRNPSHR 245
Cdd:cd14076 239 VTPKARDLLRRILVPNPRKR 258
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
2-254 1.93e-27

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: 112.40  E-value: 1.93e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIrlpKSFSNT---QNSRKEAVLLAKMKHPNIVAFKE-----SFEAEG 73
Cdd:cd07849   5 PRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKI---SPFEHQtycLRTLREIKILLRFKHENIIGILDiqrppTFESFK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  74 HLYIVMEYCDGgDLMQKIKQQKgklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARL-- 151
Cdd:cd07849  82 DVYIVQELMET-DLYKLIKTQH---LSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLARIad 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 152 -LSNPMAFACTYVGTPYYVPPEIWENLPYNNKS-DIWSLGCILYELCTLKHPFQANSWK---NLILKVC--------QGC 218
Cdd:cd07849 158 pEHDHTGFLTEYVATRWYRAPEIMLNSKGYTKAiDIWSVGCILAEMLSNRPLFPGKDYLhqlNLILGILgtpsqedlNCI 237
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 23510391 219 ISPLPSHYSYELQFLVKQMFKR-NPSHRPSATTLLSR 254
Cdd:cd07849 238 ISLKARNYIKSLPFKPKVPWNKlFPNADPKALDLLDK 274
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
4-253 2.23e-27

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: 110.40  E-value: 2.23e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLP--KSFSNTQNSRK---EAVLLAK---MKHPNIVAFKESFEAEGHL 75
Cdd:cd14005   2 YEVGDLLGKGGFGTVYSGVRIRDGLPVAVKFVPKSrvTEWAMINGPVPvplEIALLLKaskPGVPGVIRLLDWYERPDGF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  76 YIVMEY---CDggDLMQKIKQqKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQN-GKVKLGDFGSARL 151
Cdd:cd14005  82 LLIMERpepCQ--DLFDFITE-RGAL-SENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINLRtGEVKLIDFGCGAL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 152 LSNPMafACTYVGTPYYVPPE-IWENLPYNNKSDIWSLGCILYELCTLKHPFQANS----WKNLIlkvcqgcisplPSHY 226
Cdd:cd14005 158 LKDSV--YTDFDGTRVYSPPEwIRHGRYHGRPATVWSLGILLYDMLCGDIPFENDEqilrGNVLF-----------RPRL 224
                       250       260
                ....*....|....*....|....*..
gi 23510391 227 SYELQFLVKQMFKRNPSHRPSATTLLS 253
Cdd:cd14005 225 SKECCDLISRCLQFDPSKRPSLEQILS 251
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
2-206 2.41e-27

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: 110.48  E-value: 2.41e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRlPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd14191   2 DFYDIEERLGSGKFGQVFRLVEKKTKKVWAGKFFK-AYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDLMQKIKQQKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIF-LTQNG-KVKLGDFGSARLLSNPMAFA 159
Cdd:cd14191  81 VSGGELFERIIDEDFEL-TERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtKIKLIDFGLARRLENAGSLK 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 23510391 160 CTYvGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANS 206
Cdd:cd14191 160 VLF-GTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDN 205
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
7-203 2.85e-27

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: 110.76  E-value: 2.85e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   7 LRMIGEGSFGRALLVQHESSNQMFAMKeiRLPKSFSNTQNSRKEAVL----LAKMKHPNIVAFKESFEAEGHLYIVMEYC 82
Cdd:cd05607   7 FRVLGKGGFGEVCAVQVKNTGQMYACK--KLDKKRLKKKSGEKMALLekeiLEKVNSPFIVSLAYAFETKTHLCLVMSLM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  83 DGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFAcTY 162
Cdd:cd05607  85 NGGDLKYHIYNVGERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEVKEGKPIT-QR 163
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 23510391 163 VGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQ 203
Cdd:cd05607 164 AGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFR 204
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
2-208 3.53e-27

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: 110.74  E-value: 3.53e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEI---RLPKSfSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIV 78
Cdd:cd05608   1 DWFLDFRVLGKGGFGEVSACQMRATGKLYACKKLnkkRLKKR-KGYEGAMVEKRILAKVHSRFIVSLAYAFQTKTDLCLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  79 MEYCDGGDLMQKIKQ--QKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPM 156
Cdd:cd05608  80 MTIMNGGDLRYHIYNvdEENPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVELKDGQ 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 23510391 157 AFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWK 208
Cdd:cd05608 160 TKTKGYAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFRARGEK 211
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
8-252 4.50e-27

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: 109.73  E-value: 4.50e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFGRALLVQHESSNQMFAMKEIRLPksfSNTQNSRKEAV-------LLAKMKHPNIVAFKESFE--AEGHLYIV 78
Cdd:cd06653   8 KLLGRGAFGEVYLCYDADTGRELAVKQVPFD---PDSQETSKEVNaleceiqLLKNLRHDRIVQYYGCLRdpEEKKLSIF 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  79 MEYCDGGDLMQKIKQQkGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFG-SARLLSNPMA 157
Cdd:cd06653  85 VEYMPGGSVKDQLKAY-GAL-TENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGaSKRIQTICMS 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 158 FAC--TYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISP-LPSHYSYELQFLV 234
Cdd:cd06653 163 GTGikSVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPWAEYEAMAAIFKIATQPTKPqLPDGVSDACRDFL 242
                       250
                ....*....|....*...
gi 23510391 235 KQMFKRNpSHRPSATTLL 252
Cdd:cd06653 243 RQIFVEE-KRRPTAEFLL 259
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
1-202 4.70e-27

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: 109.60  E-value: 4.70e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   1 MDDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSfSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVME 80
Cdd:cd14114   1 YDHYDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPHE-SDKETVRKEIQIMNQLHHPKLINLHDAFEDDNEMVLILE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  81 YCDGGDLMQKIKQQKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLT--QNGKVKLGDFGSARLLsNPMAF 158
Cdd:cd14114  80 FLSGGELFERIAAEHYKM-SEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTtkRSNEVKLIDFGLATHL-DPKES 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 23510391 159 ACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPF 202
Cdd:cd14114 158 VKVTTGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPF 201
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
7-216 5.04e-27

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: 110.92  E-value: 5.04e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   7 LRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQ-NSRKEAVLLAKMKHPNIVAFKESFEAEgHL---YIVMEYC 82
Cdd:cd07845  12 LNRIGEGTYGIVYRARDTTSGEIVALKKVRMDNERDGIPiSSLREITLLLNLRHPNIVELKEVVVGK-HLdsiFLVMEYC 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  83 --DGGDLMQKIKQQkgklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFAC 160
Cdd:cd07845  91 eqDLASLLDNMPTP----FSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLARTYGLPAKPMT 166
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 23510391 161 TYVGTPYYVPPEI-WENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQ 216
Cdd:cd07845 167 PKVVTLWYRAPELlLGCTTYTTAIDMWAVGCILAELLAHKPLLPGKSEIEQLDLIIQ 223
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
2-245 5.71e-27

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 111.23  E-value: 5.71e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391    2 DDYMVLRMIGEGSFGRALLVQHESSN------QMFAMKEIRLPKSFSNTQNSRKeavLLAKMKHPNIVAFKESFEAEGHL 75
Cdd:PTZ00426  30 EDFNFIRTLGTGSFGRVILATYKNEDfppvaiKRFEKSKIIKQKQVDHVFSERK---ILNYINHPFCVNLYGSFKDESYL 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   76 YIVMEYCDGGDLMQKIKqqKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNP 155
Cdd:PTZ00426 107 YLVLEFVIGGEFFTFLR--RNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFAKVVDTR 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  156 MAFACtyvGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISpLPSHYSYELQFLVK 235
Cdd:PTZ00426 185 TYTLC---GTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFYANEPLLIYQKILEGIIY-FPKFLDNNCKHLMK 260
                        250
                 ....*....|
gi 23510391  236 QMFKRNPSHR 245
Cdd:PTZ00426 261 KLLSHDLTKR 270
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
10-195 6.56e-27

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: 109.12  E-value: 6.56e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKEIrlpKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDLMQ 89
Cdd:cd14065   1 LGKGFFGEVYKVTHRETGKVMVMKEL---KRFDEQRSFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGTLEE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  90 KIKQQkgklfpeDMILNWFTQMCL------GVNHIHKKRVLHRDIKSKNIFL---TQNGKVKLGDFGSARLLSNPMAF-- 158
Cdd:cd14065  78 LLKSM-------DEQLPWSQRVSLakdiasGMAYLHSKNIIHRDLNSKNCLVreaNRGRNAVVADFGLAREMPDEKTKkp 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 23510391 159 ----ACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYEL 195
Cdd:cd14065 151 drkkRLTVVGSPYWMAPEMLRGESYDEKVDVFSFGIVLCEI 191
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
10-206 7.40e-27

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: 108.85  E-value: 7.40e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKEIRLPKSfSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDLMQ 89
Cdd:cd14103   1 LGRGKFGTVYRCVEKATGKELAAKFIKCRKA-KDREDVRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAGGELFE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  90 KIKQQKGKLFPEDMILnWFTQMCLGVNHIHKKRVLHRDIKSKNIF-LTQNG-KVKLGDFGSARLLsNPMAFACTYVGTPY 167
Cdd:cd14103  80 RVVDDDFELTERDCIL-FMRQICEGVQYMHKQGILHLDLKPENILcVSRTGnQIKIIDFGLARKY-DPDKKLKVLFGTPE 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 23510391 168 YVPPEI--WENLPYnnKSDIWSLGCILYELCTLKHPFQANS 206
Cdd:cd14103 158 FVAPEVvnYEPISY--ATDMWSVGVICYVLLSGLSPFMGDN 196
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
2-195 7.43e-27

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: 110.17  E-value: 7.43e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd07869   5 DSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTAIREASLLKGLKHANIVLLHDIIHTKETLTLVFEY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGgDLMQKIKQQKGKLFPEDMILNWFtQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACT 161
Cdd:cd07869  85 VHT-DLCQYMDKHPGGLHPENVKLFLF-QLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARAKSVPSHTYSN 162
                       170       180       190
                ....*....|....*....|....*....|....*
gi 23510391 162 YVGTPYYVPPEI-WENLPYNNKSDIWSLGCILYEL 195
Cdd:cd07869 163 EVVTLWYRPPDVlLGSTEYSTCLDMWGVGCIFVEM 197
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
3-252 7.96e-27

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: 109.43  E-value: 7.96e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHES-SNQMFAMKEIRLPKSFSNTQNSRKEAV-LLAKMK---HPNIVAFKESFEAEGHLYI 77
Cdd:cd14052   1 RFANVELIGSGEFSQVYKVSERVpTGKVYAVKKLKPNYAGAKDRLRRLEEVsILRELTldgHDNIVQLIDSWEYHGHLYI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  78 VMEYCDGGDL---MQKIKQQKGklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSN 154
Cdd:cd14052  81 QTELCENGSLdvfLSELGLLGR--LDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMATVWPL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 155 PMAFACTyvGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCT-LKHPFQANSWKnlilKVCQGCISPLPSHYSYE---- 229
Cdd:cd14052 159 IRGIERE--GDREYIAPEILSEHMYDKPADIFSLGLILLEAAAnVVLPDNGDAWQ----KLRSGDLSDAPRLSSTDlhsa 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 23510391 230 --------------------LQFLVKQMFKRNPSHRPSATTLL 252
Cdd:cd14052 233 sspssnpppdppnmpilsgsLDRVVRWMLSPEPDRRPTADDVL 275
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
1-257 9.18e-27

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 109.52  E-value: 9.18e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391    1 MDDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSR-KEAVLLAKMKHPNIVAFKESFEAEGHLYIVM 79
Cdd:PLN00009   1 MDQYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQEDEGVPSTAiREISLLKEMQHGNIVRLQDVVHSEKRLYLVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   80 EYCDGgDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQ-NGKVKLGDFGSARLLSNPMAF 158
Cdd:PLN00009  81 EYLDL-DLKKHMDSSPDFAKNPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRrTNALKLADFGLARAFGIPVRT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  159 ACTYVGTPYYVPPEI-WENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQ-----------GCISpLPSHY 226
Cdd:PLN00009 160 FTHEVVTLWYRAPEIlLGSRHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEIDELFKIFRilgtpneetwpGVTS-LPDYK 238
                        250       260       270
                 ....*....|....*....|....*....|.
gi 23510391  227 SYELQFLVKQMFKRNPSHRPSATTLLSRGIV 257
Cdd:PLN00009 239 SAFPKWPPKDLATVVPTLEPAGVDLLSKMLR 269
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
10-247 9.46e-27

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: 108.68  E-value: 9.46e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGrallVQHESS--NQMFAMKEIrlpKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDL 87
Cdd:cd14058   1 VGRGSFG----VVCKARwrNQIVAVKII---ESESEKKAFEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGSL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  88 MQKIKQQKGKL-FPEDMILNWFTQMCLGVNHIHK---KRVLHRDIKSKNIFLTQNGKV-KLGDFGSARLLSNPMAfacTY 162
Cdd:cd14058  74 YNVLHGKEPKPiYTAAHAMSWALQCAKGVAYLHSmkpKALIHRDLKPPNLLLTNGGTVlKICDFGTACDISTHMT---NN 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 163 VGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQ--ANSWKNLILKVCQGCISPLPSHYSYELQFLVKQMFKR 240
Cdd:cd14058 151 KGSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPFDhiGGPAFRIMWAVHNGERPPLIKNCPKPIESLMTRCWSK 230

                ....*..
gi 23510391 241 NPSHRPS 247
Cdd:cd14058 231 DPEKRPS 237
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
10-193 1.25e-26

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: 108.27  E-value: 1.25e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKEIRLPKsFSNTQNS--RKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDL 87
Cdd:cd14082  11 LGSGQFGIVYGGKHRKTGRDVAIKVIDKLR-FPTKQESqlRNEVAILQQLSHPGVVNLECMFETPERVFVVMEKLHGDML 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  88 MQKIKQQKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNG---KVKLGDFGSARLLSNPmAFACTYVG 164
Cdd:cd14082  90 EMILSSEKGRL-PERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEpfpQVKLCDFGFARIIGEK-SFRRSVVG 167
                       170       180
                ....*....|....*....|....*....
gi 23510391 165 TPYYVPPEIWENLPYNNKSDIWSLGCILY 193
Cdd:cd14082 168 TPAYLAPEVLRNKGYNRSLDMWSVGVIIY 196
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
2-252 1.44e-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: 108.96  E-value: 1.44e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIrlpkSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd14175   1 DGYVVKETIGVGSYSVCKRCVHKATNMEYAVKVI----DKSKRDPSEEIEILLRYGQHPNIITLKDVYDDGKHVYLVTEL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDLMQKIKQQkgKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNI-FLTQNGK---VKLGDFGSARLLSNPMA 157
Cdd:cd14175  77 MRGGELLDKILRQ--KFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNIlYVDESGNpesLRICDFGFAKQLRAENG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 158 FACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQ---ANSWKNLILKVCQGCISPLPSHY---SYELQ 231
Cdd:cd14175 155 LLMTPCYTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFAngpSDTPEEILTRIGSGKFTLSGGNWntvSDAAK 234
                       250       260
                ....*....|....*....|.
gi 23510391 232 FLVKQMFKRNPSHRPSATTLL 252
Cdd:cd14175 235 DLVSKMLHVDPHQRLTAKQVL 255
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
2-210 1.57e-26

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: 109.45  E-value: 1.57e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd06615   1 DDFEKLGELGAGNGGVVTKVLHRPSGLIMARKLIHLEIKPAIRNQIIRELKVLHECNSPYIVGFYGAFYSDGEISICMEH 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDLMQKIKqqKGKLFPEDMILNWFTQMCLGVNHIHKKR-VLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMafAC 160
Cdd:cd06615  81 MDGGSLDQVLK--KAGRIPENILGKISIAVLRGLTYLREKHkIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSM--AN 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 23510391 161 TYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNL 210
Cdd:cd06615 157 SFVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGRYPIPPPDAKEL 206
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
4-247 1.68e-26

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: 108.15  E-value: 1.68e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGR---ALLVQHESSNQMFAMKEIRLPKSFSNTQNSRkEAVLLAKMKHPNIVAFKESFE-AEGHLYIVM 79
Cdd:cd14163   2 YQLGKTIGEGTYSKvkeAFSKKHQRKVAIKIIDKSGGPEEFIQRFLPR-ELQIVERLDHKNIIHVYEMLEsADGKIYLVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  80 EYCDGGDLMQKIKQQkGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLtQNGKVKLGDFGSARLL-SNPMAF 158
Cdd:cd14163  81 ELAEDGDVFDCVLHG-GPL-PEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALL-QGFTLKLTDFGFAKQLpKGGREL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 159 ACTYVGTPYYVPPEIWENLPYNN-KSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCisPLPSHY--SYELQFLVK 235
Cdd:cd14163 158 SQTFCGSTAYAAPEVLQGVPHDSrKGDIWSMGVVLYVMLCAQLPFDDTDIPKMLCQQQKGV--SLPGHLgvSRTCQDLLK 235
                       250
                ....*....|..
gi 23510391 236 QMFKRNPSHRPS 247
Cdd:cd14163 236 RLLEPDMVLRPS 247
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
9-245 1.98e-26

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: 108.98  E-value: 1.98e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   9 MIGEGSFGRALLVQHESSNQMFAMKEIrlPKSFSNTQNS--RKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGD 86
Cdd:cd14168  17 VLGTGAFSEVVLAEERATGKLFAVKCI--PKKALKGKESsiENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGE 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  87 LMQKIkQQKGkLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNI--FLTQNG-KVKLGDFGSARL--LSNPMAFACt 161
Cdd:cd14168  95 LFDRI-VEKG-FYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLlyFSQDEEsKIMISDFGLSKMegKGDVMSTAC- 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 162 yvGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNL---ILKVCQGCISPLPSHYSYELQFLVKQMF 238
Cdd:cd14168 172 --GTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLfeqILKADYEFDSPYWDDISDSAKDFIRNLM 249

                ....*..
gi 23510391 239 KRNPSHR 245
Cdd:cd14168 250 EKDPNKR 256
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
2-280 3.17e-26

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: 108.60  E-value: 3.17e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd06650   5 DDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEH 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDLMQKIKQqKGKLfPEDMILNWFTQMCLGVNHIHKK-RVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMafAC 160
Cdd:cd06650  85 MDGGSLDQVLKK-AGRI-PEQILGKVSIAVIKGLTYLREKhKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSM--AN 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 161 TYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHpfqanswknlilkvcqgcisPLPSHYSYELQFLVKQMFKR 240
Cdd:cd06650 161 SFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRY--------------------PIPPPDAKELELMFGCQVEG 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 23510391 241 NPSH-----RPSATTLLSRGIVARlvqkclPPEIIMEYGEEVLEE 280
Cdd:cd06650 221 DAAEtpprpRTPGRPLSSYGMDSR------PPMAIFELLDYIVNE 259
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
3-253 3.82e-26

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: 107.15  E-value: 3.82e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHESSNQMfAMKEIRlpKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYC 82
Cdd:cd05059   5 ELTFLKELGSGQFGVVHLGKWRGKIDV-AIKMIK--EGSMSEDDFIEEAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEYM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  83 DGGDLMQKIKQQKGKLFPEdMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPmAFACTy 162
Cdd:cd05059  82 ANGCLLNYLRERRGKFQTE-QLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLARYVLDD-EYTSS- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 163 VGTPYYV---PPEIWENLPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQMF 238
Cdd:cd05059 159 VGTKFPVkwsPPEVFMYSKFSSKSDVWSFGVLMWEVFSEgKMPYERFSNSEVVEHISQGYRLYRPHLAPTEVYTIMYSCW 238
                       250
                ....*....|....*
gi 23510391 239 KRNPSHRPSATTLLS 253
Cdd:cd05059 239 HEKPEERPTFKILLS 253
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
1-214 5.10e-26

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: 108.99  E-value: 5.10e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   1 MDDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNS--RKEAVLLAKMKHPNIVAFKESFEAEGHLYIV 78
Cdd:cd05627   1 LDDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQVAhiRAERDILVEADGAWVVKMFYSFQDKRNLYLI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  79 MEYCDGGDLMQKIkqQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSA--------- 149
Cdd:cd05627  81 MEFLPGGDMMTLL--MKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLCtglkkahrt 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 150 ----RLLSNPMA----------------------FACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQ 203
Cdd:cd05627 159 efyrNLTHNPPSdfsfqnmnskrkaetwkknrrqLAYSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFC 238
                       250
                ....*....|.
gi 23510391 204 ANSWKNLILKV 214
Cdd:cd05627 239 SETPQETYRKV 249
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
1-197 5.15e-26

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: 107.77  E-value: 5.15e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   1 MDDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVME 80
Cdd:cd07872   5 METYIKLEKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIVHTDKSLTLVFE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  81 YCDGgDLMQKIkQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFAC 160
Cdd:cd07872  85 YLDK-DLKQYM-DDCGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSVPTKTYS 162
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 23510391 161 TYVGTPYYVPPEI-WENLPYNNKSDIWSLGCILYELCT 197
Cdd:cd07872 163 NEVVTLWYRPPDVlLGSSEYSTQIDMWGVGCIFFEMAS 200
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
11-253 7.55e-26

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: 105.81  E-value: 7.55e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  11 GEGSFGRALLVQHESSNQMFAMKEIrlpksfsntQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDLMQK 90
Cdd:cd14060   2 GGGSFGSVYRAIWVSQDKEVAVKKL---------LKIEKEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLFDY 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  91 IKQQKGKLFPEDMILNWFTQMCLGVNHIHKK---RVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFacTYVGTPY 167
Cdd:cd14060  73 LNSNESEEMDMDQIMTWATDIAKGMHYLHMEapvKVIHRDLKSRNVVIAADGVLKICDFGASRFHSHTTHM--SLVGTFP 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 168 YVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISP-LPSHYSYELQFLVKQMFKRNPSHRP 246
Cdd:cd14060 151 WMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPFKGLEGLQVAWLVVEKNERPtIPSSCPRSFAELMRRCWEADVKERP 230

                ....*..
gi 23510391 247 SATTLLS 253
Cdd:cd14060 231 SFKQIIG 237
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
7-202 7.84e-26

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: 107.77  E-value: 7.84e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   7 LRMIGEGSFGRALLVQHESSNQMFAMKEIR----LPKSFSNTQNSRK---EAVllAKMKHPNIVAFKESFEAEGHLYIVM 79
Cdd:cd05589   4 IAVLGRGHFGKVLLAEYKPTGELFAIKALKkgdiIARDEVESLMCEKrifETV--NSARHPFLVNLFACFQTPEHVCFVM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  80 EYCDGGDLMQKIKQQkgkLFPEDMILnwFTQMC--LGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGsarLLSNPMA 157
Cdd:cd05589  82 EYAAGGDLMMHIHED---VFSEPRAV--FYAACvvLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFG---LCKEGMG 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 23510391 158 FA---CTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPF 202
Cdd:cd05589 154 FGdrtSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPF 201
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
10-214 9.46e-26

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: 106.59  E-value: 9.46e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKEIRLPksfsNTQN-----SRKEAVLLAKMK---HPNIVAFKE-----SFEAEGHLY 76
Cdd:cd07863   8 IGVGAYGTVYKARDPHSGHFVALKSVRVQ----TNEDglplsTVREVALLKRLEafdHPNIVRLMDvcatsRTDRETKVT 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEYCDGgDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPM 156
Cdd:cd07863  84 LVFEHVDQ-DLRTYLDKVPPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLARIYSCQM 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 23510391 157 AFACTYVgTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKV 214
Cdd:cd07863 163 ALTPVVV-TLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKI 219
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
2-254 9.61e-26

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: 106.35  E-value: 9.61e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFG---RALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEaEGHLYIV 78
Cdd:cd05056   6 EDITLGRCIGEGQFGdvyQGVYMSPENEKIAVAVKTCKNCTSPSVREKFLQEAYIMRQFDHPHIVKLIGVIT-ENPVWIV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  79 MEYCDGGDLMQKIKQQKGKLFPEDMILnWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAF 158
Cdd:cd05056  85 MELAPLGELRSYLQVNKYSLDLASLIL-YAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSRYMEDESYY 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 159 ACTYVGTPY-YVPPEIWENLPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQ 236
Cdd:cd05056 164 KASKGKLPIkWMAPESINFRRFTSASDVWMFGVCMWEILMLgVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTK 243
                       250
                ....*....|....*...
gi 23510391 237 MFKRNPSHRPSATTLLSR 254
Cdd:cd05056 244 CWAYDPSKRPRFTELKAQ 261
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
1-245 2.04e-25

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: 107.07  E-value: 2.04e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   1 MDDYMVLRMIGEGSFGRALLVQHESSNQMFAMK-----EIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHL 75
Cdd:cd05633   4 MNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKcldkkRIKMKQGETLALNERIMLSLVSTGDCPFIVCMTYAFHTPDKL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  76 YIVMEYCDGGDLMQKIKQQKgkLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNP 155
Cdd:cd05633  84 CFILDLMNGGDLHYHLSQHG--VFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACDFSKK 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 156 MAFACtyVGTPYYVPPEIWEN-LPYNNKSDIWSLGCILYELCTLKHPFQANSWKNL--ILKVCQGCISPLPSHYSYELQF 232
Cdd:cd05633 162 KPHAS--VGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKheIDRMTLTVNVELPDSFSPELKS 239
                       250
                ....*....|...
gi 23510391 233 LVKQMFKRNPSHR 245
Cdd:cd05633 240 LLEGLLQRDVSKR 252
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
4-217 2.05e-25

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: 105.96  E-value: 2.05e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSfSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCD 83
Cdd:cd06655  21 YTRYEKIGQGASGTVFTAIDVATGQEVAIKQINLQKQ-PKKELIINEILVMKELKNPNIVNFLDSFLVGDELFVVMEYLA 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  84 GGDLMQKIKQQkgkLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTYV 163
Cdd:cd06655 100 GGSLTDVVTET---CMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQITPEQSKRSTMV 176
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 23510391 164 GTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPF-QANSWKNLILKVCQG 217
Cdd:cd06655 177 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYlNENPLRALYLIATNG 231
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
3-245 2.12e-25

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: 106.29  E-value: 2.12e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHESSNQMFAMK-----EIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYI 77
Cdd:cd14223   1 DFSVHRIIGRGGFGEVYGCRKADTGKMYAMKcldkkRIKMKQGETLALNERIMLSLVSTGDCPFIVCMSYAFHTPDKLSF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  78 VMEYCDGGDLMQKIKQQKgkLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMA 157
Cdd:cd14223  81 ILDLMNGGDLHYHLSQHG--VFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLACDFSKKKP 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 158 FACtyVGTPYYVPPEIWEN-LPYNNKSDIWSLGCILYELCTLKHPFQANSWKNL--ILKVCQGCISPLPSHYSYELQFLV 234
Cdd:cd14223 159 HAS--VGTHGYMAPEVLQKgVAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKheIDRMTLTMAVELPDSFSPELRSLL 236
                       250
                ....*....|.
gi 23510391 235 KQMFKRNPSHR 245
Cdd:cd14223 237 EGLLQRDVNRR 247
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
4-206 2.79e-25

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: 105.50  E-value: 2.79e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQH-ESSNQMFAMKEIRLPKSFSNTQNS--RKEAVL--LAKMKHPNIVAFKE-----SFEAEG 73
Cdd:cd07862   3 YECVAEIGEGAYGKVFKARDlKNGGRFVALKRVRVQTGEEGMPLStiREVAVLrhLETFEHPNVVRLFDvctvsRTDRET 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  74 HLYIVMEYCDGgDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLS 153
Cdd:cd07862  83 KLTLVFEHVDQ-DLTTYLDKVPEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLARIYS 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 23510391 154 NPMAFACTYVgTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANS 206
Cdd:cd07862 162 FQMALTSVVV-TLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFRGSS 213
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
2-263 2.94e-25

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: 104.72  E-value: 2.94e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAV-----LLAKMKHPNIVAFKESFEAEGHLY 76
Cdd:cd14194   5 DYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRRGVSREDIerevsILKEIQHPNVITLHEVYENKTDVI 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEYCDGGDLMQKIKQQKGklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNG----KVKLGDFGSARLL 152
Cdd:cd14194  85 LILELVAGGELFDFLAEKES--LTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNvpkpRIKIIDFGLAHKI 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 153 SNPMAFACTYvGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVcqgcisplpSHYSYELQf 232
Cdd:cd14194 163 DFGNEFKNIF-GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANV---------SAVNYEFE- 231
                       250       260       270
                ....*....|....*....|....*....|.
gi 23510391 233 lvKQMFkrnpshrpSATTLLSRGIVARLVQK 263
Cdd:cd14194 232 --DEYF--------SNTSALAKDFIRRLLVK 252
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
8-245 3.32e-25

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: 105.07  E-value: 3.32e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFGRALLVQHESSNQMFAMKEI---RLPKSFSNTQnSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDG 84
Cdd:cd05631   6 RVLGKGGFGEVCACQVRATGKMYACKKLekkRIKKRKGEAM-ALNEKRILEKVNSRFVVSLAYAYETKDALCLVLTIMNG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  85 GDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFAcTYVG 164
Cdd:cd05631  85 GDLKFHIYNMGNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQIPEGETVR-GRVG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 165 TPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQAN----SWKNLILKVCQGcISPLPSHYSYELQFLVKQMFKR 240
Cdd:cd05631 164 TVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRkervKREEVDRRVKED-QEEYSEKFSEDAKSICRMLLTK 242

                ....*
gi 23510391 241 NPSHR 245
Cdd:cd05631 243 NPKER 247
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
10-195 4.54e-25

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: 103.71  E-value: 4.54e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKEIRLPksfSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDLMQ 89
Cdd:cd14155   1 IGSGFFSEVYKVRHRTSGQVMALKMNTLS---SNRANMLREVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGGNLEQ 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  90 kikqqkgkLFPEDMILNWFTQMCL------GVNHIHKKRVLHRDIKSKNIFL--TQNG-KVKLGDFGSARLL------SN 154
Cdd:cd14155  78 --------LLDSNEPLSWTVRVKLaldiarGLSYLHSKGIFHRDLTSKNCLIkrDENGyTAVVGDFGLAEKIpdysdgKE 149
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 23510391 155 PMAFactyVGTPYYVPPEIWENLPYNNKSDIWSLGCILYEL 195
Cdd:cd14155 150 KLAV----VGSPYWMAPEVLRGEPYNEKADVFSYGIILCEI 186
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
1-245 4.89e-25

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: 104.66  E-value: 4.89e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   1 MDDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRK-------------------------EAVLLA 55
Cdd:cd14199   1 LNQYKLKDEIGKGSYGVVKLAYNEDDNTYYAMKVLSKKKLMRQAGFPRRppprgaraapegctqprgpiervyqEIAILK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  56 KMKHPNIVAFKESFE--AEGHLYIVMEYCDGGDLMQkikQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNI 133
Cdd:cd14199  81 KLDHPNVVKLVEVLDdpSEDHLYMVFELVKQGPVME---VPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 134 FLTQNGKVKLGDFGSARLLSNPMAFACTYVGTPYYVPPEIWENLP--YNNKS-DIWSLGCILYELCTLKHPFQANSWKNL 210
Cdd:cd14199 158 LVGEDGHIKIADFGVSNEFEGSDALLTNTVGTPAFMAPETLSETRkiFSGKAlDVWAMGVTLYCFVFGQCPFMDERILSL 237
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 23510391 211 ILKV-CQGCISPLPSHYSYELQFLVKQMFKRNPSHR 245
Cdd:cd14199 238 HSKIkTQPLEFPDQPDISDDLKDLLFRMLDKNPESR 273
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
2-257 5.71e-25

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: 105.89  E-value: 5.71e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLP-KSFSNTQNSRKEAVLLAKMKHPNIVAF------KESFEAEGH 74
Cdd:cd07877  17 ERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRPfQSIIHAKRTYRELRLLKHMKHENVIGLldvftpARSLEEFND 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  75 LYIVMEYCdGGDLMQKIKQQKgklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSN 154
Cdd:cd07877  97 VYLVTHLM-GADLNNIVKCQK---LTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDD 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 155 PMAfacTYVGTPYYVPPEIWEN-LPYNNKSDIWSLGCILYELCTLKHPFQANSWKN---LILKVC----QGCISPLPSHY 226
Cdd:cd07877 173 EMT---GYVATRWYRAPEIMLNwMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDqlkLILRLVgtpgAELLKKISSES 249
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 23510391 227 SYELQFLVKQMFKRNPSH-----RPSATTLLSRGIV 257
Cdd:cd07877 250 ARNYIQSLTQMPKMNFANvfigaNPLAVDLLEKMLV 285
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
10-208 7.15e-25

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: 104.27  E-value: 7.15e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHL------YIVMEYCD 83
Cdd:cd14038   2 LGTGGFGNVLRWINQETGEQVAIKQCRQELSPKNRERWCLEIQIMKRLNHPNVVAARDVPEGLQKLapndlpLLAMEYCQ 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  84 GGDLMQKIKQQKGKL-FPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKV---KLGDFGSARLLSNpmAFA 159
Cdd:cd14038  82 GGDLRKYLNQFENCCgLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGEQRlihKIIDLGYAKELDQ--GSL 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 23510391 160 CT-YVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANsWK 208
Cdd:cd14038 160 CTsFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPFLPN-WQ 208
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
4-203 7.86e-25

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: 105.15  E-value: 7.86e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRlpKSFSNTQNSRK---EAVLLAKMKHPNIVAFK--------ESFEae 72
Cdd:cd07858   7 YVPIKPIGRGAYGIVCSAKNSETNEKVAIKKIA--NAFDNRIDAKRtlrEIKLLRHLDHENVIAIKdimppphrEAFN-- 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  73 gHLYIVMEYCDGgDLMQKIKQQKGklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLL 152
Cdd:cd07858  83 -DVYIVYELMDT-DLHQIIRSSQT--LSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLARTT 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 23510391 153 SNPMAFACTYVGTPYYVPPEI---WENlpYNNKSDIWSLGCILYELCTLKHPFQ 203
Cdd:cd07858 159 SEKGDFMTEYVVTRWYRAPELllnCSE--YTTAIDVWSVGCIFAELLGRKPLFP 210
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
2-253 7.92e-25

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


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 103.58  E-value: 7.92e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMfAMKEIRlPKSFSnTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd05072   7 ESIKLVKKLGAGQFGEVWMGYYNNSTKV-AVKTLK-PGTMS-VQAFLEEANLMKTLQHDKLVRLYAVVTKEEPIYIITEY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACT 161
Cdd:cd05072  84 MAKGSLLDFLKSDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIEDNEYTARE 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 162 YVGTPY-YVPPEIWENLPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQMFK 239
Cdd:cd05072 164 GAKFPIkWTAPEAINFGSFTIKSDVWSFGILLYEIVTYgKIPYPGMSNSDVMSALQRGYRMPRMENCPDELYDIMKTCWK 243
                       250
                ....*....|....
gi 23510391 240 RNPSHRPSATTLLS 253
Cdd:cd05072 244 EKAEERPTFDYLQS 257
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
1-210 8.44e-25

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: 105.88  E-value: 8.44e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   1 MDDYMVLRMIGEGSFGRALLVQHESSNQMFAMKeiRLPKSFSNTQNSRK----EAVLLAKMKHPNIVAFKESFEAEGHLY 76
Cdd:cd05600  10 LSDFQILTQVGQGGYGSVFLARKKDTGEICALK--IMKKKVLFKLNEVNhvltERDILTTTNSPWLVKLLYAFQDPENVY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEYCDGGDlMQKIKQQKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFG-------SA 149
Cdd:cd05600  88 LAMEYVPGGD-FRTLLNNSGIL-SEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGlasgtlsPK 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 150 RLLSN--------------------------------PMAFACtyVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCT 197
Cdd:cd05600 166 KIESMkirleevkntafleltakerrniyramrkedqNYANSV--VGSPDYMAPEVLRGEGYDLTVDYWSLGCILFECLV 243
                       250
                ....*....|....*..
gi 23510391 198 LKHPFQANS----WKNL 210
Cdd:cd05600 244 GFPPFSGSTpnetWANL 260
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
10-254 8.73e-25

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: 102.86  E-value: 8.73e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFG-------------RALLVQHESSNQMFAMKeirlpksfsntqnsrKEAVLLAKMKHPNIVAFKeSFEAEGHLY 76
Cdd:cd14062   1 IGSGSFGtvykgrwhgdvavKKLNVTDPTPSQLQAFK---------------NEVAVLRKTRHVNILLFM-GYMTKPQLA 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEYCDGGDLMQKIKQQKGKlFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARL----- 151
Cdd:cd14062  65 IVTQWCEGSSLYKHLHVLETK-FEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLATVktrws 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 152 ----LSNPMafactyvGTPYYVPPEIWENL---PYNNKSDIWSLGCILYELCTLKHPFQANSWKNLIL-KVCQGCISP-- 221
Cdd:cd14062 144 gsqqFEQPT-------GSILWMAPEVIRMQdenPYSFQSDVYAFGIVLYELLTGQLPYSHINNRDQILfMVGRGYLRPdl 216
                       250       260       270
                ....*....|....*....|....*....|....*
gi 23510391 222 --LPSHYSYELQFLVKQMFKRNPSHRPSATTLLSR 254
Cdd:cd14062 217 skVRSDTPKALRRLMEDCIKFQRDERPLFPQILAS 251
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
10-254 9.89e-25

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: 103.51  E-value: 9.89e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFG---RALLvqheSSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIV---AFkeSFEAEGHLyIVMEYCD 83
Cdd:cd14066   1 IGSGGFGtvyKGVL----ENGTVVAVKRLNEMNCAASKKEFLTELEMLGRLRHPNLVrllGY--CLESDEKL-LVYEYMP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  84 GGDLMQKIKQQKGK-LFPEDMILNWFTQMCLGVNHIH---KKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLL--SNPMA 157
Cdd:cd14066  74 NGSLEDRLHCHKGSpPLPWPQRLKIAKGIARGLEYLHeecPPPIIHGDIKSSNILLDEDFEPKLTDFGLARLIppSESVS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 158 FACTYVGTPYYVPPE-IWENLPyNNKSDIWSLGCILYELCTLKHPFQ---------------ANSWKNLILKVCQGCISP 221
Cdd:cd14066 154 KTSAVKGTIGYLAPEyIRTGRV-STKSDVYSFGVVLLELLTGKPAVDenrenasrkdlvewvESKGKEELEDILDKRLVD 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 23510391 222 LPSHYSYElqflVKQMFK-------RNPSHRPSATTLLSR 254
Cdd:cd14066 233 DDGVEEEE----VEALLRlallctrSDPSLRPSMKEVVQM 268
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
4-284 9.95e-25

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: 104.03  E-value: 9.95e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLpksfsnTQNSRKEAVL-----LAKMKHPNIVAFKESFEAEGHLYIV 78
Cdd:cd06656  21 YTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNL------QQQPKKELIIneilvMRENKNPNIVNYLDSYLVGDELWVV 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  79 MEYCDGGDLMQKIKQQkgkLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAF 158
Cdd:cd06656  95 MEYLAGGSLTDVVTET---CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSK 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 159 ACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPF-QANSWKNLILKVCQGciSPL---PSHYSYELQFLV 234
Cdd:cd06656 172 RSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYlNENPLRALYLIATNG--TPElqnPERLSAVFRDFL 249
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 23510391 235 KQMFKRNPSHRPSATTLLSRGIVaRLVQ--KCLPPEIImeygeEVLEEIKNS 284
Cdd:cd06656 250 NRCLEMDVDRRGSAKELLQHPFL-KLAKplSSLTPLII-----AAKEAIKNS 295
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
2-253 1.06e-24

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: 103.60  E-value: 1.06e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLpksfsnTQNSRKEAVLL----AKMKH---PNIVAFKESFEAEGH 74
Cdd:cd06616   6 EDLKDLGEIGRGAFGTVNKMLHKPSGTIMAVKRIRS------TVDEKEQKRLLmdldVVMRSsdcPYIVKFYGALFREGD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  75 LYIVMEYCDGG-DLMQKIKQQKGK-LFPEDMILNWFTQMCLGVNHIHKK-RVLHRDIKSKNIFLTQNGKVKLGDFGSARL 151
Cdd:cd06616  80 CWICMELMDISlDKFYKYVYEVLDsVIPEEILGKIAVATVKALNYLKEElKIIHRDVKPSNILLDRNGNIKLCDFGISGQ 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 152 LSNPMA----FACtyvgTPYYVPPEIWENL---PYNNKSDIWSLGCILYELCTLKHPFQAnsWKNLILKVCQGCISPLP- 223
Cdd:cd06616 160 LVDSIAktrdAGC----RPYMAPERIDPSAsrdGYDVRSDVWSLGITLYEVATGKFPYPK--WNSVFDQLTQVVKGDPPi 233
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 23510391 224 ------SHYSYELQFLVKQMFKRNPSHRPSATTLLS 253
Cdd:cd06616 234 lsnseeREFSPSFVNFVNLCLIKDESKRPKYKELLK 269
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
1-254 1.07e-24

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: 103.58  E-value: 1.07e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   1 MDDYMVLRMIGEGSFGR-----ALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHL 75
Cdd:cd05032   5 REKITLIRELGQGSFGMvyeglAKGVVKGEPETRVAIKTVNENASMRERIEFLNEASVMKEFNCHHVVRLLGVVSTGQPT 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  76 YIVMEYCDGGDLMQKIKQQKgklfPED------------MILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKL 143
Cdd:cd05032  85 LVVMELMAKGDLKSYLRSRR----PEAennpglgpptlqKFIQMAAEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVKI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 144 GDFGSARLLSNpmafactyvgTPYY------------VPPEIWENLPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNL 210
Cdd:cd05032 161 GDFGMTRDIYE----------TDYYrkggkgllpvrwMAPESLKDGVFTTKSDVWSFGVVLWEMATLaEQPYQGLSNEEV 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 23510391 211 ILKVCQGCISPLPSHYSYELQFLVKQMFKRNPSHRPSATTLLSR 254
Cdd:cd05032 231 LKFVIDGGHLDLPENCPDKLLELMRMCWQYNPKMRPTFLEIVSS 274
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
4-247 1.17e-24

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: 102.98  E-value: 1.17e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIrlPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCD 83
Cdd:cd14111   5 YTFLDEKARGRFGVIRRCRENATGKNFPAKIV--PYQAEEKQGVLQEYEILKSLHHERIMALHEAYITPRYLVLIAEFCS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  84 GGDLMQKIKQQKgkLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLsNPMAF--ACT 161
Cdd:cd14111  83 GKELLHSLIDRF--RYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSAQSF-NPLSLrqLGR 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 162 YVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISP--LPSHYSYELQFLVKQMFK 239
Cdd:cd14111 160 RTGTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKILVAKFDAfkLYPNVSQSASLFLKKVLS 239

                ....*...
gi 23510391 240 RNPSHRPS 247
Cdd:cd14111 240 SYPWSRPT 247
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
4-197 1.22e-24

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: 104.57  E-value: 1.22e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIR-LPKSfsnTQNSRKEAVLLAKMKH------PNIVAFKESFEAEGHLY 76
Cdd:cd14134  14 YKILRLLGEGTFGKVLECWDRKRKRYVAVKIIRnVEKY---REAAKIEIDVLETLAEkdpngkSHCVQLRDWFDYRGHMC 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEYCdGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLT-------------------Q 137
Cdd:cd14134  91 IVFELL-GPSLYDFLKKNNYGPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLVdsdyvkvynpkkkrqirvpK 169
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23510391 138 NGKVKLGDFGSArllsnpmafacTY--------VGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCT 197
Cdd:cd14134 170 STDIKLIDFGSA-----------TFddeyhssiVSTRHYRAPEVILGLGWSYPCDVWSIGCILVELYT 226
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
45-253 1.26e-24

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: 102.44  E-value: 1.26e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  45 QNSRKEAVLLAKMKHPNIV---AFKES---FEAEGHLYIVMEYCDGGDLmQKIKQQKGKLfPEDMILNWFTQMCLGVNHI 118
Cdd:cd14012  43 QLLEKELESLKKLRHPNLVsylAFSIErrgRSDGWKVYLLTEYAPGGSL-SELLDSVGSV-PLDTARRWTLQLLEALEYL 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 119 HKKRVLHRDIKSKNIFL---TQNGKVKLGDFG-SARLLSNPMAFACTYVGTPYYVPPE-IWENLPYNNKSDIWSLGCILY 193
Cdd:cd14012 121 HRNGVVHKSLHAGNVLLdrdAGTGIVKLTDYSlGKTLLDMCSRGSLDEFKQTYWLPPElAQGSKSPTRKTDVWDLGLLFL 200
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 194 ELCTLKHPFQANSWKNLILkvcqgcispLPSHYSYELQFLVKQMFKRNPSHRPSATTLLS 253
Cdd:cd14012 201 QMLFGLDVLEKYTSPNPVL---------VSLDLSASLQDFLSKCLSLDPKKRPTALELLP 251
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
31-201 1.28e-24

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: 103.63  E-value: 1.28e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  31 AMKEI--RLPKSFSNTQNSR--KEAVLLAKMKHPNIVAFKESFEAE-GHLYIVMEYCdGGDLMQKIKQQKGKL---FPED 102
Cdd:cd14001  32 AVKKInsKCDKGQRSLYQERlkEEAKILKSLNHPNIVGFRAFTKSEdGSLCLAMEYG-GKSLNDLIEERYEAGlgpFPAA 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 103 MILNWFTQMCLGVNHIH-KKRVLHRDIKSKNIFLTQNGK-VKLGDFGSA-------RLLSNPMAfacTYVGTPYYVPPEI 173
Cdd:cd14001 111 TILKVALSIARALEYLHnEKKILHGDIKSGNVLIKGDFEsVKLCDFGVSlpltenlEVDSDPKA---QYVGTEPWKAKEA 187
                       170       180
                ....*....|....*....|....*....
gi 23510391 174 W-ENLPYNNKSDIWSLGCILYELCTLKHP 201
Cdd:cd14001 188 LeEGGVITDKADIFAYGLVLWEMMTLSVP 216
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
9-202 1.35e-24

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: 102.73  E-value: 1.35e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   9 MIGEGSFGRALLVQHESSNQMFAMKEIRLpKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDLM 88
Cdd:cd14192  11 VLGGGRFGQVHKCTELSTGLTLAAKIIKV-KGAKEREEVKNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDGGELF 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  89 QKIKQQKGKLFPEDMILnwFT-QMCLGVNHIHKKRVLHRDIKSKNIF-LTQNG-KVKLGDFGSARLLsNPMAFACTYVGT 165
Cdd:cd14192  90 DRITDESYQLTELDAIL--FTrQICEGVHYLHQHYILHLDLKPENILcVNSTGnQIKIIDFGLARRY-KPREKLKVNFGT 166
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 23510391 166 PYYVPPEI--WENLPYnnKSDIWSLGCILYELCTLKHPF 202
Cdd:cd14192 167 PEFLAPEVvnYDFVSF--PTDMWSVGVITYMLLSGLSPF 203
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
2-210 1.36e-24

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: 104.36  E-value: 1.36e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd06649   5 DDFERISELGAGNGGVVTKVQHKPSGLIMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEH 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDLMQKIKQqkGKLFPEDMILNWFTQMCLGVNHIHKK-RVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAfaC 160
Cdd:cd06649  85 MDGGSLDQVLKE--AKRIPEEILGKVSIAVLRGLAYLREKhQIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMA--N 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 23510391 161 TYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNL 210
Cdd:cd06649 161 SFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYPIPPPDAKEL 210
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
4-223 1.61e-24

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: 104.36  E-value: 1.61e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLP-KSFSNTQNSRKEAVLLAKMKHPNIVAFKESF------EAEGHLY 76
Cdd:cd07878  17 YQNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLSRPfQSLIHARRTYRELRLLKHMKHENVIGLLDVFtpatsiENFNEVY 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEYCdGGDLMQKIKQQKgklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPM 156
Cdd:cd07878  97 LVTNLM-GADLNNIVKCQK---LSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLARQADDEM 172
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23510391 157 AfacTYVGTPYYVPPEIWEN-LPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLP 223
Cdd:cd07878 173 T---GYVATRWYRAPEIMLNwMHYNQTVDIWSVGCIMAELLKGKALFPGNDYIDQLKRIMEVVGTPSP 237
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
8-245 1.79e-24

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: 102.82  E-value: 1.79e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFGRALLVQHESSNQMFAMKEI---RLPKsfsntqnsRK-------EAVLLAKMKHPNIVAFKESFEAEGHLYI 77
Cdd:cd05605   6 RVLGKGGFGEVCACQVRATGKMYACKKLekkRIKK--------RKgeamalnEKQILEKVNSRFVVSLAYAYETKDALCL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  78 VMEYCDGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSA-RLLSNPM 156
Cdd:cd05605  78 VLTIMNGGDLKFHIYNMGNPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAvEIPEGET 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 157 AFActYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQAN----SWKNLILKVCQGCIsPLPSHYSYELQF 232
Cdd:cd05605 158 IRG--RVGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARkekvKREEVDRRVKEDQE-EYSEKFSEEAKS 234
                       250
                ....*....|...
gi 23510391 233 LVKQMFKRNPSHR 245
Cdd:cd05605 235 ICSQLLQKDPKTR 247
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
4-217 2.24e-24

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: 102.88  E-value: 2.24e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLpksfsnTQNSRKEAVL-----LAKMKHPNIVAFKESFEAEGHLYIV 78
Cdd:cd06654  22 YTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNL------QQQPKKELIIneilvMRENKNPNIVNYLDSYLVGDELWVV 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  79 MEYCDGGDLMQKIKQQkgkLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAF 158
Cdd:cd06654  96 MEYLAGGSLTDVVTET---CMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSK 172
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 159 ACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPF-QANSWKNLILKVCQG 217
Cdd:cd06654 173 RSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYlNENPLRALYLIATNG 232
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
4-245 2.43e-24

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: 102.72  E-value: 2.43e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEI-----------------RLPKSFSNTQNSR--------KEAVLLAKMK 58
Cdd:cd14200   2 YKLQSEIGKGSYGVVKLAYNESDDKYYAMKVLskkkllkqygfprrpppRGSKAAQGEQAKPlaplervyQEIAILKKLD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  59 HPNIVAFKESFE--AEGHLYIVMEYCDGGDLMQKIKQQKgklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLT 136
Cdd:cd14200  82 HVNIVKLIEVLDdpAEDNLYMVFDLLRKGPVMEVPSDKP---FSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 137 QNGKVKLGDFGSARLLSNPMAFACTYVGTPYYVPPEIWEN--LPYNNKS-DIWSLGCILYELCTLKHPFQANSWKNLILK 213
Cdd:cd14200 159 DDGHVKIADFGVSNQFEGNDALLSSTAGTPAFMAPETLSDsgQSFSGKAlDVWAMGVTLYCFVYGKCPFIDEFILALHNK 238
                       250       260       270
                ....*....|....*....|....*....|...
gi 23510391 214 VCQGCIS-PLPSHYSYELQFLVKQMFKRNPSHR 245
Cdd:cd14200 239 IKNKPVEfPEEPEISEELKDLILKMLDKNPETR 271
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
4-216 2.75e-24

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: 102.25  E-value: 2.75e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSfsNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCD 83
Cdd:cd14104   2 YMIAEELGRGQFGIVHRCVETSSKKTYMAKFVKVKGA--DQVLVKKEISILNIARHRNILRLHESFESHEELVMIFEFIS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  84 GGDLMQKIKQQKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNI-FLTQNGK-VKLGDFGSARLLSNPMAFACT 161
Cdd:cd14104  80 GVDIFERITTARFEL-NEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIiYCTRRGSyIKIIEFGQSRQLKPGDKFRLQ 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 23510391 162 YVgTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQ 216
Cdd:cd14104 159 YT-SAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRN 212
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
8-252 2.79e-24

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: 101.94  E-value: 2.79e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSfsnTQNSRKE-----AVLLAKMKHPNIVAFKESFEAEGHLYIVMEYC 82
Cdd:cd14197  15 RELGRGKFAVVRKCVEKDSGKEFAAKFMRKRRK---GQDCRMEiiheiAVLELAQANPWVINLHEVYETASEMILVLEYA 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  83 DGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQN---GKVKLGDFGSARLLSNPMAFA 159
Cdd:cd14197  92 AGGEIFNQCVADREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSEsplGDIKIVDFGLSRILKNSEELR 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 160 cTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCIsplpSHYSYELQFL------ 233
Cdd:cd14197 172 -EIMGTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQMNV----SYSEEEFEHLsesaid 246
                       250       260
                ....*....|....*....|
gi 23510391 234 -VKQMFKRNPSHRPSATTLL 252
Cdd:cd14197 247 fIKTLLIKKPENRATAEDCL 266
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
10-251 2.92e-24

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


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 102.20  E-value: 2.92e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKEirLPKSFSNTQ-NSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDLM 88
Cdd:cd14154   1 LGKGFFGQAIKVTHRETGEVMVMKE--LIRFDEEAQrNFLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGGTLK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  89 QKIKQqKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARL-----LSNPMAFAC--- 160
Cdd:cd14154  79 DVLKD-MARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLARLiveerLPSGNMSPSetl 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 161 ------------TYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELC----------TLKHPFQANSwKNLILKVCQGC 218
Cdd:cd14154 158 rhlkspdrkkryTVVGNPYWMAPEMLNGRSYDEKVDIFSFGIVLCEIIgrveadpdylPRTKDFGLNV-DSFREKFCAGC 236
                       250       260       270
                ....*....|....*....|....*....|...
gi 23510391 219 ISPLpshysYELQFLVKQMfkrNPSHRPSATTL 251
Cdd:cd14154 237 PPPF-----FKLAFLCCDL---DPEKRPPFETL 261
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
4-195 3.22e-24

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: 103.26  E-value: 3.22e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPksFSNTQNSRK---EAVLLAKMKHPNIV----AF--KESFEAEGH 74
Cdd:cd07850   2 YQNLKPIGSGAQGIVCAAYDTVTGQNVAIKKLSRP--FQNVTHAKRayrELVLMKLVNHKNIIgllnVFtpQKSLEEFQD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  75 LYIVMEYCDGgDLMQKIKQqkgkLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSN 154
Cdd:cd07850  80 VYLVMELMDA-NLCQVIQM----DLDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGT 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 23510391 155 pmAFACT-YVGTPYYVPPEIWENLPYNNKSDIWSLGCILYEL 195
Cdd:cd07850 155 --SFMMTpYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEM 194
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
2-202 3.34e-24

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: 103.97  E-value: 3.34e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQ--NSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVM 79
Cdd:cd05628   1 EDFESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQvgHIRAERDILVEADSLWVVKMFYSFQDKLNLYLIM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  80 EYCDGGDLMQKIkqQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLS------ 153
Cdd:cd05628  81 EFLPGGDMMTLL--MKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCTGLKkahrte 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23510391 154 -----------------------------NPMAFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPF 202
Cdd:cd05628 159 fyrnlnhslpsdftfqnmnskrkaetwkrNRRQLAFSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPF 236
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
2-253 3.56e-24

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: 101.60  E-value: 3.56e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVL-RMIGEGSFGRALLVQHESSNQMFAMKEIrlpksFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGH----LY 76
Cdd:cd14172   3 DDYKLSkQVLGLGVNGKVLECFHRRTGQKCALKLL-----YDSPKARREVEHHWRASGGPHIVHILDVYENMHHgkrcLL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEYCDGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLT---QNGKVKLGDFGSAR--L 151
Cdd:cd14172  78 IIMECMEGGELFSRIQERGDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTskeKDAVLKLTDFGFAKetT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 152 LSNPMAFACTyvgTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANS-------WKNLILKVCQGCISPLPS 224
Cdd:cd14172 158 VQNALQTPCY---TPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTgqaispgMKRRIRMGQYGFPNPEWA 234
                       250       260
                ....*....|....*....|....*....
gi 23510391 225 HYSYELQFLVKQMFKRNPSHRPSATTLLS 253
Cdd:cd14172 235 EVSEEAKQLIRHLLKTDPTERMTITQFMN 263
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
10-202 3.91e-24

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


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 101.15  E-value: 3.91e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFG---RALlvqHESSNQMFAMKEIRLpKSFSNTQNSR--KEAVLLAKMKHPNIVAFKESFEAEGHLYIVM--EYC 82
Cdd:cd13983   9 LGRGSFKtvyRAF---DTEEGIEVAWNEIKL-RKLPKAERQRfkQEIEILKSLKHPNIIKFYDSWESKSKKEVIFitELM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  83 DGGDLMQKIKqqKGKLFPEDMILNWFTQMCLGVNHIHKKR--VLHRDIKSKNIFLTQN-GKVKLGDFGSARLLSnpMAFA 159
Cdd:cd13983  85 TSGTLKQYLK--RFKRLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFINGNtGEVKIGDLGLATLLR--QSFA 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 23510391 160 CTYVGTPYYVPPEIWENlPYNNKSDIWSLGCILYELCTLKHPF 202
Cdd:cd13983 161 KSVIGTPEFMAPEMYEE-HYDEKVDIYAFGMCLLEMATGEYPY 202
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
7-252 5.53e-24

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: 101.51  E-value: 5.53e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   7 LRMIGEGSFGRALLVQHESSN----QMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGH--LYIVME 80
Cdd:cd05080   9 IRDLGEGHFGKVSLYCYDPTNdgtgEMVAVKALKADCGPQHRSGWKQEIDILKTLYHENIVKYKGCCSEQGGksLQLIME 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  81 YCDGGDLMQKIKQQKGKLfpeDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNpmafac 160
Cdd:cd05080  89 YVPLGSLRDYLPKHSIGL---AQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAKAVPE------ 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 161 tyvGTPYY------------VPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNL-ILKVCQGCIS------- 220
Cdd:cd05080 160 ---GHEYYrvredgdspvfwYAPECLKEYKFYYASDVWSFGVTLYELLTHCDSSQSPPTKFLeMIGIAQGQMTvvrliel 236
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 23510391 221 -------PLPSHYSYELQFLVKQMFKRNPSHRPSATTLL 252
Cdd:cd05080 237 lergerlPCPDKCPQEVYHLMKNCWETEASFRPTFENLI 275
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
3-253 6.19e-24

Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Wee1 is a nuclear cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. There are two distinct Wee1 proteins in vertebrates showing different expression patterns, called Wee1a and Wee1b. They are functionally dstinct and are implicated in different steps of egg maturation and embryo development. The Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270953 [Multi-domain]  Cd Length: 275  Bit Score: 101.33  E-value: 6.19e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFS-NTQNSRKE----AVLlakMKHPNIVAFKESFEAEGHLYI 77
Cdd:cd14051   1 EFHEVEKIGSGEFGSVYKCINRLDGCVYAIKKSKKPVAGSvDEQNALNEvyahAVL---GKHPHVVRYYSAWAEDDHMII 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  78 VMEYCDGGDLMQKIK--QQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKV-------------- 141
Cdd:cd14051  78 QNEYCNGGSLADAISenEKAGERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFISRTPNPvsseeeeedfegee 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 142 ----------KLGDFGSARLLSNPmafactYV--GTPYYVPPEI----WENLPynnKSDIWSLGCILYELC---TLkhPF 202
Cdd:cd14051 158 dnpesnevtyKIGDLGHVTSISNP------QVeeGDCRFLANEIlqenYSHLP---KADIFALALTVYEAAgggPL--PK 226
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 23510391 203 QANSWKNLIlkvcQGCISPLPsHYSYELQFLVKQMFKRNPSHRPSATTLLS 253
Cdd:cd14051 227 NGDEWHEIR----QGNLPPLP-QCSPEFNELLRSMIHPDPEKRPSAAALLQ 272
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
3-252 7.81e-24

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: 101.11  E-value: 7.81e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYC 82
Cdd:cd06619   2 DIQYQEILGHGNGGTVYKAYHLLTRRILAVKVIPLDITVELQKQIMSELEILYKCDSPYIIGFYGAFFVENRISICTEFM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  83 DGG--DLMQKIkqqkgklfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNpmAFAC 160
Cdd:cd06619  82 DGGslDVYRKI--------PEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLVN--SIAK 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 161 TYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHP---FQANSWKNLILKVCQgCI----SP-LPSH-YSYELQ 231
Cdd:cd06619 152 TYVGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGRFPypqIQKNQGSLMPLQLLQ-CIvdedPPvLPVGqFSEKFV 230
                       250       260
                ....*....|....*....|.
gi 23510391 232 FLVKQMFKRNPSHRPSATTLL 252
Cdd:cd06619 231 HFITQCMRKQPKERPAPENLM 251
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
2-252 1.03e-23

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: 102.02  E-value: 1.03e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSfsntQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd14176  19 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKR----DPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTEL 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDLMQKIKQQKgkLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNI-FLTQNGK---VKLGDFGSARLLSNPMA 157
Cdd:cd14176  95 MKGGELLDKILRQK--FFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNIlYVDESGNpesIRICDFGFAKQLRAENG 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 158 FACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQ---ANSWKNLILKVCQGCISPLPSHY---SYELQ 231
Cdd:cd14176 173 LLMTPCYTANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSLSGGYWnsvSDTAK 252
                       250       260
                ....*....|....*....|.
gi 23510391 232 FLVKQMFKRNPSHRPSATTLL 252
Cdd:cd14176 253 DLVSKMLHVDPHQRLTAALVL 273
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
9-202 1.76e-23

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: 99.61  E-value: 1.76e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   9 MIGEGSFGRALLVQHESSNQMFAMKEIrlpksfsNTQNSR-KEAVLLA-----KMKHPNIVAFKESFEAEGHLYIVMEYC 82
Cdd:cd14190  11 VLGGGKFGKVHTCTEKRTGLKLAAKVI-------NKQNSKdKEMVLLEiqvmnQLNHRNLIQLYEAIETPNEIVLFMEYV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  83 DGGDLMQKIKQQKGKLFPEDMILnWFTQMCLGVNHIHKKRVLHRDIKSKNIFL--TQNGKVKLGDFGSARLLsNPMAFAC 160
Cdd:cd14190  84 EGGELFERIVDEDYHLTEVDAMV-FVRQICEGIQFMHQMRVLHLDLKPENILCvnRTGHQVKIIDFGLARRY-NPREKLK 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 23510391 161 TYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPF 202
Cdd:cd14190 162 VNFGTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPF 203
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
7-252 1.92e-23

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: 99.89  E-value: 1.92e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   7 LRMIGEGSFGRALLVQHESSNQMFAMKEIRLPK-SFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGH--LYIVMEYC- 82
Cdd:cd14049  11 IARLGKGGYGKVYKVRNKLDGQYYAIKKILIKKvTKRDCMKVLREVKVLAGLQHPNIVGYHTAWMEHVQlmLYIQMQLCe 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  83 -------DGGDLMQKIKQQKGKLFP---EDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLT-QNGKVKLGDFGSA-- 149
Cdd:cd14049  91 lslwdwiVERNKRPCEEEFKSAPYTpvdVDVTTKILQQLLEGVTYIHSMGIVHRDLKPRNIFLHgSDIHVRIGDFGLAcp 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 150 RLLSNPMAFACTY----------VGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCtlkHPFQANSWK-NLILKVCQGC 218
Cdd:cd14049 171 DILQDGNDSTTMSrlnglthtsgVGTCLYAAPEQLEGSHYDFKSDMYSIGVILLELF---QPFGTEMERaEVLTQLRNGQ 247
                       250       260       270
                ....*....|....*....|....*....|....
gi 23510391 219 ISPLPSHYSYELQFLVKQMFKRNPSHRPSATTLL 252
Cdd:cd14049 248 IPKSLCKRWPVQAKYIKLLTSTEPSERPSASQLL 281
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
2-202 2.13e-23

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: 100.09  E-value: 2.13e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIrlpkSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd14178   3 DGYEIKEDIGIGSYSVCKRCVHKATSTEYAVKII----DKSKRDPSEEIEILLRYGQHPNIITLKDVYDDGKFVYLVMEL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDLMQKIKQQkgKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNI-FLTQNG---KVKLGDFGSARLLSNPMA 157
Cdd:cd14178  79 MRGGELLDRILRQ--KCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNIlYMDESGnpeSIRICDFGFAKQLRAENG 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 23510391 158 FACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPF 202
Cdd:cd14178 157 LLMTPCYTANFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPF 201
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
2-273 2.22e-23

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: 99.90  E-value: 2.22e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIrlpKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd14085   3 DFFEIESELGRGATSVVYRCRQKGTQKPYAVKKL---KKTVDKKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLEL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDLMQKIkQQKGkLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGK---VKLGDFGSARLLSNPMAF 158
Cdd:cd14085  80 VTGGELFDRI-VEKG-YYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPdapLKIADFGLSKIVDQQVTM 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 159 AcTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGC----ISPLPSHYSYELQFLV 234
Cdd:cd14085 158 K-TVCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYDERGDQYMFKRILNCdydfVSPWWDDVSLNAKDLV 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 23510391 235 KQMFKRNPSHRPSATTLLS----RGIVARLVQKCLPPEIIMEY 273
Cdd:cd14085 237 KKLIVLDPKKRLTTQQALQhpwvTGKAANFAHMDTAQKKLQEF 279
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
2-245 2.41e-23

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: 100.43  E-value: 2.41e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMK--EIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVM 79
Cdd:cd05632   2 NTFRQYRVLGKGGFGEVCACQVRATGKMYACKrlEKKRIKKRKGESMALNEKQILEKVNSQFVVNLAYAYETKDALCLVL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  80 EYCDGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFA 159
Cdd:cd05632  82 TIMNGGDLKFHIYNMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKIPEGESIR 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 160 cTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWK---NLILKVCQGCISPLPSHYSYELQFLVKQ 236
Cdd:cd05632 162 -GRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEKvkrEEVDRRVLETEEVYSAKFSEEAKSICKM 240

                ....*....
gi 23510391 237 MFKRNPSHR 245
Cdd:cd05632 241 LLTKDPKQR 249
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
4-251 3.27e-23

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: 99.32  E-value: 3.27e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFG---RAL-LVQHESSnqmfAMKEIRLPKSFSN--TQNSRKEAV----LLAKMKHPNIVAFKESFEAEG 73
Cdd:cd13990   2 YLLLNLLGKGGFSevyKAFdLVEQRYV----ACKIHQLNKDWSEekKQNYIKHALreyeIHKSLDHPRIVKLYDVFEIDT 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  74 HLYI-VMEYCDGGDLMQKIKQQKgkLFPEDMILNWFTQMCLGVNHI--HKKRVLHRDIKSKNIFLTQN---GKVKLGDFG 147
Cdd:cd13990  78 DSFCtVLEYCDGNDLDFYLKQHK--SIPEREARSIIMQVVSALKYLneIKPPIIHYDLKPGNILLHSGnvsGEIKITDFG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 148 SARLL------SNPMAFACTYVGTPYYVPPEIWENLP----YNNKSDIWSLGCILYELCTLKHPF------QANSWKNLI 211
Cdd:cd13990 156 LSKIMddesynSDGMELTSQGAGTYWYLPPECFVVGKtppkISSKVDVWSVGVIFYQMLYGRKPFghnqsqEAILEENTI 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 23510391 212 LKVCQGCISPLPsHYSYELQFLVKQMFKRNPSHRPSATTL 251
Cdd:cd13990 236 LKATEVEFPSKP-VVSSEAKDFIRRCLTYRKEDRPDVLQL 274
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
12-253 3.39e-23

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: 98.88  E-value: 3.39e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  12 EGSF-GRA-----LLVQHESsnqmFAMKEIRLpksfsntqnsrkeavLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGG 85
Cdd:cd13982  20 RGTFdGRPvavkrLLPEFFD----FADREVQL---------------LRESDEHPNVIRYFCTEKDRQFLYIALELCAAS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  86 --DLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQ-----NGKVKLGDFG-SARLLSNPMA 157
Cdd:cd13982  81 lqDLVESPRESKLFLRPGLEPVRLLRQIASGLAHLHSLNIVHRDLKPQNILISTpnahgNVRAMISDFGlCKKLDVGRSS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 158 FACTY--VGTPYYVPPEIWENLPYNNKS---DIWSLGCILYELCTL-KHPF------QANSWKNlilKVCQGCISPLPSH 225
Cdd:cd13982 161 FSRRSgvAGTSGWIAPEMLSGSTKRRQTravDIFSLGCVFYYVLSGgSHPFgdklerEANILKG---KYSLDKLLSLGEH 237
                       250       260
                ....*....|....*....|....*...
gi 23510391 226 ySYELQFLVKQMFKRNPSHRPSATTLLS 253
Cdd:cd13982 238 -GPEAQDLIERMIDFDPEKRPSAEEVLN 264
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
9-202 3.41e-23

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: 98.83  E-value: 3.41e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   9 MIGEGSFGRALLVQHESSNQMFAMKEIRLpKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDLM 88
Cdd:cd14193  11 ILGGGRFGQVHKCEEKSSGLKLAAKIIKA-RSQKEKEEVKNEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYVDGGELF 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  89 QKIKQQKGKLFPEDMILnWFTQMCLGVNHIHKKRVLHRDIKSKNIFLT--QNGKVKLGDFGSARLLsNPMAFACTYVGTP 166
Cdd:cd14193  90 DRIIDENYNLTELDTIL-FIKQICEGIQYMHQMYILHLDLKPENILCVsrEANQVKIIDFGLARRY-KPREKLRVNFGTP 167
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 23510391 167 YYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPF 202
Cdd:cd14193 168 EFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPF 203
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
2-266 6.52e-23

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: 98.56  E-value: 6.52e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRallVQHESSNQMFAMKEIRL----PKSFsntQNSRKEAVLLAKMKHPNIVAFKeSFEAEGHLYI 77
Cdd:cd14149  12 SEVMLSTRIGSGSFGT---VYKGKWHGDVAVKILKVvdptPEQF---QAFRNEVAVLRKTRHVNILLFM-GYMTKDNLAI 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  78 VMEYCDGGDLMQKIKQQKGKlFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLS--NP 155
Cdd:cd14149  85 VTQWCEGSSLYKHLHVQETK-FQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSrwSG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 156 MAFACTYVGTPYYVPPEI---WENLPYNNKSDIWSLGCILYELCTLKHPF-QANSWKNLILKVCQGCISP----LPSHYS 227
Cdd:cd14149 164 SQQVEQPTGSILWMAPEVirmQDNNPFSFQSDVYSYGIVLYELMTGELPYsHINNRDQIIFMVGRGYASPdlskLYKNCP 243
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 23510391 228 YELQFLVKQMFKRNPSHRPSATTLLSRgivARLVQKCLP 266
Cdd:cd14149 244 KAMKRLVADCIKKVKEERPLFPQILSS---IELLQHSLP 279
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
10-248 7.93e-23

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: 97.84  E-value: 7.93e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRalLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAF-----KESFEAEGhlYIVMEYCDG 84
Cdd:cd13979  11 LGSGGFGS--VYKATYKGETVAVKIVRRRRKNRASRQSFWAELNAARLRHENIVRVlaaetGTDFASLG--LIIMEYCGN 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  85 GDLMQKIKQQKGKLFPEDMILnWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAF---ACT 161
Cdd:cd13979  87 GTLQQLIYEGSEPLPLAHRIL-ISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSVKLGEGNEVgtpRSH 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 162 YVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFqANSWKNLILKVCQGCISPLPSHYSYE-----LQFLVKQ 236
Cdd:cd13979 166 IGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPY-AGLRQHVLYAVVAKDLRPDLSGLEDSefgqrLRSLISR 244
                       250
                ....*....|..
gi 23510391 237 MFKRNPSHRPSA 248
Cdd:cd13979 245 CWSAQPAERPNA 256
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
4-214 9.09e-23

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: 100.09  E-value: 9.09e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQ--NSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd05626   3 FVKIKTLGIGAFGEVCLACKVDTHALYAMKTLRKKDVLNRNQvaHVKAERDILAEADNEWVVKLYYSFQDKDNLYFVMDY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDLMQKIKQQKgkLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFG-------------- 147
Cdd:cd05626  83 IPGGDMMSLLIRME--VFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGlctgfrwthnskyy 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 148 -------------------------SARLLS--------NPMAFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYE 194
Cdd:cd05626 161 qkgshirqdsmepsdlwddvsncrcGDRLKTleqratkqHQRCLAHSLVGTPNYIAPEVLLRKGYTQLCDWWSVGVILFE 240
                       250       260
                ....*....|....*....|
gi 23510391 195 LCTLKHPFQANSWKNLILKV 214
Cdd:cd05626 241 MLVGQPPFLAPTPTETQLKV 260
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
4-214 1.02e-22

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: 99.21  E-value: 1.02e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLP-KSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHL------Y 76
Cdd:cd07879  17 YTSLKQVGSGAYGSVCSAIDKRTGEKVAIKKLSRPfQSEIFAKRAYRELTLLKHMQHENVIGLLDVFTSAVSGdefqdfY 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEYCDGgDLmQKIKqqkGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPM 156
Cdd:cd07879  97 LVMPYMQT-DL-QKIM---GHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGLARHADAEM 171
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23510391 157 AfacTYVGTPYYVPPEIWEN-LPYNNKSDIWSLGCILYELCTLKHPFQANSWKN---LILKV 214
Cdd:cd07879 172 T---GYVVTRWYRAPEVILNwMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDqltQILKV 230
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
1-215 1.07e-22

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: 98.54  E-value: 1.07e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   1 MDDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKS---FSNTqnSRKEAVLLAKMKHPNIVAF--------KESF 69
Cdd:cd07866   7 LRDYEILGKLGEGTFGEVYKARQIKTGRVVALKKILMHNEkdgFPIT--ALREIKILKKLKHPNVVPLidmaverpDKSK 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  70 EAEGHLYIVMEYCDGgDLMQKIKQQKGKLFPEDmILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSA 149
Cdd:cd07866  85 RKRGSVYMVTPYMDH-DLSGLLENPSVKLTESQ-IKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADFGLA 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 150 RLL--------SNPMAFACTYVG---TPYYVPPEI---WENlpYNNKSDIWSLGCILYELCTLKHPFQANSWKN---LIL 212
Cdd:cd07866 163 RPYdgpppnpkGGGGGGTRKYTNlvvTRWYRPPELllgERR--YTTAVDIWGIGCVFAEMFTRRPILQGKSDIDqlhLIF 240

                ...
gi 23510391 213 KVC 215
Cdd:cd07866 241 KLC 243
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
4-206 1.10e-22

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: 99.74  E-value: 1.10e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQ--NSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd05625   3 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQvaHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDLMQKIKQQKgkLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFG-------------- 147
Cdd:cd05625  83 IPGGDMMSLLIRMG--VFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGlctgfrwthdskyy 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 148 --SARLLSNPMAF-------------------------------ACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYE 194
Cdd:cd05625 161 qsGDHLRQDSMDFsnewgdpencrcgdrlkplerraarqhqrclAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFE 240
                       250
                ....*....|..
gi 23510391 195 LCTLKHPFQANS 206
Cdd:cd05625 241 MLVGQPPFLAQT 252
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
2-206 1.12e-22

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: 1.12e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAV-----LLAKMKHPNIVAFKESFEAEGHLY 76
Cdd:cd14105   5 DFYDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKASRRGVSREDIerevsILRQVLHPNIITLHDVFENKTDVV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEYCDGGDLMQKIKQQKGklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQ----NGKVKLGDFGSARLL 152
Cdd:cd14105  85 LILELVAGGELFDFLAEKES--LSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDknvpIPRIKLIDFGLAHKI 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 23510391 153 SNPMAFACTYvGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANS 206
Cdd:cd14105 163 EDGNEFKNIF-GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDT 215
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
10-254 1.13e-22

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: 97.25  E-value: 1.13e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALlvQHESSNQMFAMKEIrlpKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGhLYIVMEYCDGGDLMQ 89
Cdd:cd05083  14 IGEGEFGAVL--QGEYMGQKVAVKNI---KCDVTAQAFLEETAVMTKLQHKNLVRLLGVILHNG-LYIVMELMSKGNLVN 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  90 KIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLlsNPMAFACTYVGTPyYV 169
Cdd:cd05083  88 FLRSRGRALVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAKV--GSMGVDNSRLPVK-WT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 170 PPEIWENLPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQMFKRNPSHRPSA 248
Cdd:cd05083 165 APEALKNKKFSSKSDVWSYGVLLWEVFSYgRAPYPKMSVKEVKEAVEKGYRMEPPEGCPPDVYSIMTSCWEAEPGKRPSF 244

                ....*.
gi 23510391 249 TTLLSR 254
Cdd:cd05083 245 KKLREK 250
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
10-263 1.44e-22

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: 97.20  E-value: 1.44e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKEIRLpKSFSNtqnsrKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDLMQ 89
Cdd:cd13991  14 IGRGSFGEVHRMEDKQTGFQCAVKKVRL-EVFRA-----EELMACAGLTSPRVVPLYGAVREGPWVNIFMDLKEGGSLGQ 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  90 KIKQQkGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGK-VKLGDFGSARLLSNP----MAFACTYV- 163
Cdd:cd13991  88 LIKEQ-GCL-PEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGSdAFLCDFGHAECLDPDglgkSLFTGDYIp 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 164 GTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQG--CISPLPSHYSYELQFLVKQMFKRN 241
Cdd:cd13991 166 GTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPWTQYYSGPLCLKIANEppPLREIPPSCAPLTAQAIQAGLRKE 245
                       250       260
                ....*....|....*....|..
gi 23510391 242 PSHRPSATTLlsRGIVARLVQK 263
Cdd:cd13991 246 PVHRASAAEL--RRKTNRALQE 265
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
7-252 1.66e-22

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: 96.85  E-value: 1.66e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   7 LRMIGEGSFGRALLVQHESSNQMfAMKEIRlpKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGD 86
Cdd:cd05114   9 MKELGSGLFGVVRLGKWRAQYKV-AIKAIR--EGAMSEEDFIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFMENGC 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  87 LMQKIKQQKGKLFPeDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSAR-LLSNPMAFACTYVGT 165
Cdd:cd05114  86 LLNYLRQRRGKLSR-DMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRyVLDDQYTSSSGAKFP 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 166 PYYVPPEIWENLPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQG--CISP-LPSHYSYELQFlvkQMFKRN 241
Cdd:cd05114 165 VKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTEgKMPFESKSNYEVVEMVSRGhrLYRPkLASKSVYEVMY---SCWHEK 241
                       250
                ....*....|.
gi 23510391 242 PSHRPSATTLL 252
Cdd:cd05114 242 PEGRPTFADLL 252
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
4-225 1.81e-22

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: 98.09  E-value: 1.81e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFsnTQNSRKEAVLLAKM--------KHpNIVAFKESFEAEGHL 75
Cdd:cd14212   1 YLVLDLLGQGTFGQVVKCQDLKTNKLVAVKVLKNKPAY--FRQAMLEIAILTLLntkydpedKH-HIVRLLDHFMHHGHL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  76 YIVMEyCDGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQN--GKVKLGDFGSArlls 153
Cdd:cd14212  78 CIVFE-LLGVNLYELLKQNQFRGLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNLdsPEIKLIDFGSA---- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 154 npmafaC-------TYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELcTLKHP-FQANSWKNLILKVCQgCISPLPSH 225
Cdd:cd14212 153 ------CfenytlyTYIQSRFYRSPEVLLGLPYSTAIDMWSLGCIAAEL-FLGLPlFPGNSEYNQLSRIIE-MLGMPPDW 224
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
2-294 2.47e-22

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: 97.41  E-value: 2.47e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVL-RMIGEGSFGRALLVQHESSNQMFAMKEIR-LPKSfsntqnsRKEAVLLAKMKH-PNIV----AFKESFEAEGH 74
Cdd:cd14170   1 DDYKVTsQVLGLGINGKVLQIFNKRTQEKFALKMLQdCPKA-------RREVELHWRASQcPHIVrivdVYENLYAGRKC 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  75 LYIVMEYCDGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQ---NGKVKLGDFGSARL 151
Cdd:cd14170  74 LLIVMECLDGGELFSRIQDRGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSkrpNAILKLTDFGFAKE 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 152 LS--NPMAFACTyvgTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQAN-------SWKNLILKVCQGCISPL 222
Cdd:cd14170 154 TTshNSLTTPCY---TPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNhglaispGMKTRIRMGQYEFPNPE 230
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23510391 223 PSHYSYELQFLVKQMFKRNPSHRPSATTLLSRGIVARLVQkcLPPEIImeYGEEVLEEIKNSKHNTPRKKTN 294
Cdd:cd14170 231 WSEVSEEVKMLIRNLLKTEPTQRMTITEFMNHPWIMQSTK--VPQTPL--HTSRVLKEDKERWEDVKEEMTS 298
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
2-202 2.65e-22

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: 96.56  E-value: 2.65e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAV-----LLAKMKHPNIVAFKESFEAEGHLY 76
Cdd:cd14196   5 DFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSREEIerevsILRQVLHPNIITLHDVYENRTDVV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEYCDGGDLMQKIKQQKGklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNG----KVKLGDFGSARLL 152
Cdd:cd14196  85 LILELVSGGELFDFLAQKES--LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEI 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 23510391 153 SNPMAFACTYvGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPF 202
Cdd:cd14196 163 EDGVEFKNIF-GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPF 211
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
3-251 2.69e-22

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


Pssm-ID: 271041 [Multi-domain]  Cd Length: 274  Bit Score: 96.54  E-value: 2.69e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLP-KSFSNTQNSRKEAVLLAKM-KHPNIVAFKESFEAEGHLYIVME 80
Cdd:cd14139   1 EFLELEKIGVGEFGSVYKCIKRLDGCVYAIKRSMRPfAGSSNEQLALHEVYAHAVLgHHPHVVRYYSAWAEDDHMIIQNE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  81 YCDGGDLMQKI--KQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKV----------------- 141
Cdd:cd14139  81 YCNGGSLQDAIseNTKSGNHFEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIFICHKMQSssgvgeevsneedefls 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 142 -----KLGDFGSARLLSNPMAFACTYVGTPYYVPPEIWENLPynnKSDIWSLG-CILYELCTLKHPFQANSWKNLIlkvc 215
Cdd:cd14139 161 anvvyKIGDLGHVTSINKPQVEEGDSRFLANEILQEDYRHLP---KADIFALGlTVALAAGAEPLPTNGAAWHHIR---- 233
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 23510391 216 QGCISPLPSHYSYELQFLVKQMFKRNPSHRPSATTL 251
Cdd:cd14139 234 KGNFPDVPQELPESFSSLLKNMIQPDPEQRPSATAL 269
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
4-202 2.77e-22

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: 97.93  E-value: 2.77e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIR-LPKSFSNTQNSRKEAVLLAKMKHPNIVAFKE-----SFEAEGHLYI 77
Cdd:cd07859   2 YKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKINdVFEHVSDATRILREIKLLRLLRHPDIVEIKHimlppSRREFKDIYV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  78 VMEYCDGgDLMQKIKQQKgKLFPEDMILNWFtQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSN--- 154
Cdd:cd07859  82 VFELMES-DLHQVIKAND-DLTPEHHQFFLY-QLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLARVAFNdtp 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 23510391 155 PMAFACTYVGTPYYVPPEIWENL--PYNNKSDIWSLGCILYELCTLKHPF 202
Cdd:cd07859 159 TAIFWTDYVATRWYRAPELCGSFfsKYTPAIDIWSIGCIFAEVLTGKPLF 208
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
2-258 2.92e-22

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: 97.01  E-value: 2.92e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIrlpkSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd14177   4 DVYELKEDIGVGSYSVCKRCIHRATNMEFAVKII----DKSKRDPSEEIEILMRYGQHPNIITLKDVYDDGRYVYLVTEL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDLMQKIKQQKgkLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNG----KVKLGDFGSARLLSNPMA 157
Cdd:cd14177  80 MKGGELLDRILRQK--FFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSanadSIRICDFGFAKQLRGENG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 158 FACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQ---ANSWKNLILKVCQGCISPLPSHY---SYELQ 231
Cdd:cd14177 158 LLLTPCYTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFAngpNDTPEEILLRIGSGKFSLSGGNWdtvSDAAK 237
                       250       260
                ....*....|....*....|....*..
gi 23510391 232 FLVKQMFKRNPSHRPSATTLLSRGIVA 258
Cdd:cd14177 238 DLLSHMLHVDPHQRYTAEQVLKHSWIA 264
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
9-245 3.76e-22

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: 95.97  E-value: 3.76e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   9 MIGEGSFGRALLVQHESSNQMFAMK-----EIRLPKSFSNTQNSRKEAVLLAKMKH-PNIVAFKESFEAEGHLYIVMEYC 82
Cdd:cd05606   1 IIGRGGFGEVYGCRKADTGKMYAMKcldkkRIKMKQGETLALNERIMLSLVSTGGDcPFIVCMTYAFQTPDKLCFILDLM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  83 DGGDLMQKIKQQKgkLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACty 162
Cdd:cd05606  81 NGGDLHYHLSQHG--VFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLACDFSKKKPHAS-- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 163 VGTPYYVPPEIW-ENLPYNNKSDIWSLGCILYELCTLKHPFQANSW--KNLILKVCQGCISPLPSHYSYELQFLVKQMFK 239
Cdd:cd05606 157 VGTHGYMAPEVLqKGVAYDSSADWFSLGCMLYKLLKGHSPFRQHKTkdKHEIDRMTLTMNVELPDSFSPELKSLLEGLLQ 236

                ....*.
gi 23510391 240 RNPSHR 245
Cdd:cd05606 237 RDVSKR 242
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
2-231 5.42e-22

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: 96.94  E-value: 5.42e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLP-KSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHL----- 75
Cdd:cd07880  15 DRYRDLKQVGSGAYGTVCSALDRRTGAKVAIKKLYRPfQSELFAKRAYRELRLLKHMKHENVIGLLDVFTPDLSLdrfhd 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  76 -YIVMEYCdGGDLMQKIKQQKgklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSN 154
Cdd:cd07880  95 fYLVMPFM-GTDLGKLMKHEK---LSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARQTDS 170
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23510391 155 PMAfacTYVGTPYYVPPEIWEN-LPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPlPSHYSYELQ 231
Cdd:cd07880 171 EMT---GYVVTRWYRAPEVILNwMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHLDQLMEIMKVTGTP-SKEFVQKLQ 244
pknD PRK13184
serine/threonine-protein kinase PknD;
1-213 5.43e-22

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 99.84  E-value: 5.43e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391    1 MDDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIR--------LPKSFsntqnsRKEAVLLAKMKHPNIVAFKeSFEAE 72
Cdd:PRK13184   1 MQRYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIRedlsenplLKKRF------LREAKIAADLIHPGIVPVY-SICSD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   73 GHL-YIVMEYCDGGDLMQKIKQ--QKGKLfPEDM--------ILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKV 141
Cdd:PRK13184  74 GDPvYYTMPYIEGYTLKSLLKSvwQKESL-SKELaektsvgaFLSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  142 KLGDFGSARL----------LSNPMAFACTY--------VGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQ 203
Cdd:PRK13184 153 VILDWGAAIFkkleeedlldIDVDERNICYSsmtipgkiVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYR 232
                        250
                 ....*....|
gi 23510391  204 ANSWKNLILK 213
Cdd:PRK13184 233 RKKGRKISYR 242
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
10-195 7.43e-22

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


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 95.02  E-value: 7.43e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKE-IRLPKSfsnTQNS-RKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDL 87
Cdd:cd14221   1 LGKGCFGQAIKVTHRETGEVMVMKElIRFDEE---TQRTfLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  88 MQKIKQQKGKlFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLL----SNPMAFA---- 159
Cdd:cd14221  78 RGIIKSMDSH-YPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLARLMvdekTQPEGLRslkk 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 23510391 160 ------CTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYEL 195
Cdd:cd14221 157 pdrkkrYTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEI 198
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
2-202 1.03e-21

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: 94.68  E-value: 1.03e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAV-----LLAKMKHPNIVAFKESFEAEGHLY 76
Cdd:cd14195   5 DHYEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSSSRRGVSREEIerevnILREIQHPNIITLHDIFENKTDVV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEYCDGGDLMQKIKQQKGklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFL----TQNGKVKLGDFGSARLL 152
Cdd:cd14195  85 LILELVSGGELFDFLAEKES--LTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLldknVPNPRIKLIDFGIAHKI 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 23510391 153 SNPMAFACTYvGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPF 202
Cdd:cd14195 163 EAGNEFKNIF-GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPF 211
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
7-251 1.23e-21

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: 94.76  E-value: 1.23e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   7 LRMIGEGSFGRALLVQHE-SSNQMFAMKEIRLPKSFSNTQNSR---KEAVLLAKMKHPNIVAFKESFEAEGH--LYIVME 80
Cdd:cd05038   9 IKQLGEGHFGSVELCRYDpLGDNTGEQVAVKSLQPSGEEQHMSdfkREIEILRTLDHEYIVKYKGVCESPGRrsLRLIME 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  81 YCDGGDLMQKIKQQKGKLFPEDMILnwFT-QMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLsnPMAFA 159
Cdd:cd05038  89 YLPSGSLRDYLQRHRDQIDLKRLLL--FAsQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAKVL--PEDKE 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 160 CTYVGTP------YYVPPEIWENLpYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCIS------------- 220
Cdd:cd05038 165 YYYVKEPgespifWYAPECLRESR-FSSASDVWSFGVTLYELFTYGDPSQSPPALFLRMIGIAQGQMivtrllellksge 243
                       250       260       270
                ....*....|....*....|....*....|...
gi 23510391 221 --PLPSHYSYELQFLVKQMFKRNPSHRPSATTL 251
Cdd:cd05038 244 rlPRPPSCPDEVYDLMKECWEYEPQDRPSFSDL 276
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
23-202 1.65e-21

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


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 93.96  E-value: 1.65e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  23 HESSNQMFAMKEIRLPKSFSNTQN-------SRKEAVLLAKM-KHPNIVAFKESFEAEGHLYIVMEYCDGGDLM----QK 90
Cdd:cd14093  24 EKETGQEFAVKIIDITGEKSSENEaeelreaTRREIEILRQVsGHPNIIELHDVFESPTFIFLVFELCRKGELFdyltEV 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  91 IKqqkgklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLsNPMAFACTYVGTPYYVP 170
Cdd:cd14093 104 VT------LSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATRL-DEGEKLRELCGTPGYLA 176
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 23510391 171 PEI-----WENLP-YNNKSDIWSLGCILYELCTLKHPF 202
Cdd:cd14093 177 PEVlkcsmYDNAPgYGKEVDMWACGVIMYTLLAGCPPF 214
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
10-203 1.88e-21

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: 94.87  E-value: 1.88e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKEIRlPKSFSNTQNSRK-EAVLLAKMKHPNIV---AFKESFEAEgHLYIVMEYCDGG 85
Cdd:cd13988   1 LGQGATANVFRGRHKKTGDLYAVKVFN-NLSFMRPLDVQMrEFEVLKKLNHKNIVklfAIEEELTTR-HKVLVMELCPCG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  86 DLMQKIKQQKGKL-FPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNI--FLTQNGKV--KLGDFGSARLLSNPMAFAC 160
Cdd:cd13988  79 SLYTVLEEPSNAYgLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNImrVIGEDGQSvyKLTDFGAARELEDDEQFVS 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 23510391 161 TYvGTPYYVPPEIWENL--------PYNNKSDIWSLGCILYELCTLKHPFQ 203
Cdd:cd13988 159 LY-GTEEYLHPDMYERAvlrkdhqkKYGATVDLWSIGVTFYHAATGSLPFR 208
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
4-195 2.49e-21

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: 94.95  E-value: 2.49e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPksFSNTQNSR---KEAVLLAKMKHPNIVAFKESFEAEGH-LYIVM 79
Cdd:cd07856  12 YSDLQPVGMGAFGLVCSARDQLTGQNVAVKKIMKP--FSTPVLAKrtyRELKLLKHLRHENIISLSDIFISPLEdIYFVT 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  80 EYCdGGDLMQKIKQQKgklfPEDMILNWFT-QMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAf 158
Cdd:cd07856  90 ELL-GTDLHRLLTSRP----LEKQFIQYFLyQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLARIQDPQMT- 163
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 23510391 159 acTYVGTPYYVPPEI---WENlpYNNKSDIWSLGCILYEL 195
Cdd:cd07856 164 --GYVSTRYYRAPEImltWQK--YDVEVDIWSAGCIFAEM 199
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
7-247 3.06e-21

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: 93.54  E-value: 3.06e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   7 LRMIGEGSFGRALLVQHE----SSNQMFAMKEIRlPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEG--HLYIVME 80
Cdd:cd14205   9 LQQLGKGNFGSVEMCRYDplqdNTGEVVAVKKLQ-HSTEEHLRDFEREIEILKSLQHDNIVKYKGVCYSAGrrNLRLIME 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  81 YCDGGDLMQKIKQQKGKlFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLsnPMAFAC 160
Cdd:cd14205  88 YLPYGSLRDYLQKHKER-IDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVL--PQDKEY 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 161 TYVGTP------YYVPPEIWENlPYNNKSDIWSLGCILYELCTL--KHPFQANSWKNLILKVCQGCIS------------ 220
Cdd:cd14205 165 YKVKEPgespifWYAPESLTES-KFSVASDVWSFGVVLYELFTYieKSKSPPAEFMRMIGNDKQGQMIvfhliellknng 243
                       250       260
                ....*....|....*....|....*....
gi 23510391 221 --PLPSHYSYELQFLVKQMFKRNPSHRPS 247
Cdd:cd14205 244 rlPRPDGCPDEIYMIMTECWNNNVNQRPS 272
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
42-258 3.24e-21

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK3 shows a restricted expression pattern; it is found at high levels in the pituary glands and is also expressed in the kidney and brain. It has been shown to regulate many ion transporters including members of the SLC12A family of cation-chloride cotransporters such as NCC and NKCC2, the renal potassium channel ROMK, and the epithelial calcium channels TRPV5 and TRPV6. WNK3 appears to sense low-chloride hypotonic stress and under these conditions, it activates SPAK, which directly interacts and phosphorylates cation-chloride cotransporters. WNK3 has also been shown to promote cell survival, possibly through interaction with procaspase-3 and HSP70. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 93.25  E-value: 3.24e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  42 SNTQNSRKEAVLLAKMKHPNIVAFKESFEA----EGHLYIVMEYCDGGDLMQKIKqqKGKLFPEDMILNWFTQMCLGVNH 117
Cdd:cd14031  51 AEQQRFKEEAEMLKGLQHPNIVRFYDSWESvlkgKKCIVLVTELMTSGTLKTYLK--RFKVMKPKVLRSWCRQILKGLQF 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 118 IHKKR--VLHRDIKSKNIFLT-QNGKVKLGDFGSARLLSNpmAFACTYVGTPYYVPPEIWENlPYNNKSDIWSLGCILYE 194
Cdd:cd14031 129 LHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLATLMRT--SFAKSVIGTPEFMAPEMYEE-HYDESVDVYAFGMCMLE 205
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23510391 195 LCTLKHPF-QANSWKNLILKVCQGcISPLPSH--YSYELQFLVKQMFKRNPSHRPSATTLLSRGIVA 258
Cdd:cd14031 206 MATSEYPYsECQNAAQIYRKVTSG-IKPASFNkvTDPEVKEIIEGCIRQNKSERLSIKDLLNHAFFA 271
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
10-252 4.74e-21

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: 92.32  E-value: 4.74e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMfAMKEIRlpKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDLMQ 89
Cdd:cd05112  12 IGSGQFGLVHLGYWLNKDKV-AIKTIR--EGAMSEEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFMEHGCLSD 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  90 KIKQQKGKlFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTyvGTPYYV 169
Cdd:cd05112  89 YLRTQRGL-FSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTRFVLDDQYTSST--GTKFPV 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 170 ---PPEIWENLPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQG--CISP-LPSHYSYElqfLVKQMFKRNP 242
Cdd:cd05112 166 kwsSPEVFSFSRYSSKSDVWSFGVLMWEVFSEgKIPYENRSNSEVVEDINAGfrLYKPrLASTHVYE---IMNHCWKERP 242
                       250
                ....*....|
gi 23510391 243 SHRPSATTLL 252
Cdd:cd05112 243 EDRPSFSLLL 252
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
9-252 4.95e-21

Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie proteins, consisting of Tie1 and Tie2, are receptor PTKs (RTKs) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2, while no specific ligand has been identified for Tie1. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. In vivo studies of Tie1 show that it is critical in vascular development. The Tie subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 92.80  E-value: 4.95e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   9 MIGEGSFGRALLVQ-HESSNQMFAmkEIRLPKSFSNTQNSRK---EAVLLAKM-KHPNIVAFKESFEAEGHLYIVMEYCD 83
Cdd:cd05047   2 VIGEGNFGQVLKARiKKDGLRMDA--AIKRMKEYASKDDHRDfagELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  84 GGDLMQKIKQQK--------------GKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSA 149
Cdd:cd05047  80 HGNLLDFLRKSRvletdpafaianstASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 150 RllsnpmafactyvGTPYYVP------PEIW---ENLPYN---NKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQ 216
Cdd:cd05047 160 R-------------GQEVYVKktmgrlPVRWmaiESLNYSvytTNSDVWSYGVLLWEIVSLgGTPYCGMTCAELYEKLPQ 226
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 23510391 217 GCISPLPSHYSYELQFLVKQMFKRNPSHRPSATTLL 252
Cdd:cd05047 227 GYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 262
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
8-247 7.50e-21

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: 92.93  E-value: 7.50e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFGR-----ALLVQHESSNQMFAMKEIRlpksfSNTQNSRKEAvLLAKMK-------HPNIVAFKESFEAEGHL 75
Cdd:cd05055  41 KTLGAGAFGKvveatAYGLSKSDAVMKVAVKMLK-----PTAHSSEREA-LMSELKimshlgnHENIVNLLGACTIGGPI 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  76 YIVMEYCDGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLL--- 152
Cdd:cd05055 115 LVITEYCCYGDLLNFLRRKRESFLTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTHGKIVKICDFGLARDImnd 194
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 153 SNPMAFACTYVGTPYYVPPEIWENLpYNNKSDIWSLGCILYELCTLK-HPFQANSWKNLILKVCQ-GCISPLPSHYSYEL 230
Cdd:cd05055 195 SNYVVKGNARLPVKWMAPESIFNCV-YTFESDVWSYGILLWEIFSLGsNPYPGMPVDSKFYKLIKeGYRMAQPEHAPAEI 273
                       250
                ....*....|....*..
gi 23510391 231 QFLVKQMFKRNPSHRPS 247
Cdd:cd05055 274 YDIMKTCWDADPLKRPT 290
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
10-252 1.07e-20

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: 91.57  E-value: 1.07e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKeirlpksFSNTQNSRKEAV-----LLAKMKHPNIVAFKESFEAEGHLYIVMEYCDG 84
Cdd:cd14113  15 LGRGRFSVVKKCDQRGTKRAVATK-------FVNKKLMKRDQVthelgVLQSLQHPQLVGLLDTFETPTSYILVLEMADQ 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  85 GDLMQKIKQQkGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGK---VKLGDFGSARLLsNPMAFACT 161
Cdd:cd14113  88 GRLLDYVVRW-GNL-TEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLSkptIKLADFGDAVQL-NTTYYIHQ 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 162 YVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISpLPSHY----SYELQFLVKQM 237
Cdd:cd14113 165 LLGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLDFS-FPDDYfkgvSQKAKDFVCFL 243
                       250
                ....*....|....*
gi 23510391 238 FKRNPSHRPSATTLL 252
Cdd:cd14113 244 LQMDPAKRPSAALCL 258
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
9-252 1.11e-20

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: 91.45  E-value: 1.11e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   9 MIGEGSFGRALLVQHESSNQMFAMKEIRLPK-----SFSNTQNSRKEAVLLAKM----KHPNIVAFKESFEAEGHLYIVM 79
Cdd:cd14101   7 LLGKGGFGTVYAGHRISDGLQVAIKQISRNRvqqwsKLPGVNPVPNEVALLQSVgggpGHRGVIRLLDWFEIPEGFLLVL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  80 E---YCDggDLMQKIKQQkGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFL-TQNGKVKLGDFGSARLLSNP 155
Cdd:cd14101  87 ErpqHCQ--DLFDYITER-GAL-DESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVdLRTGDIKLIDFGSGATLKDS 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 156 MafACTYVGTPYYVPPEIWENLPYNN-KSDIWSLGCILYELCTLKHPFQANSwknLILKVcqgciSP-LPSHYSYELQFL 233
Cdd:cd14101 163 M--YTDFDGTRVYSPPEWILYHQYHAlPATVWSLGILLYDMVCGDIPFERDT---DILKA-----KPsFNKRVSNDCRSL 232
                       250
                ....*....|....*....
gi 23510391 234 VKQMFKRNPSHRPSATTLL 252
Cdd:cd14101 233 IRSCLAYNPSDRPSLEQIL 251
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
7-252 1.14e-20

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: 91.91  E-value: 1.14e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   7 LRMIGEGSFGRALLVQHE----SSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEG--HLYIVME 80
Cdd:cd05079   9 IRDLGEGHFGKVELCRYDpegdNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGgnGIKLIME 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  81 YCDGGDLMQKIKQQKGKLFPEDMiLNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFAC 160
Cdd:cd05079  89 FLPSGSLKEYLPRNKNKINLKQQ-LKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYT 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 161 TY--VGTP-YYVPPEIWENLPYNNKSDIWSLGCILYELCT--------------LKHPFQANSWKNLILKVCQ-GCISPL 222
Cdd:cd05079 168 VKddLDSPvFWYAPECLIQSKFYIASDVWSFGVTLYELLTycdsesspmtlflkMIGPTHGQMTVTRLVRVLEeGKRLPR 247
                       250       260       270
                ....*....|....*....|....*....|
gi 23510391 223 PSHYSYELQFLVKQMFKRNPSHRPSATTLL 252
Cdd:cd05079 248 PPNCPEEVYQLMRKCWEFQPSKRTTFQNLI 277
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
49-254 1.29e-20

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: 90.80  E-value: 1.29e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  49 KEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDI 128
Cdd:cd05034  39 QEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTELMSKGSLLDYLRTGEGRALRLPQLIDMAAQIASGMAYLESRNYIHRDL 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 129 KSKNIFLTQNGKVKLGDFGSARLLSNpmafaCTYV---GTPYyvpPEIW---ENLPYNN---KSDIWSLGCILYELCTL- 198
Cdd:cd05034 119 AARNILVGENNVCKVADFGLARLIED-----DEYTareGAKF---PIKWtapEAALYGRftiKSDVWSFGILLYEIVTYg 190
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 23510391 199 KHPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQMFKRNPSHRPSATTLLSR 254
Cdd:cd05034 191 RVPYPGMTNREVLEQVERGYRMPKPPGCPDELYDIMLQCWKKEPEERPTFEYLQSF 246
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
4-197 1.37e-20

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: 92.84  E-value: 1.37e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSntQNSRKEAVLLAKMKHP------NIVAFKESFEAEGHLYI 77
Cdd:cd14225  45 YEILEVIGKGSFGQVVKALDHKTNEHVAIKIIRNKKRFH--HQALVEVKILDALRRKdrdnshNVIHMKEYFYFRNHLCI 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  78 VMEYCdGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGK--VKLGDFGSArllsnp 155
Cdd:cd14225 123 TFELL-GMNLYELIKKNNFQGFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQRGQssIKVIDFGSS------ 195
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 23510391 156 mafaC-------TYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCT 197
Cdd:cd14225 196 ----CyehqrvyTYIQSRFYRSPEVILGLPYSMAIDMWSLGCILAELYT 240
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
10-253 1.42e-20

Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. B-Raf activates ERK with the strongest magnitude, compared with other Raf kinases. Mice embryos deficient in B-Raf die around midgestation due to vascular hemorrhage caused by apoptotic endothelial cells. Mutations in B-Raf have been implicated in initiating tumorigenesis and tumor progression, and are found in malignant cutaneous melanoma, papillary thyroid cancer, as well as in ovarian and colorectal carcinomas. Most oncogenic B-Raf mutations are located at the activation loop of the kinase and surrounding regions; the V600E mutation accounts for around 90% of oncogenic mutations. The V600E mutant constitutively activates MEK, resulting in sustained activation of ERK. B-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The B-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 91.66  E-value: 1.42e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGrALLVQHESSNQMFAMKEIRLPKSfSNTQNSRKEAVLLAKMKHPNIVAFKeSFEAEGHLYIVMEYCDGGDLMQ 89
Cdd:cd14151  16 IGSGSFG-TVYKGKWHGDVAVKMLNVTAPTP-QQLQAFKNEVGVLRKTRHVNILLFM-GYSTKPQLAIVTQWCEGSSLYH 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  90 KIKQQKGKlFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARL---LSNPMAFAcTYVGTP 166
Cdd:cd14151  93 HLHIIETK-FEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVksrWSGSHQFE-QLSGSI 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 167 YYVPPEI---WENLPYNNKSDIWSLGCILYELCTLKHPF-QANSWKNLILKVCQGCISP----LPSHYSYELQFLVKQMF 238
Cdd:cd14151 171 LWMAPEVirmQDKNPYSFQSDVYAFGIVLYELMTGQLPYsNINNRDQIIFMVGRGYLSPdlskVRSNCPKAMKRLMAECL 250
                       250
                ....*....|....*
gi 23510391 239 KRNPSHRPSATTLLS 253
Cdd:cd14151 251 KKKRDERPLFPQILA 265
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
10-202 1.71e-20

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 92.52  E-value: 1.71e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   10 IGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSR-------------KEAVLLAKMKHPNIVAFKESFEAEGHLY 76
Cdd:PTZ00024  17 LGEGTYGKVEKAYDTLTGKIVAIKKVKIIEISNDVTKDRqlvgmcgihfttlRELKIMNEIKHENIMGLVDVYVEGDFIN 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   77 IVMEYCDGgDLmQKIKQQKgKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPM 156
Cdd:PTZ00024  97 LVMDIMAS-DL-KKVVDRK-IRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLARRYGYPP 173
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23510391  157 AFACTY--------------VGTPYYVPPE-IWENLPYNNKSDIWSLGCILYELCTLKHPF 202
Cdd:PTZ00024 174 YSDTLSkdetmqrreemtskVVTLWYRAPElLMGAEKYHFAVDMWSVGCIFAELLTGKPLF 234
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
6-221 1.72e-20

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: 91.23  E-value: 1.72e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   6 VLRMIGEGSFGRALLVQHESSnqmFAMKEIRLPKSFS-NTQNSRKEAVLLAKMKHPNIVAFKeSFEAEGHLYIVMEYCDG 84
Cdd:cd14150   4 MLKRIGTGSFGTVFRGKWHGD---VAVKILKVTEPTPeQLQAFKNEMQVLRKTRHVNILLFM-GFMTRPNFAIITQWCEG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  85 GDLMQKIKQQKGKlFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARL---------LSNP 155
Cdd:cd14150  80 SSLYRHLHVTETR-FDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLATVktrwsgsqqVEQP 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 156 MafactyvGTPYYVPPEI---WENLPYNNKSDIWSLGCILYELCTLKHPF-QANSWKNLILKVCQGCISP 221
Cdd:cd14150 159 S-------GSILWMAPEVirmQDTNPYSFQSDVYAYGVVLYELMSGTLPYsNINNRDQIIFMVGRGYLSP 221
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
10-252 2.11e-20

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: 90.45  E-value: 2.11e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKEIRLpksfsnTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDLMQ 89
Cdd:cd13995  12 IPRGAFGKVYLAQDTKTKKRMACKLIPV------EQFKPSDVEIQACFRHENIAELYGALLWEETVHLFMEAGEGGSVLE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  90 KIkQQKGKLFPEDMIlnWFTQMCL-GVNHIHKKRVLHRDIKSKNIFLtQNGKVKLGDFGSARLLSNPMAFACTYVGTPYY 168
Cdd:cd13995  86 KL-ESCGPMREFEII--WVTKHVLkGLDFLHSKNIIHHDIKPSNIVF-MSTKAVLVDFGLSVQMTEDVYVPKDLRGTEIY 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 169 VPPEIWENLPYNNKSDIWSLGCILYELCT------LKHPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQMFKRNP 242
Cdd:cd13995 162 MSPEVILCRGHNTKADIYSLGATIIHMQTgsppwvRRYPRSAYPSYLYIIHKQAPPLEDIAQDCSPAMRELLEAALERNP 241
                       250
                ....*....|
gi 23510391 243 SHRPSATTLL 252
Cdd:cd13995 242 NHRSSAAELL 251
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
10-202 2.59e-20

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


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 90.45  E-value: 2.59e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKEIRlPKSFSNTQNSR--KEAVLLAKMKHPNIVAFKESFEA--EGHLYIVM--EYCD 83
Cdd:cd14033   9 IGRGSFKTVYRGLDTETTVEVAWCELQ-TRKLSKGERQRfsEEVEMLKGLQHPNIVRFYDSWKStvRGHKCIILvtELMT 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  84 GGDL---MQKIKQQKGKLFPEdmilnWFTQMCLGVNHIHKKR--VLHRDIKSKNIFLT-QNGKVKLGDFGSARLLSnpMA 157
Cdd:cd14033  88 SGTLktyLKRFREMKLKLLQR-----WSRQILKGLHFLHSRCppILHRDLKCDNIFITgPTGSVKIGDLGLATLKR--AS 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 23510391 158 FACTYVGTPYYVPPEIWENlPYNNKSDIWSLGCILYELCTLKHPF 202
Cdd:cd14033 161 FAKSVIGTPEFMAPEMYEE-KYDEAVDVYAFGMCILEMATSEYPY 204
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
1-247 2.74e-20

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: 90.43  E-value: 2.74e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   1 MDDYMVLRMIGEGSFGRALLVQHESSNqmFAMKEIrlpKSFSNTQNSRKEAVLLAKMKHPNIVAFKESF-EAEGHLYIVM 79
Cdd:cd05082   5 MKELKLLQTIGKGEFGDVMLGDYRGNK--VAVKCI---KNDATAQAFLAEASVMTQLRHSNLVQLLGVIvEEKGGLYIVT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  80 EYCDGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFA 159
Cdd:cd05082  80 EYMAKGSLVDYLRSRGRSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEASSTQDTG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 160 CTYVGtpyYVPPEIWENLPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQMF 238
Cdd:cd05082 160 KLPVK---WTAPEALREKKFSTKSDVWSFGILLWEIYSFgRVPYPRIPLKDVVPRVEKGYKMDAPDGCPPAVYDVMKNCW 236

                ....*....
gi 23510391 239 KRNPSHRPS 247
Cdd:cd05082 237 HLDAAMRPS 245
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
4-244 3.03e-20

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: 92.07  E-value: 3.03e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLP-KSFSNTQNSRKEAVLLAKMKHPNIVAF------KESFEAEGHLY 76
Cdd:cd07874  19 YQNLKPIGSGAQGIVCAAYDAVLDRNVAIKKLSRPfQNQTHAKRAYRELVLMKCVNHKNIISLlnvftpQKSLEEFQDVY 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEYCDGgDLMQKIKQQkgklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARllSNPM 156
Cdd:cd07874  99 LVMELMDA-NLCQVIQME----LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLAR--TAGT 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 157 AFACT-YVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLPsHYSYELQFLVK 235
Cdd:cd07874 172 SFMMTpYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVIEQLGTPCP-EFMKKLQPTVR 250

                ....*....
gi 23510391 236 QMFKRNPSH 244
Cdd:cd07874 251 NYVENRPKY 259
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
4-254 3.19e-20

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: 91.70  E-value: 3.19e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQ--MFAMKEIrlPKSFSN---TQNSRKEAVLLAKMK-HPNIV-------AFKESFE 70
Cdd:cd07857   2 YELIKELGQGAYGIVCSARNAETSEeeTVAIKKI--TNVFSKkilAKRALRELKLLRHFRgHKNITclydmdiVFPGNFN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  71 AeghLYIVMEYCDGgDLMQKIKQqkGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSAR 150
Cdd:cd07857  80 E---LYLYEELMEA-DLHQIIRS--GQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLAR 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 151 LLS-NPM---AFACTYVGTPYYVPPEIW-ENLPYNNKSDIWSLGCILYELCTLKHPFQANSWK---NLILKV-------- 214
Cdd:cd07857 154 GFSeNPGenaGFMTEYVATRWYRAPEIMlSFQSYTKAIDVWSVGCILAELLGRKPVFKGKDYVdqlNQILQVlgtpdeet 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 23510391 215 CQGCISPLPSHYSYELQFLVKQMFKR-NPSHRPSATTLLSR 254
Cdd:cd07857 234 LSRIGSPKAQNYIRSLPNIPKKPFESiFPNANPLALDLLEK 274
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
3-254 3.22e-20

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: 90.19  E-value: 3.22e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQHESSNQMfAMKEIRlPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYC 82
Cdd:cd05148   7 EFTLERKLGSGYFGEVWEGLWKNRVRV-AIKILK-SDDLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGEPVYIITELM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  83 DGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMaFACTY 162
Cdd:cd05148  85 EKGSLLAFLRSPEGQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLARLIKEDV-YLSSD 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 163 VGTPY-YVPPEIWENLPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQMFKR 240
Cdd:cd05148 164 KKIPYkWTAPEAASHGTFSTKSDVWSFGILLYEMFTYgQVPYPGMNNHEVYDQITAGYRMPCPAKCPQEIYKIMLECWAA 243
                       250
                ....*....|....
gi 23510391 241 NPSHRPSATTLLSR 254
Cdd:cd05148 244 EPEDRPSFKALREE 257
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
7-254 3.72e-20

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: 90.34  E-value: 3.72e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   7 LRMIGEGSFGRALLVQHE----SSNQMFAMKEIRlPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGH--LYIVME 80
Cdd:cd05081   9 ISQLGKGNFGSVELCRYDplgdNTGALVAVKQLQ-HSGPDQQRDFQREIQILKALHSDFIVKYRGVSYGPGRrsLRLVME 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  81 YCDGGDLMQKIKQQKGKLFPEDMILnWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLsnPMAFAC 160
Cdd:cd05081  88 YLPSGCLRDFLQRHRARLDASRLLL-YSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLL--PLDKDY 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 161 TYVGTP------YYVPPEIWENLpYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCIS-------------- 220
Cdd:cd05081 165 YVVREPgqspifWYAPESLSDNI-FSRQSDVWSFGVVLYELFTYCDKSCSPSAEFLRMMGCERDVPalcrllelleegqr 243
                       250       260       270
                ....*....|....*....|....*....|....*
gi 23510391 221 -PLPSHYSYELQFLVKQMFKRNPSHRPSATTLLSR 254
Cdd:cd05081 244 lPAPPACPAEVHELMKLCWAPSPQDRPSFSALGPQ 278
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
1-202 4.49e-20

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: 91.48  E-value: 4.49e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   1 MDDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSN--TQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIV 78
Cdd:cd05610   3 IEEFVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKADMINKnmVHQVQAERDALALSKSPFIVHLYYSLQSANNVYLV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  79 MEYCDGGDLmQKIKQQKGkLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSAR-------- 150
Cdd:cd05610  83 MEYLIGGDV-KSLLHIYG-YFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKvtlnreln 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 151 ----LLSNPMA-----FACT------------------------------------YVGTPYYVPPEIWENLPYNNKSDI 185
Cdd:cd05610 161 mmdiLTTPSMAkpkndYSRTpgqvlslisslgfntptpyrtpksvrrgaarvegerILGTPDYLAPELLLGKPHGPAVDW 240
                       250
                ....*....|....*..
gi 23510391 186 WSLGCILYELCTLKHPF 202
Cdd:cd05610 241 WALGVCLFEFLTGIPPF 257
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
10-251 5.45e-20

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


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 89.22  E-value: 5.45e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKEIR--LPKSFSNtqNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDL 87
Cdd:cd05084   4 IGRGNFGEVFSGRLRADNTPVAVKSCRetLPPDLKA--KFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGGDF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  88 MQKIkQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMaFACTyvGTPY 167
Cdd:cd05084  82 LTFL-RTEGPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSREEEDGV-YAAT--GGMK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 168 YVP-----PEIWENLPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQMFKRN 241
Cdd:cd05084 158 QIPvkwtaPEALNYGRYSSESDVWSFGILLWETFSLgAVPYANLSNQQTREAVEQGVRLPCPENCPDEVYRLMEQCWEYD 237
                       250
                ....*....|
gi 23510391 242 PSHRPSATTL 251
Cdd:cd05084 238 PRKRPSFSTV 247
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
2-206 5.49e-20

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: 90.28  E-value: 5.49e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKM--KHPNIVAF--KESFEAEGH--L 75
Cdd:cd07837   1 DAYEKLEKIGEGTYGKVYKARDKNTGKLVALKKTRLEMEEEGVPSTALREVSLLQMlsQSIYIVRLldVEHVEENGKplL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  76 YIVMEYCDGgDLMQKI---KQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFL-TQNGKVKLGDFGSARL 151
Cdd:cd07837  81 YLVFEYLDT-DLKKFIdsyGRGPHNPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVdKQKGLLKIADLGLGRA 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 23510391 152 LSNPMAFACTYVGTPYYVPPEI-WENLPYNNKSDIWSLGCILYELCTLKHPFQANS 206
Cdd:cd07837 160 FTIPIKSYTHEIVTLWYRAPEVlLGSTHYSTPVDMWSVGCIFAEMSRKQPLFPGDS 215
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
8-253 5.51e-20

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: 89.21  E-value: 5.51e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFGRALLVQHESSNQMfAMKEIR----LPKSFsntqnsRKEAVLLAKMKHPNIVAFKeSFEAEGHLYIVMEYCD 83
Cdd:cd14203   1 VKLGQGCFGEVWMGTWNGTTKV-AIKTLKpgtmSPEAF------LEEAQIMKKLRHDKLVQLY-AVVSEEPIYIVTEFMS 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  84 GGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTYV 163
Cdd:cd14203  73 KGSLLDFLKDGEGKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQGA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 164 GTPY-YVPPEIWENLPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQMFKRN 241
Cdd:cd14203 153 KFPIkWTAPEAALYGRFTIKSDVWSFGILLTELVTKgRVPYPGMNNREVLEQVERGYRMPCPPGCPESLHELMCQCWRKD 232
                       250
                ....*....|..
gi 23510391 242 PSHRPSATTLLS 253
Cdd:cd14203 233 PEERPTFEYLQS 244
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
10-253 5.86e-20

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: 89.83  E-value: 5.86e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALL-----VQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVA-FKESFEAEGHlYIVMEYCD 83
Cdd:cd05046  13 LGRGEFGEVFLakakgIEEEGGETLVLVKALQKTKDENLQSEFRRELDMFRKLSHKNVVRlLGLCREAEPH-YMILEYTD 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  84 GGDLMQKIKQQKGKLFPED-------MILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPM 156
Cdd:cd05046  92 LGDLKQFLRATKSKDEKLKppplstkQKVALCTQIALGMDHLSNARFVHRDLAARNCLVSSQREVKVSLLSLSKDVYNSE 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 157 AFACTYVGTPY-YVPPE-IWENlPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQGCIS-PLPSHYSYELQF 232
Cdd:cd05046 172 YYKLRNALIPLrWLAPEaVQED-DFSTKSDVWSFGVLMWEVFTQgELPFYGLSDEEVLNRLQAGKLElPVPEGCPSRLYK 250
                       250       260
                ....*....|....*....|.
gi 23510391 233 LVKQMFKRNPSHRPSATTLLS 253
Cdd:cd05046 251 LMTRCWAVNPKDRPSFSELVS 271
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
4-259 6.15e-20

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: 90.70  E-value: 6.15e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFG---RALlvqHESSNQMFAMKEIRlpKSFSN---TQNSRKEAVLLAKMK-HPNIVAFKESFEAEGH-- 74
Cdd:cd07852   9 YEILKKLGKGAYGivwKAI---DKKTGEVVALKKIF--DAFRNatdAQRTFREIMFLQELNdHPNIIKLLNVIRAENDkd 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  75 LYIVMEYCDGgDLMQKIKqqKGKLfpEDM----ILnwfTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSAR 150
Cdd:cd07852  84 IYLVFEYMET-DLHAVIR--ANIL--EDIhkqyIM---YQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGLAR 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 151 LLS----NPMAFACT-YVGTPYYVPPEIWENLPYNNKS-DIWSLGCILYELCTLKHPFQANSWKNLILKVCQGC------ 218
Cdd:cd07852 156 SLSqleeDDENPVLTdYVATRWYRAPEILLGSTRYTKGvDMWSVGCILGEMLLGKPLFPGTSTLNQLEKIIEVIgrpsae 235
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23510391 219 -ISPLPSHY--------------SYELQF---------LVKQMFKRNPSHRPSATTLLSRGIVAR 259
Cdd:cd07852 236 dIESIQSPFaatmleslppsrpkSLDELFpkaspdaldLLKKLLVFNPNKRLTAEEALRHPYVAQ 300
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
7-256 6.42e-20

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


Pssm-ID: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 89.70  E-value: 6.42e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   7 LRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFS-NTQNSRKEAVLLAKM-KHPNIVAFKESFEAEGHLYIVMEYCDG 84
Cdd:cd14138  10 LEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSvDEQNALREVYAHAVLgQHSHVVRYYSAWAEDDHMLIQNEYCNG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  85 GDLMQKIKQ--QKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQ-----------------NGKV--KL 143
Cdd:cd14138  90 GSLADAISEnyRIMSYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFISRtsipnaaseegdedewaSNKVifKI 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 144 GDFGSARLLSNPMAFActyvGTPYYVPPEIW-ENLPYNNKSDIWSLGciLYELCTL-KHPFQAN--SWKnlilKVCQGCI 219
Cdd:cd14138 170 GDLGHVTRVSSPQVEE----GDSRFLANEVLqENYTHLPKADIFALA--LTVVCAAgAEPLPTNgdQWH----EIRQGKL 239
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 23510391 220 SPLPSHYSYELQFLVKQMFKRNPSHRPSATTLLSRGI 256
Cdd:cd14138 240 PRIPQVLSQEFLDLLKVMIHPDPERRPSAVALVKHSV 276
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
7-254 6.97e-20

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


Pssm-ID: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 89.37  E-value: 6.97e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   7 LRMIGEGSFGRAL--LVQH---ESSNQMFAMKEirLPKSFS--NTQNSRKEAVLLAKMKHPNIVAF-KESFEAEGHlYIV 78
Cdd:cd05036  11 IRALGQGAFGEVYegTVSGmpgDPSPLQVAVKT--LPELCSeqDEMDFLMEALIMSKFNHPNIVRCiGVCFQRLPR-FIL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  79 MEYCDGGDLMQKIKQQKGKLF-PEDMILNWFTQMCL----GVNHIHKKRVLHRDIKSKNIFLTQNG---KVKLGDFGSAR 150
Cdd:cd05036  88 LELMAGGDLKSFLRENRPRPEqPSSLTMLDLLQLAQdvakGCRYLEENHFIHRDIAARNCLLTCKGpgrVAKIGDFGMAR 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 151 LLsnpmafactYVGTPY-----------YVPPEIWENLPYNNKSDIWSLGCILYELCTLKH-PFQANSWKNLILKVCQG- 217
Cdd:cd05036 168 DI---------YRADYYrkggkamlpvkWMPPEAFLDGIFTSKTDVWSFGVLLWEIFSLGYmPYPGKSNQEVMEFVTSGg 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 23510391 218 -------CISPLpshYSyelqfLVKQMFKRNPSHRPSATTLLSR 254
Cdd:cd05036 239 rmdppknCPGPV---YR-----IMTQCWQHIPEDRPNFSTILER 274
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
8-252 7.49e-20

Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily contains c-ros, Sevenless, and similar proteins. The proto-oncogene c-ros encodes an orphan receptor PTK (RTK) with an unknown ligand. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. C-ros is expressed in embryonic cells of the kidney, intestine and lung, but disappears soon after birth. It persists only in the adult epididymis. Male mice bearing inactive mutations of c-ros lack the initial segment of the epididymis and are infertile. The Drosophila protein, Sevenless, is required for the specification of the R7 photoreceptor cell during eye development. The c-ros subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 89.40  E-value: 7.49e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFGRAL------LVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVA-FKESFEAEGHlYIVME 80
Cdd:cd05044   1 KFLGSGAFGEVFegtakdILGDGSGETKVAVKTLRKGATDQEKAEFLKEAHLMSNFKHPNILKlLGVCLDNDPQ-YIILE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  81 YCDGGDLMQKIKQQKGKLFPEDMI-LNWFTQMCL----GVNHIHKKRVLHRDIKSKNIFLTQNGK----VKLGDFGSAR- 150
Cdd:cd05044  80 LMEGGDLLSYLRAARPTAFTPPLLtLKDLLSICVdvakGCVYLEDMHFVHRDLAARNCLVSSKDYrervVKIGDFGLARd 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 151 LLSNPmafactyvgtpYY------------VPPEIWENLPYNNKSDIWSLGCILYELCTLKH-PFQANSwkNL-ILKVCQ 216
Cdd:cd05044 160 IYKND-----------YYrkegegllpvrwMAPESLVDGVFTTQSDVWAFGVLMWEILTLGQqPYPARN--NLeVLHFVR 226
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 23510391 217 --GCISPlPSHYSYELQFLVKQMFKRNPSHRPSATTLL 252
Cdd:cd05044 227 agGRLDQ-PDNCPDDLYELMLRCWSTDPEERPSFARIL 263
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
1-254 8.11e-20

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


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 88.95  E-value: 8.11e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   1 MDDYMVLRMIGEGSFGRALLVQHEssNQMFAMKEIrlpKSFSNTQNS-RKEAVLLAKMKHPNIVAFKESFEAEGHLYIVM 79
Cdd:cd05039   5 KKDLKLGELIGKGEFGDVMLGDYR--GQKVAVKCL---KDDSTAAQAfLAEASVMTTLRHPNLVQLLGVVLEGNGLYIVT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  80 EYCDGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFA 159
Cdd:cd05039  80 EYMAKGSLVDYLRSRGRAVITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAKEASSNQDGG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 160 CTYVGtpyYVPPEIWENLPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQG----CISPLPSHYsYElqfLV 234
Cdd:cd05039 160 KLPIK---WTAPEALREKKFSTKSDVWSFGILLWEIYSFgRVPYPRIPLKDVVPHVEKGyrmeAPEGCPPEV-YK---VM 232
                       250       260
                ....*....|....*....|
gi 23510391 235 KQMFKRNPSHRPSATTLLSR 254
Cdd:cd05039 233 KNCWELDPAKRPTFKQLREK 252
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
2-252 8.81e-20

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: 89.74  E-value: 8.81e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKeiRLPKSFSNTQNSR----KEAVLlakMKH--PNIVAFKESFEAEGHL 75
Cdd:cd06618  15 NDLENLGEIGSGTCGQVYKMRHKKTGHVMAVK--QMRRSGNKEENKRilmdLDVVL---KSHdcPYIVKCYGYFITDSDV 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  76 YIVMEycdggdLM----QKIKQQKGKLFPEDmILNWFTQMClgVNHIH----KKRVLHRDIKSKNIFLTQNGKVKLGDFG 147
Cdd:cd06618  90 FICME------LMstclDKLLKRIQGPIPED-ILGKMTVSI--VKALHylkeKHGVIHRDVKPSNILLDESGNVKLCDFG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 148 SARLLSNPMAFACTyVGTPYYVPPE---IWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLIL-KVCQGCISPLP 223
Cdd:cd06618 161 ISGRLVDSKAKTRS-AGCAAYMAPEridPPDNPKYDIRADVWSLGISLVELATGQFPYRNCKTEFEVLtKILNEEPPSLP 239
                       250       260       270
                ....*....|....*....|....*....|.
gi 23510391 224 SHYSYELQF--LVKQMFKRNPSHRPSATTLL 252
Cdd:cd06618 240 PNEGFSPDFcsFVDLCLTKDHRYRPKYRELL 270
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
6-253 9.61e-20

Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. There are two forms of STRAD, alpha and beta, that complex with LKB1 and MO25. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha stabilized through ATP and MO25 may be needed to activate LKB1. The STRAD 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: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 90.05  E-value: 9.61e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   6 VLRMIGEGSFGRA--LLVQHESSNQMFAMKEIRLP----KSFSNTQnsrKEAVLLAKMKHPNIVAFKESFEAEGHLYIVM 79
Cdd:cd08216   2 LLYEIGKCFKGGGvvHLAKHKPTNTLVAVKKINLEsdskEDLKFLQ---QEILTSRQLQHPNILPYVTSFVVDNDLYVVT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  80 EYCDGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARllsnPMAFA 159
Cdd:cd08216  79 PLMAYGSCRDLLKTHFPEGLPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYAY----SMVKH 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 160 CTYVGTPYYVPPEIWENLP-------------YNNKSDIWSLGCILYEL-----------------------------CT 197
Cdd:cd08216 155 GKRQRVVHDFPKSSEKNLPwlspevlqqnllgYNEKSDIYSVGITACELangvvpfsdmpatqmllekvrgttpqlldCS 234
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23510391 198 LKHPFQANSWKNLILKVCQGCISPLPSHY-----SYELQFLVKQMFKRNPSHRPSATTLLS 253
Cdd:cd08216 235 TYPLEEDSMSQSEDSSTEHPNNRDTRDIPyqrtfSEAFHQFVELCLQRDPELRPSASQLLA 295
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
10-247 1.18e-19

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: 88.98  E-value: 1.18e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMfAMKEIRlPKSFSnTQNSRKEAVLLAKMKHPNIVAFKeSFEAEGHLYIVMEYCDGGDLMQ 89
Cdd:cd05071  17 LGQGCFGEVWMGTWNGTTRV-AIKTLK-PGTMS-PEAFLQEAQVMKKLRHEKLVQLY-AVVSEEPIYIVTEYMSKGSLLD 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  90 KIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTYVGTPY-Y 168
Cdd:cd05071  93 FLKGEMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAKFPIkW 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 169 VPPEIWENLPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQMFKRNPSHRPS 247
Cdd:cd05071 173 TAPEAALYGRFTIKSDVWSFGILLTELTTKgRVPYPGMVNREVLDQVERGYRMPCPPECPESLHDLMCQCWRKEPEERPT 252
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
4-253 1.23e-19

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: 88.49  E-value: 1.23e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPK-----SFSNTQNSRKEAVLLAKMKH--PNIVAFKESFEAEGHLY 76
Cdd:cd14100   2 YQVGPLLGSGGFGSVYSGIRVADGAPVAIKHVEKDRvsewgELPNGTRVPMEIVLLKKVGSgfRGVIRLLDWFERPDSFV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEYCDG-GDLMQKIKQqKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQN-GKVKLGDFGSARLLSN 154
Cdd:cd14100  82 LVLERPEPvQDLFDFITE-RGAL-PEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDLNtGELKLIDFGSGALLKD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 155 PMafACTYVGTPYYVPPEIWENLPYNNKS-DIWSLGCILYELCTLKHPFQANSwknlilKVCQGCISpLPSHYSYELQFL 233
Cdd:cd14100 160 TV--YTDFDGTRVYSPPEWIRFHRYHGRSaAVWSLGILLYDMVCGDIPFEHDE------EIIRGQVF-FRQRVSSECQHL 230
                       250       260
                ....*....|....*....|
gi 23510391 234 VKQMFKRNPSHRPSATTLLS 253
Cdd:cd14100 231 IKWCLALRPSDRPSFEDIQN 250
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
8-206 1.38e-19

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: 90.19  E-value: 1.38e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFGRALLVQHESSNQMFAMKeiRLPKSFSNTQNSRK---EAVLLAKMKHPNIVAFKE--------SFEaegHLY 76
Cdd:cd07853   6 RPIGYGAFGVVWSVTDPRDGKRVALK--KMPNVFQNLVSCKRvfrELKMLCFFKHDNVLSALDilqpphidPFE---EIY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEycdggdLMQ----KIKQQKGKLFPeDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLL 152
Cdd:cd07853  81 VVTE------LMQsdlhKIIVSPQPLSS-DHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVE 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 23510391 153 SNPMAFACTY-VGTPYYVPPEIWENLP-YNNKSDIWSLGCILYELCTLKHPFQANS 206
Cdd:cd07853 154 EPDESKHMTQeVVTQYYRAPEILMGSRhYTSAVDIWSVGCIFAELLGRRILFQAQS 209
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
10-247 1.63e-19

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: 88.59  E-value: 1.63e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMfAMKEIR----LPKSFsntqnsRKEAVLLAKMKHPNIVAFKeSFEAEGHLYIVMEYCDGG 85
Cdd:cd05069  20 LGQGCFGEVWMGTWNGTTKV-AIKTLKpgtmMPEAF------LQEAQIMKKLRHDKLVPLY-AVVSEEPIYIVTEFMGKG 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  86 DLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTYVGT 165
Cdd:cd05069  92 SLLDFLKEGDGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQGAKF 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 166 PY-YVPPEIWENLPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQMFKRNPS 243
Cdd:cd05069 172 PIkWTAPEAALYGRFTIKSDVWSFGILLTELVTKgRVPYPGMVNREVLEQVERGYRMPCPQGCPESLHELMKLCWKKDPD 251

                ....
gi 23510391 244 HRPS 247
Cdd:cd05069 252 ERPT 255
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
10-195 1.79e-19

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: 88.08  E-value: 1.79e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKEirLPKSFSNTQ-NSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDLM 88
Cdd:cd14222   1 LGKGFFGQAIKVTHKATGKVMVMKE--LIRCDEETQkTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTLK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  89 QKIKQQKGklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSN-----PMAFAC--- 160
Cdd:cd14222  79 DFLRADDP--FPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEekkkpPPDKPTtkk 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 23510391 161 ------------TYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYEL 195
Cdd:cd14222 157 rtlrkndrkkryTVVGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCEI 203
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
4-195 1.79e-19

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: 89.32  E-value: 1.79e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSntQNSRKEAVLLAKMKHPNIVAFK-----ESFEAEGHLYIV 78
Cdd:cd14229   2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKILKNHPSYA--RQGQIEVGILARLSNENADEFNfvrayECFQHRNHTCLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  79 MEYCDGgDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLT----QNGKVKLGDFGSARLLSN 154
Cdd:cd14229  80 FEMLEQ-NLYDFLKQNKFSPLPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMLVdpvrQPYRVKVIDFGSASHVSK 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 23510391 155 pmAFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYEL 195
Cdd:cd14229 159 --TVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAEL 197
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
4-205 1.92e-19

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: 87.67  E-value: 1.92e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIrlPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCD 83
Cdd:cd14110   5 YAFQTEINRGRFSVVRQCEEKRSGQMLAAKII--PYKPEDKQLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELCS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  84 GGDLMQKIKQQKgkLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTYV 163
Cdd:cd14110  83 GPELLYNLAERN--SYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLGNAQPFNQGKVLMTDKK 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 23510391 164 GtpYYV---PPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQAN 205
Cdd:cd14110 161 G--DYVetmAPELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSSD 203
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
10-252 2.17e-19

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


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 88.24  E-value: 2.17e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDLMQ 89
Cdd:cd14090  10 LGEGAYASVQTCINLYTGKEYAVKIIEKHPGHSRSRVFREVETLHQCQGHPNILQLIEYFEDDERFYLVFEKMRGGPLLS 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  90 KIKQQkgKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGK---VKLGDFGSA---RLLSNPMAFACT-- 161
Cdd:cd14090  90 HIEKR--VHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKvspVKICDFDLGsgiKLSSTSMTPVTTpe 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 162 ---YVGTPYYVPPEI-----WENLPYNNKSDIWSLGCILYELCTLKHPFQAN-----SW---------KNLILKVCQGCI 219
Cdd:cd14090 168 lltPVGSAEYMAPEVvdafvGEALSYDKRCDLWSLGVILYIMLCGYPPFYGRcgedcGWdrgeacqdcQELLFHSIQEGE 247
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 23510391 220 SPLP----SHYSYELQFLVKQMFKRNPSHRPSATTLL 252
Cdd:cd14090 248 YEFPekewSHISAEAKDLISHLLVRDASQRYTAEQVL 284
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
6-247 2.22e-19

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: 87.63  E-value: 2.22e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   6 VLRMIGEGSFGRALLvQHESSNQMFAMKEIRL----PKSFsntqnsRKEAVLLAKMKHPNIVAFKESFEAEGhLYIVMEY 81
Cdd:cd05067  11 LVERLGAGQFGEVWM-GYYNGHTKVAIKSLKQgsmsPDAF------LAEANLMKQLQHQRLVRLYAVVTQEP-IYIITEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACT 161
Cdd:cd05067  83 MENGSLVDFLKTPSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLIEDNEYTARE 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 162 YVGTPY-YVPPEIWENLPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQMFK 239
Cdd:cd05067 163 GAKFPIkWTAPEAINYGTFTIKSDVWSFGILLTEIVTHgRIPYPGMTNPEVIQNLERGYRMPRPDNCPEELYQLMRLCWK 242

                ....*...
gi 23510391 240 RNPSHRPS 247
Cdd:cd05067 243 ERPEDRPT 250
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
12-245 2.39e-19

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 87.60  E-value: 2.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   12 EGSFGRALLVQHESSNQMFAMKEIRlPKSFSNTqnsrkEAVLLAKMK-HPNIVAFKESFEAEGHLYIVMEYCDGGDLMQK 90
Cdd:PHA03390  26 DGKFGKVSVLKHKPTQKLFVQKIIK-AKNFNAI-----EPMVHQLMKdNPNFIKLYYSVTTLKGHVLIMDYIKDGDLFDL 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   91 IKQqKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQN-GKVKLGDFGSARLLSNPmafaCTYVGTPYYV 169
Cdd:PHA03390 100 LKK-EGKL-SEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRAkDRIYLCDYGLCKIIGTP----SCYDGTLDYF 173
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23510391  170 PPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCIS---PLPSHYSYELQFLVKQMFKRNPSHR 245
Cdd:PHA03390 174 SPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKEDEDEELDLESLLKRQQkklPFIKNVSKNANDFVQSMLKYNINYR 252
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
10-247 2.71e-19

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: 87.40  E-value: 2.71e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGralLVQ----HESSNQMF--AMKEIR--LPKSFSNTQNSRKEAVLLAKMKHPNIVafkesfeaegHLY----- 76
Cdd:cd05040   3 LGDGSFG---VVRrgewTTPSGKVIqvAVKCLKsdVLSQPNAMDDFLKEVNAMHSLDHPNLI----------RLYgvvls 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 ----IVMEYCDGGDLMQKIKQQKGKlFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLL 152
Cdd:cd05040  70 splmMVTELAPLGSLLDRLRKDQGH-FLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGLMRAL 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 153 SnpmafactyVGTPYYV------------PPEIWENLPYNNKSDIWSLGCILYELCTlkhpFQANSWKNL----ILKVC- 215
Cdd:cd05040 149 P---------QNEDHYVmqehrkvpfawcAPESLKTRKFSHASDVWMFGVTLWEMFT----YGEEPWLGLngsqILEKId 215
                       250       260       270
                ....*....|....*....|....*....|...
gi 23510391 216 -QGCISPLPSHYSYELQFLVKQMFKRNPSHRPS 247
Cdd:cd05040 216 kEGERLERPDDCPQDIYNVMLQCWAHKPADRPT 248
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
31-253 3.01e-19

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: 87.67  E-value: 3.01e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  31 AMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFkesFEAEGH-LYIVMEYCDGGDLMQKIKQQKGKLFPEDMIL--NW 107
Cdd:cd14000  41 MLRHLRATDAMKNFRLLRQELTVLSHLHHPSIVYL---LGIGIHpLMLVLELAPLGSLDHLLQQDSRSFASLGRTLqqRI 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 108 FTQMCLGVNHIHKKRVLHRDIKSKNIF---LTQNGKV--KLGDFGSARlLSNPMAfACTYVGTPYYVPPEIWE-NLPYNN 181
Cdd:cd14000 118 ALQVADGLRYLHSAMIIYRDLKSHNVLvwtLYPNSAIiiKIADYGISR-QCCRMG-AKGSEGTPGFRAPEIARgNVIYNE 195
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23510391 182 KSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLPSHYSY---ELQFLVKQMFKRNPSHRPSATTLLS 253
Cdd:cd14000 196 KVDVFSFGMLLYEILSGGAPMVGHLKFPNEFDIHGGLRPPLKQYECApwpEVEVLMKKCWKENPQQRPTAVTVVS 270
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
2-245 3.23e-19

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


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 87.52  E-value: 3.23e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQ-----MFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLY 76
Cdd:cd05049   5 DTIVLKRELGEGAFGKVFLGECYNLEPeqdkmLVAVKTLKDASSPDARKDFEREAELLTNLQHENIVKFYGVCTEGDPLL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEYCDGGDL-------------MQKIKQQKGKLFPEDMiLNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKL 143
Cdd:cd05049  85 MVFEYMEHGDLnkflrshgpdaafLASEDSAPGELTLSQL-LHIAVQIASGMVYLASQHFVHRDLATRNCLVGTNLVVKI 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 144 GDFGSARLLSNpmafactyvgTPYY------------VPPEIWENLPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNL 210
Cdd:cd05049 164 GDFGMSRDIYS----------TDYYrvgghtmlpirwMPPESILYRKFTTESDVWSFGVVLWEIFTYgKQPWFQLSNTEV 233
                       250       260       270
                ....*....|....*....|....*....|....*
gi 23510391 211 ILKVCQGCISPLPSHYSYELQFLVKQMFKRNPSHR 245
Cdd:cd05049 234 IECITQGRLLQRPRTCPSEVYAVMLGCWKREPQQR 268
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
1-202 3.37e-19

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: 87.90  E-value: 3.37e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   1 MDDYMVL--RMIGEGSFGRALLVQHESSNQMFAMKeIRLPKSFSNTQnsrkeaVLLAKM--KHPNIVAFKESF------- 69
Cdd:cd14171   3 LEEYEVNwtQKLGTGISGPVRVCVKKSTGERFALK-ILLDRPKARTE------VRLHMMcsGHPNIVQIYDVYansvqfp 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  70 ---EAEGHLYIVMEYCDGGDLMQKIKQQKGklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGK---VKL 143
Cdd:cd14171  76 gesSPRARLLIVMELMEGGELFDRISQHRH--FTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSEdapIKL 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 144 GDFGSARL----LSNPMAfactyvgTPYYVPPEIWE---------------NLPYN-NKS-DIWSLGCILYELCTLKHPF 202
Cdd:cd14171 154 CDFGFAKVdqgdLMTPQF-------TPYYVAPQVLEaqrrhrkersgiptsPTPYTyDKScDMWSLGVIIYIMLCGYPPF 226
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
2-247 3.84e-19

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: 87.43  E-value: 3.84e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHeSSNQMFAMKEIRlPKSFSnTQNSRKEAVLLAKMKHPNIVAFKeSFEAEGHLYIVMEY 81
Cdd:cd05070   9 ESLQLIKRLGNGQFGEVWMGTW-NGNTKVAIKTLK-PGTMS-PESFLEEAQIMKKLKHDKLVQLY-AVVSEEPIYIVTEY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACT 161
Cdd:cd05070  85 MSKGSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEYTARQ 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 162 YVGTPY-YVPPEIWENLPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQMFK 239
Cdd:cd05070 165 GAKFPIkWTAPEAALYGRFTIKSDVWSFGILLTELVTKgRVPYPGMNNREVLEQVERGYRMPCPQDCPISLHELMIHCWK 244

                ....*...
gi 23510391 240 RNPSHRPS 247
Cdd:cd05070 245 KDPEERPT 252
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
8-247 3.87e-19

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


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 86.73  E-value: 3.87e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDL 87
Cdd:cd05041   1 EKIGRGNFGDVYRGVLKPDNTEVAVKTCRETLPPDLKRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGGSL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  88 MQKIKQQKGKLFPEDMilnwfTQMCL----GVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTYV 163
Cdd:cd05041  81 LTFLRKKGARLTVKQL-----LQMCLdaaaGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSREEEDGEYTVSDGL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 164 GTpyyVP-----PEIWENLPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQM 237
Cdd:cd05041 156 KQ---IPikwtaPEALNYGRYTSESDVWSFGILLWEIFSLgATPYPGMSNQQTREQIESGYRMPAPELCPEAVYRLMLQC 232
                       250
                ....*....|
gi 23510391 238 FKRNPSHRPS 247
Cdd:cd05041 233 WAYDPENRPS 242
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
9-259 4.11e-19

Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; Tie1; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie1 is a receptor tyr kinase (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. No specific ligand has been identified for Tie1, although the angiopoietin, Ang-1, binds to Tie1 through integrins at high concentrations. In vivo studies of Tie1 show that it is critical in vascular development.


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 87.75  E-value: 4.11e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   9 MIGEGSFGRALLVQ-HESSNQMFAmkEIRLPKSFSNTQNSRK---EAVLLAKM-KHPNIVAFKESFEAEGHLYIVMEYCD 83
Cdd:cd05089   9 VIGEGNFGQVIKAMiKKDGLKMNA--AIKMLKEFASENDHRDfagELEVLCKLgHHPNIINLLGACENRGYLYIAIEYAP 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  84 GGDLMQKIKQQK--------------GKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSA 149
Cdd:cd05089  87 YGNLLDFLRKSRvletdpafakehgtASTLTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVSKIADFGLS 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 150 RLLSnpmafacTYVGTPYYVPPEIW---ENLPYN---NKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQGCISPL 222
Cdd:cd05089 167 RGEE-------VYVKKTMGRLPVRWmaiESLNYSvytTKSDVWSFGVLLWEIVSLgGTPYCGMTCAELYEKLPQGYRMEK 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 23510391 223 PSHYSYELQFLVKQMFKRNPSHRPSATTL---LSRGIVAR 259
Cdd:cd05089 240 PRNCDDEVYELMRQCWRDRPYERPPFSQIsvqLSRMLEAR 279
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
4-202 5.48e-19

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 89.75  E-value: 5.48e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391    4 YMVLRMIGEGSFGRALL------VQHE-------SSNQMFAMKEIRLPKSFSNTQNS----RKEAVLLAKMKHPNIVAFK 66
Cdd:PHA03210 150 FRVIDDLPAGAFGKIFIcalrasTEEAearrgvnSTNQGKPKCERLIAKRVKAGSRAaiqlENEILALGRLNHENILKIE 229
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   67 ESFEAEGHLYIVMEYCDGgDLMQKIKQqkGKLFPEDMILNWFT-----QMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKV 141
Cdd:PHA03210 230 EILRSEANTYMITQKYDF-DLYSFMYD--EAFDWKDRPLLKQTraimkQLLCAVEYIHDKKLIHRDIKLENIFLNCDGKI 306
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23510391  142 KLGDFGSARLLSNP-MAFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELctLKHPF 202
Cdd:PHA03210 307 VLGDFGTAMPFEKErEAFDYGWVGTVATNSPEILAGDGYCEITDIWSCGLILLDM--LSHDF 366
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
4-244 6.01e-19

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: 88.18  E-value: 6.01e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLP-KSFSNTQNSRKEAVLLAKMKHPNIVAF------KESFEAEGHLY 76
Cdd:cd07875  26 YQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSRPfQNQTHAKRAYRELVLMKCVNHKNIIGLlnvftpQKSLEEFQDVY 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEYCDGgDLMQKIKQQkgklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPM 156
Cdd:cd07875 106 IVMELMDA-NLCQVIQME----LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSF 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 157 AFAcTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLPsHYSYELQFLVKQ 236
Cdd:cd07875 181 MMT-PYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGVLFPGTDHIDQWNKVIEQLGTPCP-EFMKKLQPTVRT 258

                ....*...
gi 23510391 237 MFKRNPSH 244
Cdd:cd07875 259 YVENRPKY 266
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
9-252 6.17e-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: 87.01  E-value: 6.17e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   9 MIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDLM 88
Cdd:cd14174   9 LLGEGAYAKVQGCVSLQNGKEYAVKIIEKNAGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLRGGSIL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  89 QKIkqQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKV---KLGDF--GSARLLSNpmafACTYV 163
Cdd:cd14174  89 AHI--QKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPDKVspvKICDFdlGSGVKLNS----ACTPI 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 164 GTPY---------YVPPEIWENLP-----YNNKSDIWSLGCILYELCTLKHPFQAN-----SW-KNLILKVCQGCI---- 219
Cdd:cd14174 163 TTPElttpcgsaeYMAPEVVEVFTdeatfYDKRCDLWSLGVILYIMLSGYPPFVGHcgtdcGWdRGEVCRVCQNKLfesi 242
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 23510391 220 ----SPLP----SHYSYELQFLVKQMFKRNPSHRPSATTLL 252
Cdd:cd14174 243 qegkYEFPdkdwSHISSEAKDLISKLLVRDAKERLSAAQVL 283
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
4-229 6.68e-19

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: 87.76  E-value: 6.68e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRAL-LVQHESSNQMFAMKEIRLPKSFSntQNSRKEAVLLAKMKHPN------IVAFKESFEAEGHLY 76
Cdd:cd14214  15 YEIVGDLGEGTFGKVVeCLDHARGKSQVALKIIRNVGKYR--EAARLEINVLKKIKEKDkenkflCVLMSDWFNFHGHMC 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEYCdGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLT-------------------Q 137
Cdd:cd14214  93 IAFELL-GKNTFEFLKENNFQPYPLPHIRHMAYQLCHALKFLHENQLTHTDLKPENILFVnsefdtlynesksceeksvK 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 138 NGKVKLGDFGSARLlsnPMAFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVcQG 217
Cdd:cd14214 172 NTSIRVADFGSATF---DHEHHTTIVATRHYRPPEVILELGWAQPCDVWSLGCILFEYYRGFTLFQTHENREHLVMM-EK 247
                       250
                ....*....|..
gi 23510391 218 CISPLPSHYSYE 229
Cdd:cd14214 248 ILGPIPSHMIHR 259
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
10-252 8.32e-19

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: 85.78  E-value: 8.32e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKEIRlpKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDLMQ 89
Cdd:cd14115   1 IGRGRFSIVKKCLHKATRKDVAVKFVS--KKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRLLD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  90 KIKQQKGKLfpEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQN---GKVKLGDFGSARLLSNPMAFAcTYVGTP 166
Cdd:cd14115  79 YLMNHDELM--EEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGHRHVH-HLLGNP 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 167 YYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISpLPSHY----SYELQFLVKQMFKRNP 242
Cdd:cd14115 156 EFAAPEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFS-FPDEYfgdvSQAARDFINVILQEDP 234
                       250
                ....*....|
gi 23510391 243 SHRPSATTLL 252
Cdd:cd14115 235 RRRPTAATCL 244
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
4-213 8.38e-19

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: 87.53  E-value: 8.38e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRkEAVLLAKMKHPNIVAFKESFEAEGH--------- 74
Cdd:cd07854   7 YMDLRPLGCGSNGLVFSAVDSDCDKRVAVKKIVLTDPQSVKHALR-EIKIIRRLDHDNIVKVYEVLGPSGSdltedvgsl 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  75 -----LYIVMEYCDGgDLMQKIKQQkgkLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKV-KLGDFGS 148
Cdd:cd07854  86 telnsVYIVQEYMET-DLANVLEQG---PLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTEDLVlKIGDFGL 161
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23510391 149 ARLL----SNPMAFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQ-ANSWK--NLILK 213
Cdd:cd07854 162 ARIVdphySHKGYLSEGLVTKWYRSPRLLLSPNNYTKAIDMWAAGCIFAEMLTGKPLFAgAHELEqmQLILE 233
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
4-211 9.51e-19

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: 87.78  E-value: 9.51e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLP-KSFSNTQNSRKEAVLLAKMKHPNIVAF------KESFEAEGHLY 76
Cdd:cd07876  23 YQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRPfQNQTHAKRAYRELVLLKCVNHKNIISLlnvftpQKSLEEFQDVY 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEYCDGgDLMQKIKQQkgkLFPEDMILNWFTQMClGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPM 156
Cdd:cd07876 103 LVMELMDA-NLCQVIHME---LDHERMSYLLYQMLC-GIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTACTNF 177
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 23510391 157 AFAcTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQA----NSWKNLI 211
Cdd:cd07876 178 MMT-PYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGSVIFQGtdhiDQWNKVI 235
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
10-252 1.32e-18

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: 86.61  E-value: 1.32e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKEIRLP-KSFSNTQNSRKEAVLLAKM-------KHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd05101  32 LGEGCFGQVVMAEAVGIDKDKPKEAVTVAvKMLKDDATEKDLSDLVSEMemmkmigKHKNIINLLGACTQDGPLYVIVEY 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDLMQKIKQQK----------GKLFPEDM----ILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFG 147
Cdd:cd05101 112 ASKGNLREYLRARRppgmeysydiNRVPEEQMtfkdLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMKIADFG 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 148 SARLLSNPMAFACTYVGT-PY-YVPPEIWENLPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQGCISPLPS 224
Cdd:cd05101 192 LARDINNIDYYKKTTNGRlPVkWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLgGSPYPGIPVEELFKLLKEGHRMDKPA 271
                       250       260
                ....*....|....*....|....*...
gi 23510391 225 HYSYELQFLVKQMFKRNPSHRPSATTLL 252
Cdd:cd05101 272 NCTNELYMMMRDCWHAVPSQRPTFKQLV 299
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
49-253 1.35e-18

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: 85.32  E-value: 1.35e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  49 KEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDLMQKIKQQkGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDI 128
Cdd:cd05113  48 EEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANGCLLNYLREM-RKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDL 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 129 KSKNIFLTQNGKVKLGDFGSARLLSNPMafACTYVGTPYYV---PPEIWENLPYNNKSDIWSLGCILYELCTL-KHPFQA 204
Cdd:cd05113 127 AARNCLVNDQGVVKVSDFGLSRYVLDDE--YTSSVGSKFPVrwsPPEVLMYSKFSSKSDVWAFGVLMWEVYSLgKMPYER 204
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 23510391 205 NSWKNLILKVCQGCISPLPSHYSYELQFLVKQMFKRNPSHRPSATTLLS 253
Cdd:cd05113 205 FTNSETVEHVSQGLRLYRPHLASEKVYTIMYSCWHEKADERPTFKILLS 253
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
10-254 2.08e-18

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: 84.71  E-value: 2.08e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALL-VQHESSNQMF--AMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGhLYIVMEYCDGGD 86
Cdd:cd05060   3 LGHGNFGSVRKgVYLMKSGKEVevAVKTLKQEHEKAGKKEFLREASVMAQLDHPCIVRLIGVCKGEP-LMLVMELAPLGP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  87 LMQKIkqQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSnpmafactyVGTP 166
Cdd:cd05060  82 LLKYL--KKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMSRALG---------AGSD 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 167 YY------------VPPEIWENLPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQGCISPLPSHYSYELQFL 233
Cdd:cd05060 151 YYrattagrwplkwYAPECINYGKFSSKSDVWSYGVTLWEAFSYgAKPYGEMKGPEVIAMLESGERLPRPEECPQEIYSI 230
                       250       260
                ....*....|....*....|.
gi 23510391 234 VKQMFKRNPSHRPSATTLLSR 254
Cdd:cd05060 231 MLSCWKYRPEDRPTFSELEST 251
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
3-252 2.09e-18

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: 85.83  E-value: 2.09e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVL-RMIGEGSFGRALLVQ-----HESSNQM--FAMKEIRLPKSFSNTQNSRKEAVLLAKM-KHPNIVAFKESFEAEG 73
Cdd:cd05098  13 DRLVLgKPLGEGCFGQVVLAEaigldKDKPNRVtkVAVKMLKSDATEKDLSDLISEMEMMKMIgKHKNIINLLGACTQDG 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  74 HLYIVMEYCDGGDLMQKIKQQKGKLF---------PEDM-----ILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNG 139
Cdd:cd05098  93 PLYVIVEYASKGNLREYLQARRPPGMeycynpshnPEEQlsskdLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDN 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 140 KVKLGDFGSARLLSNPMAFACTYVGT-PY-YVPPEIWENLPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQ 216
Cdd:cd05098 173 VMKIADFGLARDIHHIDYYKKTTNGRlPVkWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLgGSPYPGVPVEELFKLLKE 252
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 23510391 217 GCISPLPSHYSYELQFLVKQMFKRNPSHRPSATTLL 252
Cdd:cd05098 253 GHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLV 288
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
45-258 2.99e-18

Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK2 is widely expressed and has been shown to be epigenetically silenced in gliomas. It inhibits cell growth by acting as a negative regulator of MEK1-ERK1/2 signaling. WNK2 modulates growth factor-induced cancer cell proliferation, suggesting that it may be a tumor suppressor gene. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. The WNK2-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 84.74  E-value: 2.99e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  45 QNSRKEAVLLAKMKHPNIVAFKESFEAEGH----LYIVMEYCDGGDLMQKIKqqKGKLFPEDMILNWFTQMCLGVNHIHK 120
Cdd:cd14032  45 QRFKEEAEMLKGLQHPNIVRFYDFWESCAKgkrcIVLVTELMTSGTLKTYLK--RFKVMKPKVLRSWCRQILKGLLFLHT 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 121 KR--VLHRDIKSKNIFLT-QNGKVKLGDFGSARLlsNPMAFACTYVGTPYYVPPEIWENlPYNNKSDIWSLGCILYELCT 197
Cdd:cd14032 123 RTppIIHRDLKCDNIFITgPTGSVKIGDLGLATL--KRASFAKSVIGTPEFMAPEMYEE-HYDESVDVYAFGMCMLEMAT 199
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23510391 198 LKHPFQANSWKNLILKVCQGCISP--LPSHYSYELQFLVKQMFKRNPSHRPSATTLLSRGIVA 258
Cdd:cd14032 200 SEYPYSECQNAAQIYRKVTCGIKPasFEKVTDPEIKEIIGECICKNKEERYEIKDLLSHAFFA 262
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
2-253 3.35e-18

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: 84.31  E-value: 3.35e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd14088   1 DRYDLGQVIKTEEFCEIFRAKDKTTGKLYTCKKFLKRDGRKVRKAAKNEINILKMVKHPNILQLVDVFETRKEYFIFLEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDLMQKIKQQKgkLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFL---TQNGKVKLGDFGSARLLSNPMAF 158
Cdd:cd14088  81 ATGREVFDWILDQG--YYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYynrLKNSKIVISDFHLAKLENGLIKE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 159 ACtyvGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPF--------QANSWKNLILKVCQGCI---SPLPSHYS 227
Cdd:cd14088 159 PC---GTPEYLAPEVVGRQRYGRPVDCWAIGVIMYILLSGNPPFydeaeeddYENHDKNLFRKILAGDYefdSPYWDDIS 235
                       250       260
                ....*....|....*....|....*.
gi 23510391 228 YELQFLVKQMFKRNPSHRPSATTLLS 253
Cdd:cd14088 236 QAAKDLVTRLMEVEQDQRITAEEAIS 261
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
59-245 3.45e-18

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: 84.10  E-value: 3.45e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  59 HPNIVAFKESFEAEG-HLYIVMEYCDGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLtQ 137
Cdd:cd14109  55 HPNIVQMHDAYDDEKlAVTVIDNLASTIELVRDNLLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILL-Q 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 138 NGKVKLGDFGSARLLSNPMAFACTYvGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKV--- 214
Cdd:cd14109 134 DDKLKLADFGQSRRLLRGKLTTLIY-GSPEFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDRETLTNVrsg 212
                       170       180       190
                ....*....|....*....|....*....|..
gi 23510391 215 -CQGCISPLpSHYSYELQFLVKQMFKRNPSHR 245
Cdd:cd14109 213 kWSFDSSPL-GNISDDARDFIKKLLVYIPESR 243
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
4-197 3.66e-18

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: 85.95  E-value: 3.66e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFsnTQNSRKEAVLLAKMKHP------NIVAFKESFEAEGHLYI 77
Cdd:cd14224  67 YEVLKVIGKGSFGQVVKAYDHKTHQHVALKMVRNEKRF--HRQAAEEIRILEHLKKQdkdntmNVIHMLESFTFRNHICM 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  78 VMEYCDGgDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGK--VKLGDFGSARLLSNP 155
Cdd:cd14224 145 TFELLSM-NLYELIKKNKFQGFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRsgIKVIDFGSSCYEHQR 223
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 23510391 156 MAfacTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCT 197
Cdd:cd14224 224 IY---TYIQSRFYRAPEVILGARYGMPIDMWSFGCILAELLT 262
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
4-260 5.73e-18

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 85.31  E-value: 5.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391    4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSntqnsrkEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCD 83
Cdd:PHA03209  68 YTVIKTLTPGSEGRVFVATKPGQPDPVVLKIGQKGTTLI-------EAMLLQNVNHPSVIRMKDTLVSGAITCMVLPHYS 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   84 GgDLMQKIKQQKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARL-LSNPMAFACTy 162
Cdd:PHA03209 141 S-DLYTYLTKRSRPL-PIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLGAAQFpVVAPAFLGLA- 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  163 vGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPF----------QANSWKNLILKVCQGC-ISP--LPS----- 224
Cdd:PHA03209 218 -GTVETNAPEVLARDKYNSKADIWSAGIVLFEMLAYPSTIfedppstpeeYVKSCHSHLLKIISTLkVHPeeFPRdpgsr 296
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23510391  225 ------HYS---------------YEL----QFLVKQMFKRNPSHRPSATTLLSRGIVARL 260
Cdd:PHA03209 297 lvrgfiEYAslerqpytrypcfqrVNLpidgEFLVHKMLTFDAAMRPSAEEILNYPMFAQL 357
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
2-195 6.39e-18

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: 85.14  E-value: 6.39e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSntQNSRKEAVLLAKMKHP-----NIVAFKESFEAEGHLY 76
Cdd:cd14227  15 NTYEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYA--RQGQIEVSILARLSTEsaddyNFVRAYECFQHKNHTC 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEYCDGgDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLT----QNGKVKLGDFGSARLL 152
Cdd:cd14227  93 LVFEMLEQ-NLYDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVdpsrQPYRVKVIDFGSASHV 171
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 23510391 153 SNpmAFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYEL 195
Cdd:cd14227 172 SK--AVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAEL 212
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
8-253 7.57e-18

Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Hck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Hck is present in myeloid and lymphoid cells that play a role in the development of cancer. It may be important in the oncogenic signaling of the protein Tel-Abl, which induces a chronic myelogenous leukemia (CML)-like disease. Hck also acts as a negative regulator of G-CSF-induced proliferation of granulocytic precursors, suggesting a possible role in the development of acute myeloid leukemia (AML). In addition, Hck is essential in regulating the degranulation of polymorphonuclear leukocytes. Genetic polymorphisms affect the expression level of Hck, which affects PMN mediator release and influences the development of chronic obstructive pulmonary disease (COPD). Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Hck subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 83.54  E-value: 7.57e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFGRALLVQHESSNQMfAMKEIRlPKSFSnTQNSRKEAVLLAKMKHPNIVAFKESFEAEGhLYIVMEYCDGGDL 87
Cdd:cd05073  17 KKLGAGQFGEVWMATYNKHTKV-AVKTMK-PGSMS-VEAFLAEANVMKTLQHDKLVKLHAVVTKEP-IYIITEFMAKGSL 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  88 MQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTYVGTPY 167
Cdd:cd05073  93 LDFLKSDEGSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVIEDNEYTAREGAKFPI 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 168 -YVPPEIWENLPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQMFKRNPSHR 245
Cdd:cd05073 173 kWTAPEAINFGSFTIKSDVWSFGILLMEIVTYgRIPYPGMSNPEVIRALERGYRMPRPENCPEELYNIMMRCWKNRPEER 252

                ....*...
gi 23510391 246 PSATTLLS 253
Cdd:cd05073 253 PTFEYIQS 260
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
2-254 7.94e-18

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: 83.04  E-value: 7.94e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFG---RALLVQHES----SNQMFAMKEIRLPKSFSNTQNsrkEAVLLAKMK-HPNIVAFKESFEAEG 73
Cdd:cd14019   1 NKYRIIEKIGEGTFSsvyKAEDKLHDLydrnKGRLVALKHIYPTSSPSRILN---ELECLERLGgSNNVSGLITAFRNED 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  74 HLYIVMEYCDGGDLMQKIKqqkgKLFPEDmILNWFTQMCLGVNHIHKKRVLHRDIKSKNiFL--TQNGKVKLGDFGSARL 151
Cdd:cd14019  78 QVVAVLPYIEHDDFRDFYR----KMSLTD-IRIYLRNLFKALKHVHSFGIIHRDVKPGN-FLynRETGKGVLVDFGLAQR 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 152 LSNPMAFACTYVGTPYYVPPEIWenLPYNNKS---DIWSLGCI-LYELCTLKHPFQANSWKNLILKVCqgCISPlpshyS 227
Cdd:cd14019 152 EEDRPEQRAPRAGTRGFRAPEVL--FKCPHQTtaiDIWSAGVIlLSILSGRFPFFFSSDDIDALAEIA--TIFG-----S 222
                       250       260
                ....*....|....*....|....*..
gi 23510391 228 YELQFLVKQMFKRNPSHRPSATTLLSR 254
Cdd:cd14019 223 DEAYDLLDKLLELDPSKRITAEEALKH 249
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
2-223 1.32e-17

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: 83.57  E-value: 1.32e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSR------KEAVLLAKMKHPNIVAFKESFEAEGHL 75
Cdd:cd14041   6 DRYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIHQLNKNWRDEKKENyhkhacREYRIHKELDHPRIVKLYDYFSLDTDS 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  76 Y-IVMEYCDGGDLMQKIKQQKgkLFPEDMILNWFTQMCLGVNHIHKKR--VLHRDIKSKNIFL---TQNGKVKLGDFGSA 149
Cdd:cd14041  86 FcTVLEYCEGNDLDFYLKQHK--LMSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLvngTACGEIKITDFGLS 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 150 RLLSNP-------MAFACTYVGTPYYVPPEIW----ENLPYNNKSDIWSLGCILYELCTLKHPFQANS------WKNLIL 212
Cdd:cd14041 164 KIMDDDsynsvdgMELTSQGAGTYWYLPPECFvvgkEPPKISNKVDVWSVGVIFYQCLYGRKPFGHNQsqqdilQENTIL 243
                       250
                ....*....|.
gi 23510391 213 KVCQGCISPLP 223
Cdd:cd14041 244 KATEVQFPPKP 254
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
10-202 1.35e-17

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK1 is widely expressed and is most abundant in the testis. In hyperosmotic or hypotonic low-chloride stress conditions, WNK1 is activated and it phosphorylates its substrates including SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. Mutations in WNK1 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK1 negates WNK4-mediated inhibition of the sodium-chloride cotransporter NCC and activates the epithelial sodium channel ENaC by activating SGK1. WNK1 also decreases the surface expression of renal outer medullary potassium channel (ROMK) by stimulating their endocytosis. Hypertension and hyperkalemia in PHAII patients with WNK1 mutations may be due partly to increased activity of NCC and ENaC, and impaired renal potassium secretion by ROMK, respectively. In addition, WNK1 interacts with MEKK2/3 and acts as an activator of extracellular signal-regulated kinase (ERK) 5. It also negatively regulates TGFbeta signaling. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 83.18  E-value: 1.35e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKEIRLPK-SFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGH----LYIVMEYCDG 84
Cdd:cd14030  33 IGRGSFKTVYKGLDTETTVEVAWCELQDRKlSKSERQRFKEEAGMLKGLQHPNIVRFYDSWESTVKgkkcIVLVTELMTS 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  85 GDLMQKIKqqKGKLFPEDMILNWFTQMCLGVNHIHKKR--VLHRDIKSKNIFLT-QNGKVKLGDFGSARLlsNPMAFACT 161
Cdd:cd14030 113 GTLKTYLK--RFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLATL--KRASFAKS 188
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 23510391 162 YVGTPYYVPPEIWENlPYNNKSDIWSLGCILYELCTLKHPF 202
Cdd:cd14030 189 VIGTPEFMAPEMYEE-KYDESVDVYAFGMCMLEMATSEYPY 228
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
10-197 1.46e-17

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: 83.58  E-value: 1.46e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSN--QMFAMKEIrlpKSFSNTQNSRKEAVLLAKMKHPNIVAFKESF--EAEGHLYIVMEYCDGg 85
Cdd:cd07867  10 VGRGTYGHVYKAKRKDGKdeKEYALKQI---EGTGISMSACREIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEH- 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  86 DLMQKIK-------QQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLT----QNGKVKLGDFGSARLLSN 154
Cdd:cd07867  86 DLWHIIKfhraskaNKKPMQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMgegpERGRVKIADMGFARLFNS 165
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 23510391 155 ---PMAFACTYVGTPYYVPPEIWENLPYNNKS-DIWSLGCILYELCT 197
Cdd:cd07867 166 plkPLADLDPVVVTFWYRAPELLLGARHYTKAiDIWAIGCIFAELLT 212
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
4-195 1.53e-17

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: 83.65  E-value: 1.53e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSntQNSRKEAVLLAKMKHP-----NIVAFKESFEAEGHLYIV 78
Cdd:cd14211   1 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYA--RQGQIEVSILSRLSQEnadefNFVRAYECFQHKNHTCLV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  79 MEYCDGgDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLT----QNGKVKLGDFGSARLLSN 154
Cdd:cd14211  79 FEMLEQ-NLYDFLKQNKFSPLPLKYIRPILQQVLTALLKLKSLGLIHADLKPENIMLVdpvrQPYRVKVIDFGSASHVSK 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 23510391 155 pmAFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYEL 195
Cdd:cd14211 158 --AVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAEL 196
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
49-251 1.71e-17

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: 82.45  E-value: 1.71e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  49 KEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDLMQKIKQQKGKLFPEDMIlNWFTQMCLGVNHIHKKRVLHRDI 128
Cdd:cd05068  52 REAQIMKKLRHPKLIQLYAVCTLEEPIYIITELMKHGSLLEYLQGKGRSLQLPQLI-DMAAQVASGMAYLESQNYIHRDL 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 129 KSKNIFLTQNGKVKLGDFGSARLLSNPMAFAcTYVGTPY---YVPPEIWENLPYNNKSDIWSLGCILYELCTL-KHPFQA 204
Cdd:cd05068 131 AARNVLVGENNICKVADFGLARVIKVEDEYE-AREGAKFpikWTAPEAANYNRFSIKSDVWSFGILLTEIVTYgRIPYPG 209
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 23510391 205 NSWKNLILKVCQGCISPLPSHYSYELQFLVKQMFKRNPSHRPSATTL 251
Cdd:cd05068 210 MTNAEVLQQVERGYRMPCPPNCPPQLYDIMLECWKADPMERPTFETL 256
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
3-247 1.88e-17

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: 83.09  E-value: 1.88e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVL-RMIGEGSFGRALLVQHESSNQMFAMKEIRLP-KSFSNTQNSRKEAVLLAKM-------KHPNIVAFKESFEAEG 73
Cdd:cd05099  12 DRLVLgKPLGEGCFGQVVRAEAYGIDKSRPDQTVTVAvKMLKDNATDKDLADLISEMelmkligKHKNIINLLGVCTQEG 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  74 HLYIVMEYCDGGDLMQKIKQQK---------GKLFPEDMI-----LNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNG 139
Cdd:cd05099  92 PLYVIVEYAAKGNLREFLRARRppgpdytfdITKVPEEQLsfkdlVSCAYQVARGMEYLESRRCIHRDLAARNVLVTEDN 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 140 KVKLGDFGSARLLSNPMAFACTYVG-TPY-YVPPEIWENLPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQ 216
Cdd:cd05099 172 VMKIADFGLARGVHDIDYYKKTSNGrLPVkWMAPEALFDRVYTHQSDVWSFGILMWEIFTLgGSPYPGIPVEELFKLLRE 251
                       250       260       270
                ....*....|....*....|....*....|.
gi 23510391 217 GCISPLPSHYSYELQFLVKQMFKRNPSHRPS 247
Cdd:cd05099 252 GHRMDKPSNCTHELYMLMRECWHAVPTQRPT 282
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
10-195 2.04e-17

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: 81.80  E-value: 2.04e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKeirLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDLMQ 89
Cdd:cd14156   1 IGSGFFSKVYKVTHGATGKVMVVK---IYKNDVDQHKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCLEE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  90 kikqqkgKLFPEDMILNWFTQMCL------GVNHIHKKRVLHRDIKSKNIFLTQNGKVK---LGDFGSARLL----SNPM 156
Cdd:cd14156  78 -------LLAREELPLSWREKVELacdisrGMVYLHSKNIYHRDLNSKNCLIRVTPRGReavVTDFGLAREVgempANDP 150
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 23510391 157 AFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYEL 195
Cdd:cd14156 151 ERKLSLVGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEI 189
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
2-243 2.12e-17

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: 83.60  E-value: 2.12e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSntQNSRKEAVLLAKMKHPN-----IVAFKESFEAEGHLY 76
Cdd:cd14228  15 NSYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYA--RQGQIEVSILSRLSSENadeynFVRSYECFQHKNHTC 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEYCDGgDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLT----QNGKVKLGDFGSARLL 152
Cdd:cd14228  93 LVFEMLEQ-NLYDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVdpvrQPYRVKVIDFGSASHV 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 153 SNpmAFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQgcISPLPSHYSYELQF 232
Cdd:cd14228 172 SK--AVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQ--TQGLPAEYLLSAGT 247
                       250
                ....*....|.
gi 23510391 233 LVKQMFKRNPS 243
Cdd:cd14228 248 KTSRFFNRDPN 258
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
9-252 3.33e-17

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: 82.00  E-value: 3.33e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   9 MIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDLM 88
Cdd:cd14173   9 VLGEGAYARVQTCINLITNKEYAVKIIEKRPGHSRSRVFREVEMLYQCQGHRNVLELIEFFEEEDKFYLVFEKMRGGSIL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  89 QKIKQQKGklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFL---TQNGKVKLGDF--GSARLL---SNPMAFA- 159
Cdd:cd14173  89 SHIHRRRH--FNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCehpNQVSPVKICDFdlGSGIKLnsdCSPISTPe 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 160 -CTYVGTPYYVPPEIWENLP-----YNNKSDIWSLGCILYELCTLKHPFQAN-----SWKNliLKVCQGCISPL------ 222
Cdd:cd14173 167 lLTPCGSAEYMAPEVVEAFNeeasiYDKRCDLWSLGVILYIMLSGYPPFVGRcgsdcGWDR--GEACPACQNMLfesiqe 244
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 23510391 223 -----P----SHYSYELQFLVKQMFKRNPSHRPSATTLL 252
Cdd:cd14173 245 gkyefPekdwAHISCAAKDLISKLLVRDAKQRLSAAQVL 283
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
49-247 3.72e-17

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


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 81.31  E-value: 3.72e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  49 KEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDI 128
Cdd:cd05052  51 KEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMPYGNLLDYLRECNREELNAVVLLYMATQIASAMEYLEKKNFIHRDL 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 129 KSKNIFLTQNGKVKLGDFGSARLLSNPmafacTYVGTPYYVPPEIW---ENLPYNN---KSDIWSLGCILYELCTLK-HP 201
Cdd:cd05052 131 AARNCLVGENHLVKVADFGLSRLMTGD-----TYTAHAGAKFPIKWtapESLAYNKfsiKSDVWAFGVLLWEIATYGmSP 205
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 23510391 202 FQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQMFKRNPSHRPS 247
Cdd:cd05052 206 YPGIDLSQVYELLEKGYRMERPEGCPPKVYELMRACWQWNPSDRPS 251
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
7-197 3.75e-17

Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. Gain of function alterations, through their overexpression, deletions, or point mutations in their kinase domains, have been implicated in various cancers. These receptors are targets of many small molecule inhibitors and monoclonal antibodies used in cancer therapy. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 81.69  E-value: 3.75e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   7 LRMIGEGSFGRAL----LVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLyIVMEYC 82
Cdd:cd05057  12 GKVLGSGAFGTVYkgvwIPEGEKVKIPVAIKVLREETGPKANEEILDEAYVMASVDHPHLVRLLGICLSSQVQ-LITQLM 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  83 DGGDLMQKIKQQKGKLFPEDMiLNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSnpmAFACTY 162
Cdd:cd05057  91 PLGCLLDYVRNHRDNIGSQLL-LNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGLAKLLD---VDEKEY 166
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 23510391 163 VGTPYYVP-----PEIWENLPYNNKSDIWSLGCILYELCT 197
Cdd:cd05057 167 HAEGGKVPikwmaLESIQYRIYTHKSDVWSYGVTVWELMT 206
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
10-197 4.51e-17

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: 82.41  E-value: 4.51e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHE--SSNQMFAMKEIrlpKSFSNTQNSRKEAVLLAKMKHPNIVAFKESF--EAEGHLYIVMEYCDGg 85
Cdd:cd07868  25 VGRGTYGHVYKAKRKdgKDDKDYALKQI---EGTGISMSACREIALLRELKHPNVISLQKVFlsHADRKVWLLFDYAEH- 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  86 DLMQKIK-------QQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLT----QNGKVKLGDFGSARLLSN 154
Cdd:cd07868 101 DLWHIIKfhraskaNKKPVQLPRGMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMgegpERGRVKIADMGFARLFNS 180
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 23510391 155 ---PMAFACTYVGTPYYVPPEIWENLPYNNKS-DIWSLGCILYELCT 197
Cdd:cd07868 181 plkPLADLDPVVVTFWYRAPELLLGARHYTKAiDIWAIGCIFAELLT 227
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
10-252 5.09e-17

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: 81.99  E-value: 5.09e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHESSNQMFAMKEIRLP-KSFSNTQNSRKEAVLLAKM-------KHPNIVAFKESFEAEGHLYIVMEY 81
Cdd:cd05100  20 LGEGCFGQVVMAEAIGIDKDKPNKPVTVAvKMLKDDATDKDLSDLVSEMemmkmigKHKNIINLLGACTQDGPLYVLVEY 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDLMQKIKQQKGK---------LFPEDMI-----LNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFG 147
Cdd:cd05100 100 ASKGNLREYLRARRPPgmdysfdtcKLPEEQLtfkdlVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFG 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 148 SARLLSNPMAFACTYVGT-PY-YVPPEIWENLPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQGCISPLPS 224
Cdd:cd05100 180 LARDVHNIDYYKKTTNGRlPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLgGSPYPGIPVEELFKLLKEGHRMDKPA 259
                       250       260
                ....*....|....*....|....*...
gi 23510391 225 HYSYELQFLVKQMFKRNPSHRPSATTLL 252
Cdd:cd05100 260 NCTHELYMIMRECWHAVPSQRPTFKQLV 287
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
9-202 5.10e-17

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: 81.17  E-value: 5.10e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   9 MIGEGSFGRALLVQHESSNQMFAMKEIRL-PKSFSNTQ------NSRKEAVLLAKMK-HPNIVAFKESFEAEGHLYIVMe 80
Cdd:cd14181  17 VIGRGVSSVVRRCVHRHTGQEFAVKIIEVtAERLSPEQleevrsSTLKEIHILRQVSgHPSIITLIDSYESSTFIFLVF- 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  81 ycdggDLMQKikqqkGKLF---PEDMILNWFTQMCL------GVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARL 151
Cdd:cd14181  96 -----DLMRR-----GELFdylTEKVTLSEKETRSImrslleAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFSCH 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 23510391 152 LSnPMAFACTYVGTPYYVPPEIW-----ENLP-YNNKSDIWSLGCILYELCTLKHPF 202
Cdd:cd14181 166 LE-PGEKLRELCGTPGYLAPEILkcsmdETHPgYGKEVDLWACGVILFTLLAGSPPF 221
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
49-251 6.19e-17

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


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 80.44  E-value: 6.19e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  49 KEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDLMQKIKQQKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDI 128
Cdd:cd05085  42 SEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVPGGDFLSFLRKKKDEL-KTKQLVKFSLDAAAGMAYLESKNCIHRDL 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 129 KSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTYVGTPY-YVPPEIWENLPYNNKSDIWSLGCILYELCTLKH-PFQANS 206
Cdd:cd05085 121 AARNCLVGENNALKISDFGMSRQEDDGVYSSSGLKQIPIkWTAPEALNYGRYSSESDVWSFGILLWETFSLGVcPYPGMT 200
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 23510391 207 WKNLILKVCQGCISPLPSHYSYELQFLVKQMFKRNPSHRPSATTL 251
Cdd:cd05085 201 NQQAREQVEKGYRMSAPQRCPEDIYKIMQRCWDYNPENRPKFSEL 245
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
3-245 8.58e-17

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


Pssm-ID: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 80.82  E-value: 8.58e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFGRALLVQ----HESSNQMF-AMKEIRLPkSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYI 77
Cdd:cd05094   6 DIVLKRELGEGAFGKVFLAEcynlSPTKDKMLvAVKTLKDP-TLAARKDFQREAELLTNLQHDHIVKFYGVCGDGDPLIM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  78 VMEYCDGGDLMQKIK---------------QQKGKLFPEDMiLNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVK 142
Cdd:cd05094  85 VFEYMKHGDLNKFLRahgpdamilvdgqprQAKGELGLSQM-LHIATQIASGMVYLASQHFVHRDLATRNCLVGANLLVK 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 143 LGDFGSAR-LLSNPMAFACTYVGTPY-YVPPEIWENLPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQGCI 219
Cdd:cd05094 164 IGDFGMSRdVYSTDYYRVGGHTMLPIrWMPPESIMYRKFTTESDVWSFGVILWEIFTYgKQPWFQLSNTEVIECITQGRV 243
                       250       260
                ....*....|....*....|....*.
gi 23510391 220 SPLPSHYSYELQFLVKQMFKRNPSHR 245
Cdd:cd05094 244 LERPRVCPKEVYDIMLGCWQREPQQR 269
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
4-247 1.11e-16

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: 79.61  E-value: 1.11e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIrlPKSFSNTQNSRK------EAVLLAKMKHP--NIVAFKESFEAEGHL 75
Cdd:cd14102   2 YQVGSVLGSGGFGTVYAGSRIADGLPVAVKHV--VKERVTEWGTLNgvmvplEIVLLKKVGSGfrGVIKLLDWYERPDGF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  76 YIVMEYCD-GGDLMQKIKQqKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFL-TQNGKVKLGDFGSARLLS 153
Cdd:cd14102  80 LIVMERPEpVKDLFDFITE-KGAL-DEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVdLRTGELKLIDFGSGALLK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 154 NPMafACTYVGTPYYVPPEIWENLPYNNKS-DIWSLGCILYELCTLKHPFQANSwknlilKVCQGCISpLPSHYSYELQF 232
Cdd:cd14102 158 DTV--YTDFDGTRVYSPPEWIRYHRYHGRSaTVWSLGVLLYDMVCGDIPFEQDE------EILRGRLY-FRRRVSPECQQ 228
                       250
                ....*....|....*
gi 23510391 233 LVKQMFKRNPSHRPS 247
Cdd:cd14102 229 LIKWCLSLRPSDRPT 243
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
8-247 1.16e-16

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: 80.39  E-value: 1.16e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFGR-----ALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYC 82
Cdd:cd05045   6 KTLGEGEFGKvvkatAFRLKGRAGYTTVAVKMLKENASSSELRDLLSEFNLLKQVNHPHVIKLYGACSQDGPLLLIVEYA 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  83 DGGDLMQKIKQQK---------------GKLFPED-------MILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGK 140
Cdd:cd05045  86 KYGSLRSFLRESRkvgpsylgsdgnrnsSYLDNPDeraltmgDLISFAWQISRGMQYLAEMKLVHRDLAARNVLVAEGRK 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 141 VKLGDFGSARLLSNPMAFACTYVG-TPY-YVPPEIWENLPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQG 217
Cdd:cd05045 166 MKISDFGLSRDVYEEDSYVKRSKGrIPVkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLgGNPYPGIAPERLFNLLKTG 245
                       250       260       270
                ....*....|....*....|....*....|
gi 23510391 218 CISPLPSHYSYELQFLVKQMFKRNPSHRPS 247
Cdd:cd05045 246 YRMERPENCSEEMYNLMLTCWKQEPDKRPT 275
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
10-247 1.28e-16

Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TNNI3K, also called cardiac ankyrin repeat kinase (CARK), is a cardiac-specific troponin I-interacting kinase that promotes cardiac myogenesis, improves cardiac performance, and protects the myocardium from ischemic injury. It contains N-terminal ankyrin repeats, a catalytic kinase domain, and a C-terminal serine-rich domain. TNNI3K exerts a disease-accelerating effect on cardiac dysfunction and reduced survival in mouse models of cardiomyopathy. The TNNI3K subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 79.50  E-value: 1.28e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRalLVQHESSNQMFAMKEIRlpksfSNTQNSR-------KEAVLLAKMKHPNIVAF-KESFEAEGHLYIVMEY 81
Cdd:cd14064   1 IGSGSFGK--VYKGRCRNKIVAIKRYR-----ANTYCSKsdvdmfcREVSILCRLNHPCVIQFvGACLDDPSQFAIVTQY 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  82 CDGGDLMQKIKQQKGKLFPED-MILNwfTQMCLGVNHIHK--KRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAF 158
Cdd:cd14064  74 VSGGSLFSLLHEQKRVIDLQSkLIIA--VDVAKGMEYLHNltQPIIHRDLNSHNILLYEDGHAVVADFGESRFLQSLDED 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 159 ACT-YVGTPYYVPPEIW-ENLPYNNKSDIWSLGCILYELCTLKHPFQ----ANSWKNLILKVCQgciSPLPSHYSYELQF 232
Cdd:cd14064 152 NMTkQPGNLRWMAPEVFtQCTRYSIKADVFSYALCLWELLTGEIPFAhlkpAAAAADMAYHHIR---PPIGYSIPKPISS 228
                       250
                ....*....|....*
gi 23510391 233 LVKQMFKRNPSHRPS 247
Cdd:cd14064 229 LLMRGWNAEPESRPS 243
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
4-199 1.49e-16

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: 80.34  E-value: 1.49e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHES-SNQMFAMKEIRLPKSFSNTqnSRKEAVLLAKM--------KHpnIVAFKESFEAEGH 74
Cdd:cd14135   2 YRVYGYLGKGVFSNVVRARDLArGNQEVAIKIIRNNELMHKA--GLKELEILKKLndadpddkKH--CIRLLRHFEHKNH 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  75 LYIVMEYCDGG--DLMQKIKQQKGklfpedmiLN------WFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKV-KLGD 145
Cdd:cd14135  78 LCLVFESLSMNlrEVLKKYGKNVG--------LNikavrsYAQQLFLALKHLKKCNILHADIKPDNILVNEKKNTlKLCD 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 146 FGSARLLS-NPMafactyvgTPY-----YVPPEIWENLPYNNKSDIWSLGCILYELCTLK 199
Cdd:cd14135 150 FGSASDIGeNEI--------TPYlvsrfYRAPEIILGLPYDYPIDMWSVGCTLYELYTGK 201
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
4-213 2.24e-16

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: 79.72  E-value: 2.24e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSR------KEAVLLAKMKHPNIVAFKESFEAEGHLY- 76
Cdd:cd14040   8 YLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKENyhkhacREYRIHKELDHPRIVKLYDYFSLDTDTFc 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEYCDGGDLMQKIKQQKgkLFPEDMILNWFTQMCLGVNHIH--KKRVLHRDIKSKNIFL---TQNGKVKLGDFGSARL 151
Cdd:cd14040  88 TVLEYCEGNDLDFYLKQHK--LMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLvdgTACGEIKITDFGLSKI 165
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23510391 152 LSNP------MAFACTYVGTPYYVPPEIW----ENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILK 213
Cdd:cd14040 166 MDDDsygvdgMDLTSQGAGTYWYLPPECFvvgkEPPKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQ 237
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
10-254 2.59e-16

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkA is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkA to its ligand, nerve growth factor (NGF), results in receptor oligomerization and activation of the catalytic domain. TrkA is expressed mainly in neural-crest-derived sensory and sympathetic neurons of the peripheral nervous system, and in basal forebrain cholinergic neurons of the central nervous system. It is critical for neuronal growth, differentiation and survival. Alternative TrkA splicing has been implicated as a pivotal regulator of neuroblastoma (NB) behavior. Normal TrkA expression is associated with better NB prognosis, while the hypoxia-regulated TrkAIII splice variant promotes NB pathogenesis and progression. Aberrant TrkA expression has also been demonstrated in non-neural tumors including prostate, breast, lung, and pancreatic cancers. The TrkA 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: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 79.24  E-value: 2.59e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQ-----HESSNQMFAMKEIRlPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDG 84
Cdd:cd05092  13 LGEGAFGKVFLAEchnllPEQDKMLVAVKALK-EATESARQDFQREAELLTVLQHQHIVRFYGVCTEGEPLIMVFEYMRH 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  85 GDLMQKIK--------------QQKGKLFPEDMiLNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSAR 150
Cdd:cd05092  92 GDLNRFLRshgpdakildggegQAPGQLTLGQM-LQIASQIASGMVYLASLHFVHRDLATRNCLVGQGLVVKIGDFGMSR 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 151 LLSNpmafactyvgTPYY------------VPPEIWENLPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQG 217
Cdd:cd05092 171 DIYS----------TDYYrvggrtmlpirwMPPESILYRKFTTESDIWSFGVVLWEIFTYgKQPWYQLSNTEAIECITQG 240
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 23510391 218 CISPLPSHYSYELQFLVKQMFKRNPSHRPSATTLLSR 254
Cdd:cd05092 241 RELERPRTCPPEVYAIMQGCWQREPQQRHSIKDIHSR 277
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
4-221 2.59e-16

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 81.24  E-value: 2.59e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391    4 YMVLRMIGEGSFGrallVQHES----SNQMFAMKeirlpKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEG------ 73
Cdd:PTZ00036  68 YKLGNIIGNGSFG----VVYEAicidTSEKVAIK-----KVLQDPQYKNRELLIMKNLNHINIIFLKDYYYTECfkknek 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   74 --HLYIVMEYcdggdLMQKIKQ------QKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNG-KVKLG 144
Cdd:PTZ00036 139 niFLNVVMEF-----IPQTVHKymkhyaRNNHALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDPNThTLKLC 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  145 DFGSAR-LLSNPMafACTYVGTPYYVPPEIW-ENLPYNNKSDIWSLGCILYELcTLKHP-FQANSWKNLILKVCQGCISP 221
Cdd:PTZ00036 214 DFGSAKnLLAGQR--SVSYICSRFYRAPELMlGATNYTTHIDLWSLGCIIAEM-ILGYPiFSGQSSVDQLVRIIQVLGTP 290
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
27-248 3.04e-16

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


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 78.59  E-value: 3.04e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  27 NQMFAMKEIRlpKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDLmQKIkqqkgkLFPEDMILN 106
Cdd:cd13992  25 GRTVAIKHIT--FSRTEKRTILQELNQLKELVHDNLNKFIGICINPPNIAVVTEYCTRGSL-QDV------LLNREIKMD 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 107 WFTQMCL------GVNHIHKKR-VLHRDIKSKNIFLTQNGKVKLGDFGSARLLSN--PMAFACTYVGTPY-YVPPEI--W 174
Cdd:cd13992  96 WMFKSSFikdivkGMNYLHSSSiGYHGRLKSSNCLVDSRWVVKLTDFGLRNLLEEqtNHQLDEDAQHKKLlWTAPELlrG 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 175 ENLPYNN--KSDIWSLGCILYELCTLKHPFqANSWKNLILKVCQGCISPLPS---HYSY-----ELQFLVKQMFKRNPSH 244
Cdd:cd13992 176 SLLEVRGtqKGDVYSFAIILYEILFRSDPF-ALEREVAIVEKVISGGNKPFRpelAVLLdefppRLVLLVKQCWAENPEK 254

                ....
gi 23510391 245 RPSA 248
Cdd:cd13992 255 RPSF 258
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
4-245 3.33e-16

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: 79.51  E-value: 3.33e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRAL-LVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPN----IVAFKESFEAEGHLYIV 78
Cdd:cd14213  14 YEIVDTLGEGAFGKVVeCIDHKMGGMHVAVKIVKNVDRYREAARSEIQVLEHLNTTDPNstfrCVQMLEWFDHHGHVCIV 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  79 MEYCdGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQ-------------------NG 139
Cdd:cd14213  94 FELL-GLSTYDFIKENSFLPFPIDHIRNMAYQICKSVNFLHHNKLTHTDLKPENILFVQsdyvvkynpkmkrdertlkNP 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 140 KVKLGDFGSARLLSNpmaFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLiLKVCQGCI 219
Cdd:cd14213 173 DIKVVDFGSATYDDE---HHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFQTHDSKEH-LAMMERIL 248
                       250       260
                ....*....|....*....|....*.
gi 23510391 220 SPLPSHysyelqfLVKQMFKRNPSHR 245
Cdd:cd14213 249 GPLPKH-------MIQKTRKRKYFHH 267
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
59-252 3.41e-16

Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB3 binds and regulates ATF4, p65/RelA, and PKB (or Akt). It negatively regulates ATF4-mediated gene expression including that of CHOP (C/EBP homologous protein) and HO-1, which are both involved in modulating apoptosis. It also inhibits insulin-mediated phosphorylation of PKB and is a possible determinant of insulin resistance and related disorders. In osteoarthritic chondrocytes where it inhibits insulin-like growth factor 1-mediated cell survival, TRB3 is overexpressed, resulting in increased cell death. TRB3 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB3 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 78.00  E-value: 3.41e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  59 HPNIVAFKESFEAEGHLYIVMEYcDGGDLMQKIKQQKGklFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLT-- 136
Cdd:cd14024  44 HEGVCSVLEVVIGQDRAYAFFSR-HYGDMHSHVRRRRR--LSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTde 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 137 QNGKVKLGDFGSARLLSNPMAFACTYVGTPYYVPPEIWEN-LPYNNK-SDIWSLGCILYELCTLKHPFQANSWKNLILKV 214
Cdd:cd14024 121 LRTKLVLVNLEDSCPLNGDDDSLTDKHGCPAYVGPEILSSrRSYSGKaADVWSLGVCLYTMLLGRYPFQDTEPAALFAKI 200
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 23510391 215 CQGCISpLPSHYSYELQFLVKQMFKRNPSHRPSATTLL 252
Cdd:cd14024 201 RRGAFS-LPAWLSPGARCLVSCMLRRSPAERLKASEIL 237
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
1-197 4.47e-16

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: 79.29  E-value: 4.47e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   1 MDDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNtqNSRKEAVLLAKM-KHP-----NIVAFKESFEAEGH 74
Cdd:cd14226  12 MDRYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKIIKNKKAFLN--QAQIEVRLLELMnKHDtenkyYIVRLKRHFMFRNH 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  75 LYIVME---YcdggDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKK--RVLHRDIKSKNIFLTqNGK---VKLGDF 146
Cdd:cd14226  90 LCLVFEllsY----NLYDLLRNTNFRGVSLNLTRKFAQQLCTALLFLSTPelSIIHCDLKPENILLC-NPKrsaIKIIDF 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 23510391 147 GSARLLSNPMAfacTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCT 197
Cdd:cd14226 165 GSSCQLGQRIY---QYIQSRFYRSPEVLLGLPYDLAIDMWSLGCILVEMHT 212
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
4-197 5.57e-16

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: 78.77  E-value: 5.57e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFsnTQNSRKEAVLL-----AKMKHP---NIVAFKESFEAEG-- 73
Cdd:cd14136  12 YHVVRKLGWGHFSTVWLCWDLQNKRFVALKVVKSAQHY--TEAALDEIKLLkcvreADPKDPgreHVVQLLDDFKHTGpn 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  74 --HLYIVMEYCdGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKK-RVLHRDIKSKNIFLT-QNGKVKLGDFGSA 149
Cdd:cd14136  90 gtHVCMVFEVL-GPNLLKLIKRYNYRGIPLPLVKKIARQVLQGLDYLHTKcGIIHTDIKPENVLLCiSKIEVKIADLGNA 168
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 23510391 150 rllsnpmafaC-TY------VGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCT 197
Cdd:cd14136 169 ----------CwTDkhftedIQTRQYRSPEVILGAGYGTPADIWSTACMAFELAT 213
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
59-252 5.66e-16

Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Tribbles Homolog (TRB) proteins interact with many proteins involved in signaling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, differentiation, and gene expression. TRB proteins bind to the middle kinase in mitogen activated protein kinase (MAPK) signaling cascades, MAPK kinases. They regulate the activity of MAPK kinases, and thus, affect MAPK signaling. In Drosophila, Tribbles regulates String, the ortholog of mammalian Cdc25, during morphogenesis. String is implicated in the progression of mitosis during embryonic development. Vertebrates contain three TRB proteins encoded by three separate genes: Tribbles-1 (TRB1 or TRIB1), Tribbles-2 (TRB2 or TRIB2), and Tribbles-3 (TRB3 or TRIB3). The TRB 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: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 77.47  E-value: 5.66e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  59 HPNIVAFKESFEAEGHLYIVMEYcDGGDLMQKIKQQKGKLFPEDMILnwFTQMCLGVNHIHKKRVLHRDIK-SKNIFLT- 136
Cdd:cd13976  44 HPNISGVHEVIAGETKAYVFFER-DHGDLHSYVRSRKRLREPEAARL--FRQIASAVAHCHRNGIVLRDLKlRKFVFADe 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 137 QNGKVKLGDFGSARLLSNPMAFACTYVGTPYYVPPEIWE-NLPYNNK-SDIWSLGCILYELCTLKHPFQANSWKNLILKV 214
Cdd:cd13976 121 ERTKLRLESLEDAVILEGEDDSLSDKHGCPAYVSPEILNsGATYSGKaADVWSLGVILYTMLVGRYPFHDSEPASLFAKI 200
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 23510391 215 CQGCISpLPSHYSYELQFLVKQMFKRNPSHRPSATTLL 252
Cdd:cd13976 201 RRGQFA-IPETLSPRARCLIRSLLRREPSERLTAEDIL 237
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
23-253 6.17e-16

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: 78.03  E-value: 6.17e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  23 HESSNQMFAMKEIRLPKSFSNT--------QNSRKEAVLLAKMK-HPNIVAFKESFEAEGHLYIVMEYCDGGDLMQKIKQ 93
Cdd:cd14182  24 HKPTRQEYAVKIIDITGGGSFSpeevqelrEATLKEIDILRKVSgHPNIIQLKDTYETNTFFFLVFDLMKKGELFDYLTE 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  94 QKgkLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGsarllsnpmaFACTY---------VG 164
Cdd:cd14182 104 KV--TLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFG----------FSCQLdpgeklrevCG 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 165 TPYYVPPEIWE-----NLP-YNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCI---SPLPSHYSYELQFLVK 235
Cdd:cd14182 172 TPGYLAPEIIEcsmddNHPgYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGNYqfgSPEWDDRSDTVKDLIS 251
                       250
                ....*....|....*...
gi 23510391 236 QMFKRNPSHRPSATTLLS 253
Cdd:cd14182 252 RFLVVQPQKRYTAEEALA 269
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
2-251 6.19e-16

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: 78.23  E-value: 6.19e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKM-------KHPNIVAFKESFEAEGH 74
Cdd:cd05053  12 DRLTLGKPLGEGAFGQVVKAEAVGLDNKPNEVVTVAVKMLKDDATEKDLSDLVSEMemmkmigKHKNIINLLGACTQDGP 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  75 LYIVMEYCDGGDLMQKIKQQK---------GKLFPEDMILNW-FTQMCL----GVNHIHKKRVLHRDIKSKNIFLTQNGK 140
Cdd:cd05053  92 LYVVVEYASKGNLREFLRARRppgeeaspdDPRVPEEQLTQKdLVSFAYqvarGMEYLASKKCIHRDLAARNVLVTEDNV 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 141 VKLGDFGSARLLSNPMAFACTYVG-TPY-YVPPEIWENLPYNNKSDIWSLGCILYELCTLK-HPFQANSWKNLILKVCQG 217
Cdd:cd05053 172 MKIADFGLARDIHHIDYYRKTTNGrLPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGgSPYPGIPVEELFKLLKEG 251
                       250       260       270
                ....*....|....*....|....*....|....
gi 23510391 218 CISPLPSHYSYELQFLVKQMFKRNPSHRPSATTL 251
Cdd:cd05053 252 HRMEKPQNCTQELYMLMRDCWHEVPSQRPTFKQL 285
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
4-254 7.92e-16

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: 78.37  E-value: 7.92e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLpKSFSNTQNSRKE--AVLLAKMKHPNIVAFKE-------------- 67
Cdd:cd13977   2 YSLIREVGRGSYGVVYEAVVRRTGARVAVKKIRC-NAPENVELALREfwALSSIQRQHPNVIQLEEcvlqrdglaqrmsh 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  68 ----------------------SFEAEGHLYIVMEYCDGGDLMQKIKQQKgklfPEDMILNWFT-QMCLGVNHIHKKRVL 124
Cdd:cd13977  81 gssksdlylllvetslkgercfDPRSACYLWFVMEFCDGGDMNEYLLSRR----PDRQTNTSFMlQLSSALAFLHRNQIV 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 125 HRDIKSKNIFLTQNGK---VKLGDFGSARLLS----NPMA-------FACTYVGTPYYVPPEIWENlPYNNKSDIWSLGC 190
Cdd:cd13977 157 HRDLKPDNILISHKRGepiLKVADFGLSKVCSgsglNPEEpanvnkhFLSSACGSDFYMAPEVWEG-HYTAKADIFALGI 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 191 ILYELCTLKHPFQANSWKNLI-LKVCQGC-ISPL------------------PSHYSYELQFLVKQMFKRNPSHRPSATT 250
Cdd:cd13977 236 IIWAMVERITFRDGETKKELLgTYIQQGKeIVPLgeallenpklelqiplkkKKSMNDDMKQLLRDMLAANPQERPDAFQ 315

                ....
gi 23510391 251 LLSR 254
Cdd:cd13977 316 LELR 319
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
8-245 8.51e-16

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkB is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkB to its ligands, brain-derived neurotrophic factor (BDNF) or neurotrophin 4 (NT4), results in receptor oligomerization and activation of the catalytic domain. TrkB is broadly expressed in the nervous system and in some non-neural tissues. It plays important roles in cell proliferation, differentiation, and survival. BDNF/Trk signaling plays a key role in regulating activity-dependent synaptic plasticity. TrkB also contributes to protection against gp120-induced neuronal cell death. TrkB overexpression is associated with poor prognosis in neuroblastoma (NB) and other human cancers. It acts as a suppressor of anoikis (detachment-induced apoptosis) and contributes to tumor metastasis. The TrkB 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: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 77.77  E-value: 8.51e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFGRALLVQ-----HESSNQMFAMKEIRlPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYC 82
Cdd:cd05093  11 RELGEGAFGKVFLAEcynlcPEQDKILVAVKTLK-DASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYM 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  83 DGGDLMQKIK------------QQKGKLFPEDMiLNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSAR 150
Cdd:cd05093  90 KHGDLNKFLRahgpdavlmaegNRPAELTQSQM-LHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 151 -LLSNPMAFACTYVGTPY-YVPPEIWENLPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQGCISPLPSHYS 227
Cdd:cd05093 169 dVYSTDYYRVGGHTMLPIrWMPPESIMYRKFTTESDVWSLGVVLWEIFTYgKQPWYQLSNNEVIECITQGRVLQRPRTCP 248
                       250
                ....*....|....*...
gi 23510391 228 YELQFLVKQMFKRNPSHR 245
Cdd:cd05093 249 KEVYDLMLGCWQREPHMR 266
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
32-254 1.64e-15

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: 76.54  E-value: 1.64e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  32 MKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVA----------FKESFEAEGHLYIVMEYcdggdlmqkiKQQKGKLFPE 101
Cdd:cd14067  42 LKHLRAADAMKNFSEFRQEASMLHSLQHPCIVYligisihplcFALELAPLGSLNTVLEE----------NHKGSSFMPL 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 102 DMILNWFT--QMCLGVNHIHKKRVLHRDIKSKNIFL-----TQNGKVKLGDFGSARLLSNPMAFACTyvGTPYYVPPEIW 174
Cdd:cd14067 112 GHMLTFKIayQIAAGLAYLHKKNIIFCDLKSDNILVwsldvQEHINIKLSDYGISRQSFHEGALGVE--GTPGYQAPEIR 189
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 175 ENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGcISPL---PSHYS-YELQFLVKQMFKRNPSHRPSATT 250
Cdd:cd14067 190 PRIVYDEKVDMFSYGMVLYELLSGQRPSLGHHQLQIAKKLSKG-IRPVlgqPEEVQfFRLQALMMECWDTKPEKRPLACS 268

                ....
gi 23510391 251 LLSR 254
Cdd:cd14067 269 VVEQ 272
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
7-254 2.36e-15

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: 76.26  E-value: 2.36e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   7 LRMIGEGSFGRA-----LLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAF-----KES-----FE- 70
Cdd:cd05048  10 LEELGEGAFGKVykgelLGPSSEESAISVAIKTLKENASPKTQQDFRREAELMSDLQHPNIVCLlgvctKEQpqcmlFEy 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  71 -AEG--HLYIVME--YCDGGdLMQKIKQQKGKLFPEDMiLNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGD 145
Cdd:cd05048  90 mAHGdlHEFLVRHspHSDVG-VSSDDDGTASSLDQSDF-LHIAIQIAAGMEYLSSHHYVHRDLAARNCLVGDGLTVKISD 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 146 FGSARLLsnpmafactYVGTPYYV-----------PPEIWENLPYNNKSDIWSLGCILYELCTLK-HPFQANSWKNLILK 213
Cdd:cd05048 168 FGLSRDI---------YSSDYYRVqsksllpvrwmPPEAILYGKFTTESDVWSFGVVLWEIFSYGlQPYYGYSNQEVIEM 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 23510391 214 VCQGCISPLPSHYSYELQFLVKQMFKRNPSHRPSATTLLSR 254
Cdd:cd05048 239 IRSRQLLPCPEDCPARVYSLMVECWHEIPSRRPRFKEIHTR 279
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
8-247 2.40e-15

Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of RIP4, ankyrin (ANK) repeat and kinase domain containing 1 (ANKK1), and similar proteins, all of which harbor C-terminal ANK repeats. RIP4, also called Protein Kinase C-associated kinase (PKK), regulates keratinocyte differentiation and cutaneous inflammation. It activates NF-kappaB and is important in the survival of diffuse large B-cell lymphoma cells. The ANKK1 protein, also called PKK2, has not been studied extensively. The ANKK1 gene, located less than 10kb downstream of the D2 dopamine receptor (DRD2) locus, is altered in the Taq1 A1 polymorphism, which is related to a reduced DRD2 binding affinity and consequently, to mental disorders. The RIP4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 75.99  E-value: 2.40e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFGRALLVQHESSNQMFAMKeirLPKSFSNTQNSR----KEAVLLAKMKHPNIVA-FKESFEAEGhlyIVMEYC 82
Cdd:cd14025   2 EKVGSGGFGQVYKVRHKHWKTWLAIK---CPPSLHVDDSERmellEEAKKMEMAKFRHILPvYGICSEPVG---LVMEYM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  83 DGGDLMQKIKQQKgklFPEDMILNWFTQMCLGVNHIH--KKRVLHRDIKSKNIFLTQNGKVKLGDFGSARL--LSNPMAF 158
Cdd:cd14025  76 ETGSLEKLLASEP---LPWELRFRIIHETAVGMNFLHcmKPPLLHLDLKPANILLDAHYHVKISDFGLAKWngLSHSHDL 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 159 AC-TYVGTPYYVPPE--IWENLPYNNKSDIWSLGCILYELCTLKHPFQanSWKNL---ILKVCQG---CISPLPSHYSYE 229
Cdd:cd14025 153 SRdGLRGTIAYLPPErfKEKNRCPDTKHDVYSFAIVIWGILTQKKPFA--GENNIlhiMVKVVKGhrpSLSPIPRQRPSE 230
                       250       260
                ....*....|....*....|.
gi 23510391 230 LQFLVKQM---FKRNPSHRPS 247
Cdd:cd14025 231 CQQMICLMkrcWDQDPRKRPT 251
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
7-252 2.48e-15

Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB1 interacts directly with the mitogen activated protein kinase (MAPK) kinase MKK4, an activator of JNK. It regulates vascular smooth muscle cell proliferation and chemotaxis through the JNK signaling pathway. It is found to be down-regulated in human acute myeloid leukaemia (AML) and may play a role in the pathogenesis of the disease. It has also been identified as a potential biomarker for antibody-mediated allograft failure. TRB1 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 TRB1 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: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 75.47  E-value: 2.48e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   7 LRMIGEGSFGRALLVqHESSNQMFAMKEIRlpksfsNTQNSRKEAVLLAKmkHPNIVAFKESFEAEGHLYIVMEYcDGGD 86
Cdd:cd14023   1 LPTGGREHVYRALQL-HSGAELQCKVFPLK------HYQDKIRPYIQLPS--HRNITGIVEVILGDTKAYVFFEK-DFGD 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  87 LMQKIKQQKgkLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIK-SKNIFLT-QNGKVKLGDFGSARLLSNPMAFACTYVG 164
Cdd:cd14023  71 MHSYVRSCK--RLREEEAARLFKQIVSAVAHCHQSAIVLGDLKlRKFVFSDeERTQLRLESLEDTHIMKGEDDALSDKHG 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 165 TPYYVPPEIWENL-PYNNKS-DIWSLGCILYELCTLKHPFQANSWKNLILKVCQG--CIsplPSHYSYELQFLVKQMFKR 240
Cdd:cd14023 149 CPAYVSPEILNTTgTYSGKSaDVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGqfCI---PDHVSPKARCLIRSLLRR 225
                       250
                ....*....|..
gi 23510391 241 NPSHRPSATTLL 252
Cdd:cd14023 226 EPSERLTAPEIL 237
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
13-245 2.63e-15

Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RPK118 contains an N-terminal Phox homology (PX) domain, a Microtubule Interacting and Trafficking (MIT) domain, and a kinase domain containing a long uncharacterized insert. Also included in the family is human RPK60 (or ribosomal protein S6 kinase-like 1), which also contains MIT and kinase domains but lacks a PX domain. RPK118 binds sphingosine kinase, a key enzyme in the synthesis of sphingosine 1-phosphate (SPP), a lipid messenger involved in many cellular events. RPK118 may be involved in transmitting SPP-mediated signaling. RPK118 also binds the antioxidant peroxiredoxin-3. RPK118 may be involved in the transport of PRDX3 from the cytoplasm to its site of function in the mitochondria. The RPK118-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: 270728 [Multi-domain]  Cd Length: 265  Bit Score: 76.05  E-value: 2.63e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  13 GSFGRALLVQHESSNQMFAMKEirLPKSfsnTQNSRKEAVLLAKMKhPNIVAFKESFEAEGHLYIVMEYCDGGDLMQKI- 91
Cdd:cd05576  10 GVIDKVLLVMDTRTQETFILKG--LRKS---SEYSRERKTIIPRCV-PNMVCLRKYIISEESVFLVLQHAEGGKLWSYLs 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  92 KQQKGK----LF---------------PEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLL 152
Cdd:cd05576  84 KFLNDKeihqLFadlderlaaasrfyiPEECIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEV 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 153 SNPmafACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLK-----HPFQANSWKNLilkvcqgcisPLPSHYS 227
Cdd:cd05576 164 EDS---CDSDAIENMYCAPEVGGISEETEACDWWSLGALLFELLTGKalvecHPAGINTHTTL----------NIPEWVS 230
                       250
                ....*....|....*...
gi 23510391 228 YELQFLVKQMFKRNPSHR 245
Cdd:cd05576 231 EEARSLLQQLLQFNPTER 248
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
9-252 2.78e-15

Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie2 is a receptor PTK (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie2 is expressed mainly in endothelial cells and hematopoietic stem cells. It is also found in a subset of tumor-associated monocytes and eosinophils. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. Tie2 signaling plays key regulatory roles in vascular integrity and quiescence, and in inflammation. The Tie2 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: 133219 [Multi-domain]  Cd Length: 303  Bit Score: 76.57  E-value: 2.78e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   9 MIGEGSFGRAL--LVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKM-KHPNIVAFKESFEAEGHLYIVMEYCDGG 85
Cdd:cd05088  14 VIGEGNFGQVLkaRIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPHG 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  86 DLMQKIKQQK--------------GKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARL 151
Cdd:cd05088  94 NLLDFLRKSRvletdpafaianstASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRG 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 152 LSnpmafacTYVGTPYYVPPEIW---ENLPYN---NKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQGCISPLPS 224
Cdd:cd05088 174 QE-------VYVKKTMGRLPVRWmaiESLNYSvytTNSDVWSYGVLLWEIVSLgGTPYCGMTCAELYEKLPQGYRLEKPL 246
                       250       260
                ....*....|....*....|....*...
gi 23510391 225 HYSYELQFLVKQMFKRNPSHRPSATTLL 252
Cdd:cd05088 247 NCDDEVYDLMRQCWREKPYERPSFAQIL 274
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
2-248 3.31e-15

Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Musk is a receptor PTK (RTK) containing an extracellular region with four immunoglobulin-like domains and a cysteine-rich cluster, a transmembrane segment, and an intracellular catalytic domain. Musk is expressed and concentrated in the postsynaptic membrane in skeletal muscle. It is essential for the establishment of the neuromuscular junction (NMJ), a peripheral synapse that conveys signals from motor neurons to muscle cells. Agrin, a large proteoglycan released from motor neurons, stimulates Musk autophosphorylation and activation, leading to the clustering of acetylcholine receptors (AChRs). To date, there is no evidence to suggest that agrin binds directly to Musk. Mutations in AChR, Musk and other partners are responsible for diseases of the NMJ, such as the autoimmune syndrome myasthenia gravis. The Musk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 76.02  E-value: 3.31e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   2 DDYMVLRMIGEGSFGRAL------LVQHESsNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHL 75
Cdd:cd05050   5 NNIEYVRDIGQGAFGRVFqarapgLLPYEP-FTMVAVKMLKEEASADMQADFQREAALMAEFDHPNIVKLLGVCAVGKPM 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  76 YIVMEYCDGGDLMQKIKQQ-------------KGKLFPEDMI-LNWFTQMCL------GVNHIHKKRVLHRDIKSKNIFL 135
Cdd:cd05050  84 CLLFEYMAYGDLNEFLRHRspraqcslshstsSARKCGLNPLpLSCTEQLCIakqvaaGMAYLSERKFVHRDLATRNCLV 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 136 TQNGKVKLGDFGsarlLSNPMAFACTYVGTP------YYVPPE-IWENlPYNNKSDIWSLGCILYELCTLK-HPFQANSW 207
Cdd:cd05050 164 GENMVVKIADFG----LSRNIYSADYYKASEndaipiRWMPPEsIFYN-RYTTESDVWAYGVVLWEIFSYGmQPYYGMAH 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 23510391 208 KNLILKVCQGCISPLPSHYSYELQFLVKQMFKRNPSHRPSA 248
Cdd:cd05050 239 EEVIYYVRDGNVLSCPDNCPLELYNLMRLCWSKLPSDRPSF 279
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
8-246 4.20e-15

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The EphA2 receptor is overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 75.40  E-value: 4.20e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFG---RALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDG 84
Cdd:cd05063  11 KVIGAGEFGevfRGILKMPGRKEVAVAIKTLKPGYTEKQRQDFLSEASIMGQFSHHNIIRLEGVVTKFKPAMIITEYMEN 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  85 GDLMQKIKQQKGKlFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSN-PMAfacTYV 163
Cdd:cd05063  91 GALDKYLRDHDGE-FSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRVLEDdPEG---TYT 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 164 GTPYYVP-----PEIWENLPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQM 237
Cdd:cd05063 167 TSGGKIPirwtaPEAIAYRKFTSASDVWSFGIVMWEVMSFgERPYWDMSNHEVMKAINDGFRLPAPMDCPSAVYQLMLQC 246

                ....*....
gi 23510391 238 FKRNPSHRP 246
Cdd:cd05063 247 WQQDRARRP 255
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
9-254 4.37e-15

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: 74.99  E-value: 4.37e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   9 MIGEGSFGRALLVQHEssnqmfamKEIRLPKSFSNTQNSR---KEAVLLAKMKHPNIVAFKESFEAEGHLyiVMEYCDGG 85
Cdd:cd14068   1 LLGDGGFGSVYRAVYR--------GEDVAVKIFNKHTSFRllrQELVVLSHLHHPSLVALLAAGTAPRML--VMELAPKG 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  86 DLMQKIKQQKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFL---TQNGKV--KLGDFGSARllsnpmaFAC 160
Cdd:cd14068  71 SLDALLQQDNASL-TRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLftlYPNCAIiaKIADYGIAQ-------YCC 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 161 -----TYVGTPYYVPPEIWE-NLPYNNKSDIWSLGCILYELCT--------LKHPfqaNSWKNLILkvcQGCISPLPSHY 226
Cdd:cd14068 143 rmgikTSEGTPGFRAPEVARgNVIYNQQADVYSFGLLLYDILTcgerivegLKFP---NEFDELAI---QGKLPDPVKEY 216
                       250       260       270
                ....*....|....*....|....*....|..
gi 23510391 227 SY----ELQFLVKQMFKRNPSHRPSATTLLSR 254
Cdd:cd14068 217 GCapwpGVEALIKDCLKENPQCRPTSAQVFDI 248
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
8-254 6.22e-15

Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Met and Ron are receptor PTKs (RTKs) composed of an alpha-beta heterodimer. The extracellular alpha chain is disulfide linked to the beta chain, which contains an extracellular ligand-binding region with a sema domain, a PSI domain and four IPT repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. Met binds to the ligand, hepatocyte growth factor/scatter factor (HGF/SF), and is also called the HGF receptor. HGF/Met signaling plays a role in growth, transformation, cell motility, invasion, metastasis, angiogenesis, wound healing, and tissue regeneration. Aberrant expression of Met through mutations or gene amplification is associated with many human cancers including hereditary papillary renal and gastric carcinomas. The ligand for Ron is macrophage stimulating protein (MSP). Ron signaling is important in regulating cell motility, adhesion, proliferation, and apoptosis. Aberrant Ron expression is implicated in tumorigenesis and metastasis. The Met/Ron subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 74.82  E-value: 6.22e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFG---RALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKE-SFEAEGHLYIVMEYCD 83
Cdd:cd05058   1 EVIGKGHFGcvyHGTLIDSDGQKIHCAVKSLNRITDIEEVEQFLKEGIIMKDFSHPNVLSLLGiCLPSEGSPLVVLPYMK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  84 GGDLMQKIKQQKGKLFPEDMIlNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNpmafactyv 163
Cdd:cd05058  81 HGDLRNFIRSETHNPTVKDLI-GFGLQVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVADFGLARDIYD--------- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 164 gTPYYVP--------PEIW---ENL---PYNNKSDIWSLGCILYELCTLKHP--FQANSWkNLILKVCQGCISPLPSHYS 227
Cdd:cd05058 151 -KEYYSVhnhtgaklPVKWmalESLqtqKFTTKSDVWSFGVLLWELMTRGAPpyPDVDSF-DITVYLLQGRRLLQPEYCP 228
                       250       260
                ....*....|....*....|....*..
gi 23510391 228 YELQFLVKQMFKRNPSHRPSATTLLSR 254
Cdd:cd05058 229 DPLYEVMLSCWHPKPEMRPTFSELVSR 255
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
3-246 6.60e-15

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: 75.44  E-value: 6.60e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   3 DYMVLRMIGEGSFG---RALLV-QHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNI-----VAFKESFEAEG 73
Cdd:cd05108   8 EFKKIKVLGSGAFGtvyKGLWIpEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVcrllgICLTSTVQLIT 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  74 HLyivMEYcdgGDLMQKIKQQKGKLFPEdMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLS 153
Cdd:cd05108  88 QL---MPF---GCLLDYVREHKDNIGSQ-YLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 154 npmAFACTYVGTPYYVPPEiWENLP------YNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQGCISPLPSHY 226
Cdd:cd05108 161 ---AEEKEYHAEGGKVPIK-WMALEsilhriYTHQSDVWSYGVTVWELMTFgSKPYDGIPASEISSILEKGERLPQPPIC 236
                       250       260
                ....*....|....*....|
gi 23510391 227 SYELQFLVKQMFKRNPSHRP 246
Cdd:cd05108 237 TIDVYMIMVKCWMIDADSRP 256
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
7-251 7.19e-15

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk3, also called lemur tyrosine kinase 3 (Lmtk3) is a receptor kinase containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. The function of Aatyk3 is still unknown. The Aatyk3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271108 [Multi-domain]  Cd Length: 276  Bit Score: 74.99  E-value: 7.19e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   7 LRMIGEGSFGRALL--VQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDG 84
Cdd:cd14206   2 LQEIGNGWFGKVILgeIFSDYTPAQVVVKELRVSAGPLEQRKFISEAQPYRSLQHPNILQCLGLCTETIPFLLIMEFCQL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  85 GDLMQKIKQQKG------KLFPEDM--ILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARllSNpm 156
Cdd:cd14206  82 GDLKRYLRAQRKadgmtpDLPTRDLrtLQRMAYEITLGLLHLHKNNYIHSDLALRNCLLTSDLTVRIGDYGLSH--NN-- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 157 aFACTYVGTP-------YYVPPEIWENLPYN-------NKSDIWSLGCILYELCTL-KHPFQANSWKNLI--------LK 213
Cdd:cd14206 158 -YKEDYYLTPdrlwiplRWVAPELLDELHGNlivvdqsKESNVWSLGVTIWELFEFgAQPYRHLSDEEVLtfvvreqqMK 236
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 23510391 214 VCQGCISPLPSHYSYElqflVKQMFKRNPSHRPSATTL 251
Cdd:cd14206 237 LAKPRLKLPYADYWYE----IMQSCWLPPSQRPSVEEL 270
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
10-251 7.81e-15

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Aatyk subfamily is also referred to as the lemur tyrosine kinase (Lmtk) subfamily. It consists of Aatyk1 (Lmtk1), Aatyk2 (Lmtk2, Brek), Aatyk3 (Lmtk3), and similar proteins. Aatyk proteins are mostly receptor PTKs (RTKs) containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk1 does not contain a transmembrane segment and is a cytoplasmic (or nonreceptor) kinase. Aatyk proteins are classified as PTKs based on overall sequence similarity and the phylogenetic tree. However, analysis of catalytic residues suggests that Aatyk proteins may be multispecific kinases, functioning also as serine/threonine kinases. They are involved in neural differentiation, nerve growth factor (NGF) signaling, apoptosis, and spermatogenesis. The Aatyk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270638 [Multi-domain]  Cd Length: 269  Bit Score: 74.55  E-value: 7.81e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALL--VQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIV-AFKESFEAEGHLyIVMEYCDGGD 86
Cdd:cd05042   3 IGNGWFGKVLLgeIYSGTSVAQVVVKELKASANPKEQDTFLKEGQPYRILQHPNILqCLGQCVEAIPYL-LVMEFCDLGD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  87 LMQKIK-QQKGKLFPEDMILnwFTQMCL----GVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARllsnpmafaCT 161
Cdd:cd05042  82 LKAYLRsEREHERGDSDTRT--LQRMACevaaGLAHLHKLNFVHSDLALRNCLLTSDLTVKIGDYGLAH---------SR 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 162 YVGTPYYVPPEIWENLPY------------------NNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQGCISPL 222
Cdd:cd05042 151 YKEDYIETDDKLWFPLRWtapelvtefhdrllvvdqTKYSNIWSLGVTLWELFENgAQPYSNLSDLDVLAQVVREQDTKL 230
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 23510391 223 P--------SHYSYElqflVKQMFKRNPSHRPSATTL 251
Cdd:cd05042 231 PkpqlelpySDRWYE----VLQFCWLSPEQRPAAEDV 263
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
7-247 8.33e-15

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


Pssm-ID: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 74.57  E-value: 8.33e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   7 LRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSR--KEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDG 84
Cdd:cd14026   2 LRYLSRGAFGTVSRARHADWRVTVAIKCLKLDSPVGDSERNCllKEAEILHKARFSYILPILGICNEPEFLGIVTEYMTN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  85 GDLMQKIKQQKgkLFPE---DMILNWFTQMCLGVNHIHKKR--VLHRDIKSKNIFLTQNGKVKLGDFGSA--RLLSNPMA 157
Cdd:cd14026  82 GSLNELLHEKD--IYPDvawPLRLRILYEIALGVNYLHNMSppLLHHDLKTQNILLDGEFHVKIADFGLSkwRQLSISQS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 158 FACTYV---GTPYYVPPEIWEnlPYNN-----KSDIWSLGCILYELCTLKHPFQ-ANSWKNLILKVCQGCiSPLPSHYSY 228
Cdd:cd14026 160 RSSKSApegGTIIYMPPEEYE--PSQKrrasvKHDIYSYAIIMWEVLSRKIPFEeVTNPLQIMYSVSQGH-RPDTGEDSL 236
                       250       260
                ....*....|....*....|....*..
gi 23510391 229 ELQF--------LVKQMFKRNPSHRPS 247
Cdd:cd14026 237 PVDIphratlinLIESGWAQNPDERPS 263
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
108-248 9.87e-15

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: 74.84  E-value: 9.87e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 108 FTQMCLGVNHIHKKRVLHRDIKSKNIFL----TQNGKVKLGDFGSA---RLLSNPMAFACTYV---GTPYYVPPEIWENL 177
Cdd:cd14018 144 ILQLLEGVDHLVRHGIAHRDLKSDNILLeldfDGCPWLVIADFGCCladDSIGLQLPFSSWYVdrgGNACLMAPEVSTAV 223
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23510391 178 PYNN------KSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQ-GCISPLPSHYSYELQFLVKQMFKRNPSHRPSA 248
Cdd:cd14018 224 PGPGvvinysKADAWAVGAIAYEIFGLSNPFYGLGDTMLESRSYQeSQLPALPSAVPPDVRQVVKDLLQRDPNKRVSA 301
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
9-217 1.01e-14

Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR2 interacts with the protein phosphatase calcineurin and functions in calcium-mediated ERK signaling. It also functions in energy metabolism by regulating AMP kinase and AMPK-dependent processes such as glucose uptake and fatty acid oxidation. KSR proteins act as scaffold proteins that function 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. The KSR2 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: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 74.27  E-value: 1.01e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   9 MIGEGSFGRallVQHESSNQMFAMKEIRLPKSFSNTQNS-RKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDL 87
Cdd:cd14153   7 LIGKGRFGQ---VYHGRWHGEVAIRLIDIERDNEEQLKAfKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  88 MQKIKQQKgKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLtQNGKVKLGDFG----SARL--------LSNP 155
Cdd:cd14153  84 YSVVRDAK-VVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGlftiSGVLqagrredkLRIQ 161
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 156 MAFACtyvgtpYYVP-------PEIWEN-LPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQG 217
Cdd:cd14153 162 SGWLC------HLAPeiirqlsPETEEDkLPFSKHSDVFAFGTIWYELHAREWPFKTQPAEAIIWQVGSG 225
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
6-247 1.26e-14

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: 74.30  E-value: 1.26e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   6 VLRMIGEGSFGRALLVQHESSN----------------QMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESF 69
Cdd:cd05051   9 FVEKLGEGQFGEVHLCEANGLSdltsddfigndnkdepVLVAVKMLRPDASKNAREDFLKEVKIMSQLKDPNIVRLLGVC 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  70 EAEGHLYIVMEYCDGGDLMQKIKQQ----------KGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNG 139
Cdd:cd05051  89 TRDEPLCMIVEYMENGDLNQFLQKHeaetqgasatNSKTLSYGTLLYMATQIASGMKYLESLNFVHRDLATRNCLVGPNY 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 140 KVKLGDFGSARLLsnpmaFACTYVGTPYYVPPEI----WENL---PYNNKSDIWSLGCILYELCTL--KHP--------- 201
Cdd:cd05051 169 TIKIADFGMSRNL-----YSGDYYRIEGRAVLPIrwmaWESIllgKFTTKSDVWAFGVTLWEILTLckEQPyehltdeqv 243
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 23510391 202 ------FQANSWKNLILKVCQGCISPLpshysYElqfLVKQMFKRNPSHRPS 247
Cdd:cd05051 244 ienageFFRDDGMEVYLSRPPNCPKEI-----YE---LMLECWRRDEEDRPT 287
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
13-247 3.71e-14

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


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 72.53  E-value: 3.71e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  13 GSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDLMQKIK 92
Cdd:cd14027   4 GGFGKVSLCFHRTQGLVVLKTVYTGPNCIEHNEALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNLMHVLK 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  93 QQKGKLFPEDMILNWFTQmclGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSA-------------RLLSNPMAFA 159
Cdd:cd14027  84 KVSVPLSVKGRIILEIIE---GMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwskltkeehNEQREVDGTA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 160 CTYVGTPYYVPPEIWE--NLPYNNKSDIWSLGCILYELCTLKHPFQ-ANSWKNLILKVCQG---CISPLPSHYSYELQFL 233
Cdd:cd14027 161 KKNAGTLYYMAPEHLNdvNAKPTEKSDVYSFAIVLWAIFANKEPYEnAINEDQIIMCIKSGnrpDVDDITEYCPREIIDL 240
                       250
                ....*....|....
gi 23510391 234 VKQMFKRNPSHRPS 247
Cdd:cd14027 241 MKLCWEANPEARPT 254
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
9-195 3.71e-14

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


Pssm-ID: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 72.79  E-value: 3.71e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   9 MIGEGSFG---RALLVQHESS-NQMFAMKeIRLPKSFSNTQNsRKEAVLLAKMKHPNIVAFKESFEAEGHL----YIVME 80
Cdd:cd14055   2 LVGKGRFAevwKAKLKQNASGqYETVAVK-IFPYEEYASWKN-EKDIFTDASLKHENILQFLTAEERGVGLdrqyWLITA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  81 YCDGGDLMQKIKQQkgklfpedmILNWfTQMCL-------GVNHIHKKR---------VLHRDIKSKNIFLTQNGKVKLG 144
Cdd:cd14055  80 YHENGSLQDYLTRH---------ILSW-EDLCKmagslarGLAHLHSDRtpcgrpkipIAHRDLKSSNILVKNDGTCVLA 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23510391 145 DFGSA-RL--LSNPMAFACT-YVGTPYYVPPEIWE------NLPYNNKSDIWSLGCILYEL 195
Cdd:cd14055 150 DFGLAlRLdpSLSVDELANSgQVGTARYMAPEALEsrvnleDLESFKQIDVYSMALVLWEM 210
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
12-198 4.33e-14

Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase (RTK) containing an extracellular region with two leucine-rich motifs, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. The extracellular region of Ryk shows homology to the N-terminal domain of Wnt inhibitory factor-1 (WIF) and serves as the ligand (Wnt) binding domain of Ryk. Ryk is expressed in many different tissues both during development and in adults, suggesting a widespread function. It acts as a chemorepulsive axon guidance receptor of Wnt glycoproteins and is responsible for the establishment of axon tracts during the development of the central nervous system. In addition, studies in mice reveal that Ryk is essential in skeletal, craniofacial, and cardiac development. Thus, it appears Ryk is involved in signal transduction despite its lack of kinase activity. Ryk may function as an accessory protein that modulates the signals coming from catalytically active partner RTKs such as the Eph receptors. The Ryk subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 72.48  E-value: 4.33e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  12 EGSFGR---ALLVQHESSNQMFAMKEIRlpKSFSNTQNSR--KEAVLLAKMKHPNIVA-FKESFEAEGHLYIVMEYCDGG 85
Cdd:cd05043  16 EGTFGRifhGILRDEKGKEEEVLVKTVK--DHASEIQVTMllQESSLLYGLSHQNLLPiLHVCIEDGEKPMVLYPYMNWG 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  86 DLmqKIKQQKGKLFPEDM--------ILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSnPMA 157
Cdd:cd05043  94 NL--KLFLQQCRLSEANNpqalstqqLVHMALQIACGMSYLHRRGVIHKDIAARNCVIDDELQVKITDNALSRDLF-PMD 170
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 23510391 158 FACtyVGTPYYVP-----PEIWENLPYNNKSDIWSLGCILYELCTL 198
Cdd:cd05043 171 YHC--LGDNENRPikwmsLESLVNKEYSSASDVWSFGVLLWELMTL 214
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
10-246 4.52e-14

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: 72.74  E-value: 4.52e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRA----LLVQHESSNQMFAMKEIrlpKSFSNTQN---SRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYC 82
Cdd:cd05090  13 LGECAFGKIykghLYLPGMDHAQLVAIKTL---KDYNNPQQwneFQQEASLMTELHHPNIVCLLGVVTQEQPVCMLFEFM 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  83 DGGDL-----MQKIKQQKGKLFPEDM----------ILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFG 147
Cdd:cd05090  90 NQGDLhefliMRSPHSDVGCSSDEDGtvkssldhgdFLHIAIQIAAGMEYLSSHFFVHKDLAARNILVGEQLHVKISDLG 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 148 sarlLSNPMAFACTYVGTP------YYVPPEIWENLPYNNKSDIWSLGCILYELCTLK-HPFQANSWKNLILKVCQGCIS 220
Cdd:cd05090 170 ----LSREIYSSDYYRVQNksllpiRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGlQPYYGFSNQEVIEMVRKRQLL 245
                       250       260
                ....*....|....*....|....*.
gi 23510391 221 PLPSHYSYELQFLVKQMFKRNPSHRP 246
Cdd:cd05090 246 PCSEDCPPRMYSLMTECWQEIPSRRP 271
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
9-217 6.54e-14

Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KSR1 functions as a transducer of TNFalpha-stimulated C-Raf activation of ERK1/2 and NF-kB. Detected activity of KSR1 is cell type specific and context dependent. It is inactive in normal colon epithelial cells and becomes activated at the onset of inflammatory bowel disease (IBD). Similarly, KSR1 activity is undetectable prior to stimulation by EGF or ceramide in COS-7 or YAMC cells, respectively. KSR proteins are widely regarded as pseudokinases, however, this matter is up for debate as catalytic activity has been detected for KSR1 in some systems. The KSR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 71.92  E-value: 6.54e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   9 MIGEGSFGRAllvqheSSNQMFAMKEIRLPKSFSNTQNS----RKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDG 84
Cdd:cd14152   7 LIGQGRWGKV------HRGRWHGEVAIRLLEIDGNNQDHlklfKKEVMNYRQTRHENVVLFMGACMHPPHLAIITSFCKG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  85 GDLMQKIKQQKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLtQNGKVKLGDFGSARL--------LSNPM 156
Cdd:cd14152  81 RTLYSFVRDPKTSL-DINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLFGIsgvvqegrRENEL 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 157 AFACTYVgtpYYVPPEI---------WENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQG 217
Cdd:cd14152 159 KLPHDWL---CYLAPEIvremtpgkdEDCLPFSKAADVYAFGTIWYELQARDWPLKNQPAEALIWQIGSG 225
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
1-202 6.88e-14

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: 72.19  E-value: 6.88e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   1 MDDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKsfsnTQNSRKEAVLLAKMK-HPNIVAFKESF--EAEGHLYI 77
Cdd:cd14132  17 QDDYEIIRKIGRGKYSEVFEGINIGNNEKVVIKVLKPVK----KKKIKREIKILQNLRgGPNIVKLLDVVkdPQSKTPSL 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  78 VMEYCDGGDLmqkiKQQKGKLFPEDmILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNG-KVKLGDFGSARLLSnPM 156
Cdd:cd14132  93 IFEYVNNTDF----KTLYPTLTDYD-IRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDHEKrKLRLIDWGLAEFYH-PG 166
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 23510391 157 AFACTYVGTPYYVPPEIWENLPYNNKS-DIWSLGCILYELCTLKHPF 202
Cdd:cd14132 167 QEYNVRVASRYYKGPELLVDYQYYDYSlDMWSLGCMLASMIFRKEPF 213
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
10-195 7.36e-14

Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk2 is a member of the Aatyk subfamily of proteins, which are receptor kinases containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk2 is also called lemur tyrosine kinase 2 (Lmtk2) or brain-enriched kinase (Brek). It is expressed at high levels in early postnatal brain, and has been shown to play a role in nerve growth factor (NGF) signaling. Studies with knockout mice reveal that Aatyk2 is essential for late stage spermatogenesis. Although it is classified as a PTK based on sequence similarity and the phylogenetic tree, Aatyk2 has been functionally characterized as a serine/threonine kinase. The Aatyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270669 [Multi-domain]  Cd Length: 271  Bit Score: 71.82  E-value: 7.36e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALL--VQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIV-AFKESFEAEGHLyIVMEYCDGGD 86
Cdd:cd05086   5 IGNGWFGKVLLgeIYTGTSVARVVVKELKASANPKEQDDFLQQGEPYYILQHPNILqCVGQCVEAIPYL-LVFEFCDLGD 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  87 LMQKIKQQKGKLF--PEDMILNWFT-QMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSArllsnPMAFACTYV 163
Cdd:cd05086  84 LKTYLANQQEKLRgdSQIMLLQRMAcEIAAGLAHMHKHNFLHSDLALRNCYLTSDLTVKVGDYGIG-----FSRYKEDYI 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 23510391 164 GT--PYYVP-----PEIWEN-------LPYNNKSDIWSLGCILYEL 195
Cdd:cd05086 159 ETddKKYAPlrwtaPELVTSfqdgllaAEQTKYSNIWSLGVTLWEL 204
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
7-248 8.54e-14

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk1 (or simply Aatyk) is also called lemur tyrosine kinase 1 (Lmtk1). It is a cytoplasmic (or nonreceptor) kinase containing a long C-terminal region. The expression of Aatyk1 is upregulated during growth arrest and apoptosis in myeloid cells. Aatyk1 has been implicated in neural differentiation, and is a regulator of the Na-K-2Cl cotransporter, a membrane protein involved in cell proliferation and survival, epithelial transport, and blood pressure control. The Aatyk1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 71.56  E-value: 8.54e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   7 LRMIGEGSFGRALL--VQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIV-AFKESFEAEGHLyIVMEYCD 83
Cdd:cd05087   2 LKEIGHGWFGKVFLgeVNSGLSSTQVVVKELKASASVQDQMQFLEEAQPYRALQHTNLLqCLAQCAEVTPYL-LVMEFCP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  84 GGDLMQKIKQQKG--KLFPEDMILNWFT-QMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFAc 160
Cdd:cd05087  81 LGDLKGYLRSCRAaeSMAPDPLTLQRMAcEVACGLLHLHRNNFVHSDLALRNCLLTADLTVKIGDYGLSHCKYKEDYFV- 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 161 tyVGTPYYVP-----PEIWENLPYN-------NKSDIWSLGCILYELCTL-KHPFQANSWKNLI--------LKVCQGCI 219
Cdd:cd05087 160 --TADQLWVPlrwiaPELVDEVHGNllvvdqtKQSNVWSLGVTIWELFELgNQPYRHYSDRQVLtytvreqqLKLPKPQL 237
                       250       260       270
                ....*....|....*....|....*....|
gi 23510391 220 S-PLPSHYSYELQFLVKQmfkrnPSHRPSA 248
Cdd:cd05087 238 KlSLAERWYEVMQFCWLQ-----PEQRPTA 262
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
101-254 1.28e-13

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: 71.96  E-value: 1.28e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 101 EDMILNWFtQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSAR-LLSNP--MAFACTYVGTPYYVPPEIWENL 177
Cdd:cd14207 180 EDLISYSF-QVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARdIYKNPdyVRKGDARLPLKWMAPESIFDKI 258
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23510391 178 pYNNKSDIWSLGCILYELCTL-KHPFQANSW-KNLILKVCQGCISPLPSHYSYELQFLVKQMFKRNPSHRPSATTLLSR 254
Cdd:cd14207 259 -YSTKSDVWSYGVLLWEIFSLgASPYPGVQIdEDFCSKLKEGIRMRAPEFATSEIYQIMLDCWQGDPNERPRFSELVER 336
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
45-252 1.73e-13

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 71.95  E-value: 1.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   45 QNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVME------YCDGGDlmqkikqqKGKLFPEDMiLNWFTQMCLGVNHI 118
Cdd:PHA03212 128 GGTATEAHILRAINHPSIIQLKGTFTYNKFTCLILPryktdlYCYLAA--------KRNIAICDI-LAIERSVLRAIQYL 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  119 HKKRVLHRDIKSKNIFLTQNGKVKLGDFGSArllSNPMAFACT----YVGTPYYVPPEIWENLPYNNKSDIWSLGCILYE 194
Cdd:PHA03212 199 HENRIIHRDIKAENIFINHPGDVCLGDFGAA---CFPVDINANkyygWAGTIATNAPELLARDPYGPAVDIWSAGIVLFE 275
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  195 LCTLK----------------------------HP--FQANSWKNL---ILKVCQGC-----ISPLPSH---YSYELQFL 233
Cdd:PHA03212 276 MATCHdslfekdgldgdcdsdrqikliirrsgtHPneFPIDAQANLdeiYIGLAKKSsrkpgSRPLWTNlyeLPIDLEYL 355
                        250
                 ....*....|....*....
gi 23510391  234 VKQMFKRNPSHRPSATTLL 252
Cdd:PHA03212 356 ICKMLAFDAHHRPSAEALL 374
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
8-212 2.85e-13

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: 70.22  E-value: 2.85e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFGraLLVQHESSNQMFAMKEIrLPKSFSNTQNSRK----EAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCD 83
Cdd:cd14158  21 NKLGEGGFG--VVFKGYINDKNVAVKKL-AAMVDISTEDLTKqfeqEIQVMAKCQHENLVELLGYSCDGPQLCLVYTYMP 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  84 GGDLMQKIKQQKGKL-FPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARllSNPmAFACTY 162
Cdd:cd14158  98 NGSLLDRLACLNDTPpLSWHMRCKIAQGTANGINYLHENNHIHRDIKSANILLDETFVPKISDFGLAR--ASE-KFSQTI 174
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 23510391 163 -----VGTPYYVPPEIWENlPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLIL 212
Cdd:cd14158 175 mteriVGTTAYMAPEALRG-EITPKSDIFSFGVVLLEIITGLPPVDENRDPQLLL 228
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
8-251 2.88e-13

Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Axl is widely expressed in a variety of organs and cells including epithelial, mesenchymal, hematopoietic, as well as non-transformed cells. It is important in many cellular functions such as survival, anti-apoptosis, proliferation, migration, and adhesion. Axl was originally isolated from patients with chronic myelogenous leukemia and a chronic myeloproliferative disorder. It is overexpressed in many human cancers including colon, squamous cell, thyroid, breast, and lung carcinomas. Axl is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to its ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Axl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 70.04  E-value: 2.88e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFGRAL--LVQHESSNQMFAMKEIRLPK-SFSNTQNSRKEAVLLAKMKHPNI-----VAFKESfEAEGHL--YI 77
Cdd:cd05075   6 KTLGEGEFGSVMegQLNQDDSVLKVAVKTMKIAIcTRSEMEDFLSEAVCMKEFDHPNVmrligVCLQNT-ESEGYPspVV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  78 VMEYCDGGDLMQKIKQQK----GKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLS 153
Cdd:cd05075  85 ILPFMKHGDLHSFLLYSRlgdcPVYLPTQMLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADFGLSKKIY 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 154 NPMAFACTYVG-TPY-YVPPEIWENLPYNNKSDIWSLGCILYELCT---LKHPFQANS------WKNLILKVCQGCISPL 222
Cdd:cd05075 165 NGDYYRQGRISkMPVkWIAIESLADRVYTTKSDVWSFGVTMWEIATrgqTPYPGVENSeiydylRQGNRLKQPPDCLDGL 244
                       250       260
                ....*....|....*....|....*....
gi 23510391 223 pshysYELQFLVKQMfkrNPSHRPSATTL 251
Cdd:cd05075 245 -----YELMSSCWLL---NPKDRPSFETL 265
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
8-251 2.96e-13

Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The TAM subfamily consists of Tyro3 (or Sky), Axl, Mer (or Mertk), and similar proteins. TAM subfamily members are receptor tyr kinases (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. TAM proteins are implicated in a variety of cellular effects including survival, proliferation, migration, and phagocytosis. They are also associated with several types of cancer as well as inflammatory, autoimmune, vascular, and kidney diseases. The TAM subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 69.87  E-value: 2.96e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFG---RALLVQHESSNQMFAMKEIRLP-KSFSNTQNSRKEAVLLAKMKHPNI-----VAFK-ESFEAEGHLYI 77
Cdd:cd05035   5 KILGEGEFGsvmEAQLKQDDGSQLKVAVKTMKVDiHTYSEIEEFLSEAACMKDFDHPNVmrligVCFTaSDLNKPPSPMV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  78 VMEYCDGGDL-----MQKIKQQKGKlFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLL 152
Cdd:cd05035  85 ILPFMKHGDLhsyllYSRLGGLPEK-LPLQTLLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVCVADFGLSRKI 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 153 SNPMAFACTYVGTpyyvPPEIW---ENLP---YNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQGCISPLPSH 225
Cdd:cd05035 164 YSGDYYRQGRISK----MPVKWialESLAdnvYTSKSDVWSFGVTMWEIATRgQTPYPGVENHEIYDYLRNGNRLKQPED 239
                       250       260
                ....*....|....*....|....*.
gi 23510391 226 YSYELQFLVKQMFKRNPSHRPSATTL 251
Cdd:cd05035 240 CLDEVYFLMYFCWTVDPKDRPTFTKL 265
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
4-224 3.16e-13

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: 70.82  E-value: 3.16e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRAL-LVQHESSNQMFAMKEIRLPKSFSntQNSRKEAVLLAKM--KHPN----IVAFKESFEAEGHLY 76
Cdd:cd14215  14 YEIVSTLGEGTFGRVVqCIDHRRGGARVALKIIKNVEKYK--EAARLEINVLEKIneKDPEnknlCVQMFDWFDYHGHMC 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEYCdGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLT-------------------Q 137
Cdd:cd14215  92 ISFELL-GLSTFDFLKENNYLPYPIHQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFVnsdyeltynlekkrdersvK 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 138 NGKVKLGDFGSARLLSNPMAfacTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLiLKVCQG 217
Cdd:cd14215 171 STAIRVVDFGSATFDHEHHS---TIVSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNREH-LAMMER 246

                ....*..
gi 23510391 218 CISPLPS 224
Cdd:cd14215 247 ILGPIPS 253
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
7-197 3.86e-13

Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER3 contains an impaired tyr kinase domain, which lacks crucial residues for catalytic activity against exogenous substrates but is still able to bind ATP and autophosphorylate. HER3 binds the neuregulin ligands, NRG1 and NRG2, and it relies on its heterodimerization partners for activity following ligand binding. The HER2-HER3 heterodimer constitutes a high affinity co-receptor capable of potent mitogenic signaling. HER3 participates in a signaling pathway involved in the proliferation, survival, adhesion, and motility of tumor cells. The HER3 subfamily is part of a larger superfamily that includes other pseudokinases and the the catalytic domains of active kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 69.60  E-value: 3.86e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   7 LRMIGEGSFGRA----LLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKeSFEAEGHLYIVMEYC 82
Cdd:cd05111  12 LKVLGSGVFGTVhkgiWIPEGDSIKIPVAIKVIQDRSGRQSFQAVTDHMLAIGSLDHAYIVRLL-GICPGASLQLVTQLL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  83 DGGDLMQKIKQQKGKLFPEdMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLsnpmafactY 162
Cdd:cd05111  91 PLGSLLDHVRQHRGSLGPQ-LLLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLKSPSQVQVADFGVADLL---------Y 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 23510391 163 VGTPYYVPPEI-----WENLP------YNNKSDIWSLGCILYELCT 197
Cdd:cd05111 161 PDDKKYFYSEAktpikWMALEsihfgkYTHQSDVWSYGVTVWEMMT 206
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
9-253 4.66e-13

Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EphB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphB receptors play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphBs are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion. The EphB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 69.13  E-value: 4.66e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   9 MIGEGSFG---RALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGG 85
Cdd:cd05065  11 VIGAGEFGevcRGRLKLPGKREIFVAIKTLKSGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTKSRPVMIITEFMENG 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  86 DLMQKIKQQKGKlFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLL----SNPMAFACT 161
Cdd:cd05065  91 ALDSFLRQNDGQ-FTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLeddtSDPTYTSSL 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 162 YVGTPY-YVPPEIWENLPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQMFK 239
Cdd:cd05065 170 GGKIPIrWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYgERPYWDMSNQDVINAIEQDYRLPPPMDCPTALHQLMLDCWQ 249
                       250
                ....*....|....
gi 23510391 240 RNPSHRPSATTLLS 253
Cdd:cd05065 250 KDRNLRPKFGQIVN 263
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
10-198 4.95e-13

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR2 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR2 results in a slow but sustained receptor activation. DDR2 binds mostly to fibrillar collagens as well as collagen X. DDR2 is widely expressed in many tissues with the highest levels found in skeletal muscle, skin, kidney and lung. It is important in cell proliferation and development. Mice, with a deletion of DDR2, suffer from dwarfism and delayed healing of epidermal wounds. DDR2 also contributes to collagen (type I) regulation by inhibiting fibrillogenesis and altering the morphology of collagen fibers. It is also expressed in immature dendritic cells (DCs), where it plays a role in DC activation and function. The DDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 69.64  E-value: 4.95e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHE--------------SSNQ--MFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEG 73
Cdd:cd05095  13 LGEGQFGEVHLCEAEgmekfmdkdfalevSENQpvLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIRLLAVCITDD 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  74 HLYIVMEYCDGGDLMQKIKQQK---GKLFPEDMILNWFTQMCL-------GVNHIHKKRVLHRDIKSKNIFLTQNGKVKL 143
Cdd:cd05095  93 PLCMITEYMENGDLNQFLSRQQpegQLALPSNALTVSYSDLRFmaaqiasGMKYLSSLNFVHRDLATRNCLVGKNYTIKI 172
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23510391 144 GDFGSARLLsnpmafactYVGTPYYVPPEI--------WENL---PYNNKSDIWSLGCILYELCTL 198
Cdd:cd05095 173 ADFGMSRNL---------YSGDYYRIQGRAvlpirwmsWESIllgKFTTASDVWAFGVTLWETLTF 229
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
28-247 5.06e-13

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


Pssm-ID: 270947 [Multi-domain]  Cd Length: 269  Bit Score: 69.12  E-value: 5.06e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  28 QMFAMKEIrLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDLmqkikqqKGKLFPEDMILNW 107
Cdd:cd14045  31 RTVAIKKI-AKKSFTLSKRIRKEVKQVRELDHPNLCKFIGGCIEVPNVAIITEYCPKGSL-------NDVLLNEDIPLNW 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 108 FTQMCL------GVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFG--SARLLSNPMAFAcTYVG--TPYYVPPEIwENL 177
Cdd:cd14045 103 GFRFSFatdiarGMAYLHQHKIYHGRLKSSNCVIDDRWVCKIADYGltTYRKEDGSENAS-GYQQrlMQVYLPPEN-HSN 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 178 PY---NNKSDIWSLGCILYELCTLKHPFQAN------SW----KNLIL-KVCQGCisPLPSHYSYelqfLVKQMFKRNPS 243
Cdd:cd14045 181 TDtepTQATDVYSYAIILLEIATRNDPVPEDdysldeAWcpplPELISgKTENSC--PCPADYVE----LIRRCRKNNPA 254

                ....
gi 23510391 244 HRPS 247
Cdd:cd14045 255 QRPT 258
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
39-202 5.15e-13

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 70.64  E-value: 5.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   39 KSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEY--CDggdLMQKIkQQKGKLFPEDMIlnwFTQMCL--G 114
Cdd:PHA03207 125 KAVTGGKTPGREIDILKTISHRAIINLIHAYRWKSTVCMVMPKykCD---LFTYV-DRSGPLPLEQAI---TIQRRLleA 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  115 VNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSA-RLLSNPMAFAC-TYVGTPYYVPPEIWENLPYNNKSDIWSLGCIL 192
Cdd:PHA03207 198 LAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGAAcKLDAHPDTPQCyGWSGTLETNSPELLALDPYCAKTDIWSAGLVL 277
                        170
                 ....*....|
gi 23510391  193 YELCTLKHPF 202
Cdd:PHA03207 278 FEMSVKNVTL 287
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
28-254 8.60e-13

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror2 plays important roles in skeletal and heart formation. Ror2-deficient mice show widespread bone abnormalities, ventricular defects in the heart, and respiratory dysfunction. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Ror2 is also implicated in neural development. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 68.89  E-value: 8.60e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  28 QMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDLMQKI---------------K 92
Cdd:cd05091  37 QAVAIKTLKDKAEGPLREEFRHEAMLRSRLQHPNIVCLLGVVTKEQPMSMIFSYCSHGDLHEFLvmrsphsdvgstdddK 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  93 QQKGKLFPEDMiLNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSAR---------LLSNPMafactyv 163
Cdd:cd05091 117 TVKSTLEPADF-LHIVTQIAAGMEYLSSHHVVHKDLATRNVLVFDKLNVKISDLGLFRevyaadyykLMGNSL------- 188
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 164 gTPY-YVPPEIWENLPYNNKSDIWSLGCILYELCTLK-HPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQMFKRN 241
Cdd:cd05091 189 -LPIrWMSPEAIMYGKFSIDSDIWSYGVVLWEVFSYGlQPYCGYSNQDVIEMIRNRQVLPCPDDCPAWVYTLMLECWNEF 267
                       250
                ....*....|...
gi 23510391 242 PSHRPSATTLLSR 254
Cdd:cd05091 268 PSRRPRFKDIHSR 280
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
8-253 8.81e-13

Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of most class EphA receptors including EphA3, EphA4, EphA5, and EphA7, but excluding EphA1, EphA2 and EphA10. Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. One exception is EphA4, which also binds ephrins-B2/B3. EphA receptors and ephrin-A ligands are expressed in multiple areas of the developing brain, especially in the retina and tectum. They are part of a system controlling retinotectal mapping. EphRs comprise the largest subfamily of receptor PTKs (RTKs). EphRs contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 68.35  E-value: 8.81e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFGRALLVQHESSNQM---FAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDG 84
Cdd:cd05066  10 KVIGAGEFGEVCSGRLKLPGKReipVAIKTLKAGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTRSKPVMIVTEYMEN 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  85 GDLMQKIKQQKGKlFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTYVG 164
Cdd:cd05066  90 GSLDAFLRKHDGQ-FTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDPEAAYTTRG 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 165 TPY---YVPPEIWENLPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQMFKR 240
Cdd:cd05066 169 GKIpirWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYgERPYWEMSNQDVIKAIEEGYRLPAPMDCPAALHQLMLDCWQK 248
                       250
                ....*....|...
gi 23510391 241 NPSHRPSATTLLS 253
Cdd:cd05066 249 DRNERPKFEQIVS 261
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
8-254 9.31e-13

Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyro3 (or Sky) is predominantly expressed in the central nervous system and the brain, and functions as a neurotrophic factor. It is also expressed in osteoclasts and has a role in bone resorption. Tyro3 is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Tyro3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 68.79  E-value: 9.31e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   8 RMIGEGSFG---RALLVQHESSNQMFAMKEIRLP-KSFSNTQNSRKEAVLLAKMKHPNI---VAFKESFEAEGHLYIVM- 79
Cdd:cd05074  15 RMLGKGEFGsvrEAQLKSEDGSFQKVAVKMLKADiFSSSDIEEFLREAACMKEFDHPNViklIGVSLRSRAKGRLPIPMv 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  80 --EYCDGGDL-----MQKIKQQKGKLfPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLL 152
Cdd:cd05074  95 ilPFMKHGDLhtfllMSRIGEEPFTL-PLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCMLNENMTVCVADFGLSKKI 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 153 snpmafactYVGTpYYVP------PEIW---ENLP---YNNKSDIWSLGCILYELCTL-KHPF----QANSWKNLI---- 211
Cdd:cd05074 174 ---------YSGD-YYRQgcasklPVKWlalESLAdnvYTTHSDVWAFGVTMWEIMTRgQTPYagveNSEIYNYLIkgnr 243
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 23510391 212 LKVCQGCISPLpshysYELQFlvkQMFKRNPSHRPSATTLLSR 254
Cdd:cd05074 244 LKQPPDCLEDV-----YELMC---QCWSPEPKCRPSFQHLRDQ 278
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
104-247 1.12e-12

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: 69.67  E-value: 1.12e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 104 ILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLL---SNPMAFACTYVGTPYYVPPEIWENLpYN 180
Cdd:cd05105 239 LLSFTYQVARGMEFLASKNCVHRDLAARNVLLAQGKIVKICDFGLARDImhdSNYVSKGSTFLPVKWMAPESIFDNL-YT 317
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23510391 181 NKSDIWSLGCILYELCTLKH-PFQA----NSWKNlilKVCQGCISPLPSHYSYELQFLVKQMFKRNPSHRPS 247
Cdd:cd05105 318 TLSDVWSYGILLWEIFSLGGtPYPGmivdSTFYN---KIKSGYRMAKPDHATQEVYDIMVKCWNSEPEKRPS 386
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
10-195 1.16e-12

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


Pssm-ID: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 68.23  E-value: 1.16e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFG---RALLVQHESSNQMFamkeirlpkSFSNTQNSRKEAVLLAK--MKHPNIVAFKESFEAEGH----LYIVME 80
Cdd:cd13998   3 IGKGRFGevwKASLKNEPVAVKIF---------SSRDKQSWFREKEIYRTpmLKHENILQFIAADERDTAlrteLWLVTA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  81 YCDGGDLMQKIKQQkgklfpedmILNWFT------QMCLGVNHIH---------KKRVLHRDIKSKNIFLTQNGKVKLGD 145
Cdd:cd13998  74 FHPNGSL*DYLSLH---------TIDWVSlcrlalSVARGLAHLHseipgctqgKPAIAHRDLKSKNILVKNDGTCCIAD 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23510391 146 FG-SARLLSN----PMAfACTYVGTPYYVPPEIWE---NLPYNN---KSDIWSLGCILYEL 195
Cdd:cd13998 145 FGlAVRLSPStgeeDNA-NNGQVGTKRYMAPEVLEgaiNLRDFEsfkRVDIYAMGLVLWEM 204
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
10-204 1.26e-12

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


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 67.91  E-value: 1.26e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFG---RALLVQHessnQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGD 86
Cdd:cd14664   1 IGRGGAGtvyKGVMPNG----TLVAVKRLKGEGTQGGDHGFQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPNGS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  87 LMQKIKQQKGKLFPedmiLNWFT------QMCLGVNHIHKK---RVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMA 157
Cdd:cd14664  77 LGELLHSRPESQPP----LDWETrqrialGSARGLAYLHHDcspLIIHRDVKSNNILLDEEFEAHVADFGLAKLMDDKDS 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 23510391 158 FACTYV-GTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQA 204
Cdd:cd14664 153 HVMSSVaGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRPFDE 200
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
10-251 1.28e-12

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: 68.29  E-value: 1.28e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGR-----ALLVQHESSNQMFAMKEIRLpksfSNTQNSRKeaVLLAKMK-------HPNIV-AFKESFEAEGHLY 76
Cdd:cd05054  15 LGRGAFGKviqasAFGIDKSATCRTVAVKMLKE----GATASEHK--ALMTELKilihighHLNVVnLLGACTKPGGPLM 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  77 IVMEYCDGGDLMQKIKQQKGKLFP-------------------------EDMILNWFtQMCLGVNHIHKKRVLHRDIKSK 131
Cdd:cd05054  89 VIVEFCKFGNLSNYLRSKREEFVPyrdkgardveeeedddelykepltlEDLICYSF-QVARGMEFLASRKCIHRDLAAR 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 132 NIFLTQNGKVKLGDFGSAR-LLSNPMAFACTYVGTP--YYVPPEIWENLpYNNKSDIWSLGCILYELCTL-KHPFQA-NS 206
Cdd:cd05054 168 NILLSENNVVKICDFGLARdIYKDPDYVRKGDARLPlkWMAPESIFDKV-YTTQSDVWSFGVLLWEIFSLgASPYPGvQM 246
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 23510391 207 WKNLILKVCQGCISPLPSHYSYELQFLVKQMFKRNPSHRPSATTL 251
Cdd:cd05054 247 DEEFCRRLKEGTRMRAPEYTTPEIYQIMLDCWHGEPKERPTFSEL 291
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
6-254 1.40e-12

Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They can be classified into two classes (EphA and EphB), according to their extracellular sequences, which largely correspond to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.The EphR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 67.78  E-value: 1.40e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   6 VLRMIGEGSFG---RALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYC 82
Cdd:cd05033   8 IEKVIGGGEFGevcSGSLKLPGKKEIDVAIKTLKSGYSDKQRLDFLTEASIMGQFDHPNVIRLEGVVTKSRPVMIVTEYM 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  83 DGGDLMQKIKQQKGKLFPEdMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAfacTY 162
Cdd:cd05033  88 ENGSLDKFLRENDGKFTVT-QLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLSRRLEDSEA---TY 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 163 VGTPYYVP-----PEIWENLPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQ 236
Cdd:cd05033 164 TTKGGKIPirwtaPEAIAYRKFTSASDVWSFGIVMWEVMSYgERPYWDMSNQDVIKAVEDGYRLPPPMDCPSALYQLMLD 243
                       250
                ....*....|....*...
gi 23510391 237 MFKRNPSHRPSATTLLSR 254
Cdd:cd05033 244 CWQKDRNERPTFSQIVST 261
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
10-198 1.66e-12

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


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 68.08  E-value: 1.66e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGRALLVQHE--------SSNQ------MFAMKEIRlPKSFSNTQNS-RKEAVLLAKMKHPNIVAFKESFEAEGH 74
Cdd:cd05097  13 LGEGQFGEVHLCEAEglaeflgeGAPEfdgqpvLVAVKMLR-ADVTKTARNDfLKEIKIMSRLKNPNIIRLLGVCVSDDP 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  75 LYIVMEYCDGGDLMQKIKQQ-------KGKLFPEDMILNWF---TQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLG 144
Cdd:cd05097  92 LCMITEYMENGDLNQFLSQReiestftHANNIPSVSIANLLymaVQIASGMKYLASLNFVHRDLATRNCLVGNHYTIKIA 171
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23510391 145 DFGSARLLsnpmafactYVGTPYYVPPE--------IWENL---PYNNKSDIWSLGCILYELCTL 198
Cdd:cd05097 172 DFGMSRNL---------YSGDYYRIQGRavlpirwmAWESIllgKFTTASDVWAFGVTLWEMFTL 227
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
10-206 1.74e-12

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 67.93  E-value: 1.74e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  10 IGEGSFGraLLVQHESSNQMFAMKEIR---------LPKSFsntqnsRKEAVLLAKMKHPNIVAFKeSFEAEGHLY-IVM 79
Cdd:cd14159   1 IGEGGFG--CVYQAVMRNTEYAVKRLKedseldwsvVKNSF------LTEVEKLSRFRHPNIVDLA-GYSAQQGNYcLIY 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  80 EYCDGGDLMQKIKQQKGklFPEdmiLNWFTQMCL------GVNHIHKKR--VLHRDIKSKNIFLTQNGKVKLGDFGSARL 151
Cdd:cd14159  72 VYLPNGSLEDRLHCQVS--CPC---LSWSQRLHVllgtarAIQYLHSDSpsLIHGDVKSSNILLDAALNPKLGDFGLARF 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23510391 152 --------LSNPMAFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANS 206
Cdd:cd14159 147 srrpkqpgMSSTLARTQTVRGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLTGRRAMEVDS 209
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
57-196 1.91e-12

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: 67.68  E-value: 1.91e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  57 MKHPNIVAF--KESFEAEGH--LYIVMEYCDGGDLMQKIkqQKGKLFPEDMiLNWFTQMCLGVNHIH--------KKRVL 124
Cdd:cd14056  46 LRHENILGFiaADIKSTGSWtqLWLITEYHEHGSLYDYL--QRNTLDTEEA-LRLAYSAASGLAHLHteivgtqgKPAIA 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 125 HRDIKSKNIFLTQNGKVKLGDFGSA---RLLSNPMAFACTY-VGTPYYVPPEIW-ENLPYNN-----KSDIWSLGCILYE 194
Cdd:cd14056 123 HRDLKSKNILVKRDGTCCIADLGLAvryDSDTNTIDIPPNPrVGTKRYMAPEVLdDSINPKSfesfkMADIYSFGLVLWE 202

                ..
gi 23510391 195 LC 196
Cdd:cd14056 203 IA 204
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
7-253 3.04e-12

Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER2 (ErbB2, HER2/neu) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER2 does not bind to any known EGFR subfamily ligands, but contributes to the kinase activity of all possible heterodimers. It acts as the preferred partner of other ligand-bound EGFR proteins and functions as a signal amplifier, with the HER2-HER3 heterodimer being the most potent pair in mitogenic signaling. HER2 plays an important role in cell development, proliferation, survival and motility. Overexpression of HER2 results in its activation and downstream signaling, even in the absence of ligand. HER2 overexpression, mainly due to gene amplification, has been shown in a variety of human cancers. Its role in breast cancer is especially well-documented. HER2 is up-regulated in about 25% of breast tumors and is associated with increases in tumor aggressiveness, recurrence and mortality. HER2 is a target for monoclonal antibodies and small molecule inhibitors, which are being developed as treatments for cancer. The first humanized antibody approved for clinical use is Trastuzumab (Herceptin), which is being used in combination with other therapies to improve the survival rates of patients with HER2-overexpressing breast cancer. The HER2 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: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 66.97  E-value: 3.04e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   7 LRMIGEGSFGRAL----LVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNI-----VAFKESFEAEGHLyi 77
Cdd:cd05109  12 VKVLGSGAFGTVYkgiwIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVcrllgICLTSTVQLVTQL-- 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  78 vMEYcdgGDLMQKIKQQKGKLFPEDMiLNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSnpma 157
Cdd:cd05109  90 -MPY---GCLLDYVRENKDRIGSQDL-LNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFGLARLLD---- 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391 158 factYVGTPYYVP----PEIWENLP------YNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQGCISPLPSHY 226
Cdd:cd05109 161 ----IDETEYHADggkvPIKWMALEsilhrrFTHQSDVWSYGVTVWELMTFgAKPYDGIPAREIPDLLEKGERLPQPPIC 236
                       250       260
                ....*....|....*....|....*..
gi 23510391 227 SYELQFLVKQMFKRNPSHRPSATTLLS 253
Cdd:cd05109 237 TIDVYMIMVKCWMIDSECRPRFRELVD 263
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
4-210 3.73e-12

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. TTBK1 has been linked to Alzheimer's disease (AD) while TTBK2 is associated with spinocerebellar ataxia type 11 (SCA11). Both AD and SCA11 patients show the presence of neurofibrillary tangles in the brain. The Drosophila TTBK homolog, Asator, is an essential protein that localizes to the mitotic spindle during mitosis and may be involved in regulating microtubule dynamics and function. The TTBK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 66.51  E-value: 3.73e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391   4 YMVLRMIGEGSFGRALLVQHESSNQMFAMKeirLPKSFSNTQNSRKEAVLLAKM---KH-PNIVAFKESfeaEGHLYIVM 79
Cdd:cd14017   2 WKVVKKIGGGGFGEIYKVRDVVDGEEVAMK---VESKSQPKQVLKMEVAVLKKLqgkPHfCRLIGCGRT---ERYNYIVM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23510391  80 EYCdGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNG----KVKLGDFGSARLLSN- 154
Cdd:cd14017  76 TLL-GPNLAELRRSQPRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIGRGPsderTVYILDFGLARQYTNk 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23510391 155 ------PMAFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYEL--CTLkhpfqanSWKNL 210
Cdd:cd14017 155 dgeverPPRNAAGFRGTVRYASVNAHRNKEQGRRDDLWSWFYMLIEFvtGQL-------PWRKL 211
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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