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Conserved domains on  [gi|334185276|ref|NP_001189867|]
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NIMA-related kinase 7 [Arabidopsis thaliana]

Protein Classification

protein kinase family protein( domain architecture ID 229378)

protein kinase family protein may catalyze the transfer of the gamma-phosphoryl group from ATP to substrates such as serine/threonine and/or tyrosine residues on proteins, or may be a pseudokinase

CATH:  1.10.510.10
PubMed:  16244704
SCOP:  4003661

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
18-283 1.38e-89

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member cd08215:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 258  Bit Score: 277.04  E-value: 1.38e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  18 NYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAKHTDKLKQTALQEIsravinydlmKLLSSLKNPYIVHYEDSWID 97
Cdd:cd08215    1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMSEKEREEALNEV----------KLLSKLKHPNIVKYYESFEE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  98 NDNnACIFTAYYEGGNMANAIKKAR--GKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGL 175
Cdd:cd08215   71 NGK-LCIVMEYADGGDLAQKIKKQKkkGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGI 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 176 AKLINPEKPV--SMVsGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPLPIVYS 253
Cdd:cd08215  150 SKVLESTTDLakTVV-GTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYPPIPSQYS 228
                        250       260       270
                 ....*....|....*....|....*....|
gi 334185276 254 STLKQMIKLMLRKKPEYRPTACELLRNPSL 283
Cdd:cd08215  229 SELRDLVNSMLQKDPEKRPSANEILSSPFI 258
 
Name Accession Description Interval E-value
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
18-283 1.38e-89

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: 277.04  E-value: 1.38e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  18 NYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAKHTDKLKQTALQEIsravinydlmKLLSSLKNPYIVHYEDSWID 97
Cdd:cd08215    1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMSEKEREEALNEV----------KLLSKLKHPNIVKYYESFEE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  98 NDNnACIFTAYYEGGNMANAIKKAR--GKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGL 175
Cdd:cd08215   71 NGK-LCIVMEYADGGDLAQKIKKQKkkGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGI 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 176 AKLINPEKPV--SMVsGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPLPIVYS 253
Cdd:cd08215  150 SKVLESTTDLakTVV-GTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYPPIPSQYS 228
                        250       260       270
                 ....*....|....*....|....*....|
gi 334185276 254 STLKQMIKLMLRKKPEYRPTACELLRNPSL 283
Cdd:cd08215  229 SELRDLVNSMLQKDPEKRPSANEILSSPFI 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
19-281 9.19e-56

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 188.51  E-value: 9.19e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276    19 YHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLaKHTDKLKQTALQEIsravinydlmKLLSSLKNPYIVHYEDSWIDN 98
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKK-KKIKKDRERILREI----------KILKKLKHPNIVRLYDVFEDE 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276    99 DNNaCIFTAYYEGGNMANAIKKARGklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKL 178
Cdd:smart00220  70 DKL-YLVMEYCEGGDLFDLLKKRGR--LSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQ 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276   179 INPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPD----MAGLINKINRSLMSPLPIVySS 254
Cdd:smart00220 147 LDPGEKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDqlleLFKKIGKPKPPFPPPEWDI-SP 225
                          250       260
                   ....*....|....*....|....*..
gi 334185276   255 TLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:smart00220 226 EAKDLIRKLLVKDPEKRLTAEEALQHP 252
Pkinase pfam00069
Protein kinase domain;
19-281 2.52e-35

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 132.37  E-value: 2.52e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276   19 YHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAKHTDKLKQTALQEIsravinydlmKLLSSLKNPYIVHYEDSWIDN 98
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREI----------KILKKLNHPNIVRLYDAFEDK 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276   99 DNnACIFTAYYEGGNMANAIKkaRGKLFPEERIFKWLAQLLLAVNylhsnrvvhmdltcsniflpkddhvqlgnyglakl 178
Cdd:pfam00069  71 DN-LYLVLEYVEGGSLFDLLS--EKGAFSEREAKFIMKQILEGLE----------------------------------- 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  179 iNPEKPVSMVsGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKI--NRSLMSPLPIVYSSTL 256
Cdd:pfam00069 113 -SGSSLTTFV-GTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIidQPYAFPELPSNLSEEA 190
                         250       260
                  ....*....|....*....|....*
gi 334185276  257 KQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:pfam00069 191 KDLLKKLLKKDPSKRLTATQALQHP 215
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
16-279 3.90e-29

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 120.89  E-value: 3.90e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  16 LDNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAKHTD-KLKQTALQEIsravinydlmKLLSSLKNPYIVHYEDS 94
Cdd:COG0515    6 LGRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADpEARERFRREA----------RALARLNHPNIVRVYDV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  95 WIDnDNNACIFTAYYEGGNMANAIKkARGKLfPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYG 174
Cdd:COG0515   76 GEE-DGRPYLVMEYVEGESLADLLR-RRGPL-PPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 175 LAKLINPE--KPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPLPIV- 251
Cdd:COG0515  153 IARALGGAtlTQTGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELr 232
                        250       260       270
                 ....*....|....*....|....*....|
gi 334185276 252 --YSSTLKQMIKLMLRKKPEYRPTACELLR 279
Cdd:COG0515  233 pdLPPALDAIVLRALAKDPEERYQSAAELA 262
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
29-284 5.70e-24

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 105.48  E-value: 5.70e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  29 KSSSDFVVLHDIEDKKYAMKKI-CLAkhtdklkqtalqeisrAVINYDLMKllsslknpyivHYEDswIDNDNNACIFTA 107
Cdd:PTZ00267  95 KVVAKFVMLNDERQAAYARSELhCLA----------------ACDHFGIVK-----------HFDD--FKSDDKLLLIME 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 108 YYEGGNMANAIKKARGKLFP--EERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPV 185
Cdd:PTZ00267 146 YGSGGDLNKQIKQRLKEHLPfqEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQYSDSVSL 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 186 SMVS---GISNSMCPEVLEDQPYGYKSDIWSLGCCMYE-ITAHQPaFKAPDMAGLINKINRSLMSPLPIVYSSTLKQMIK 261
Cdd:PTZ00267 226 DVASsfcGTPYYLAPELWERKRYSKKADMWSLGVILYElLTLHRP-FKGPSQREIMQQVLYGKYDPFPCPVSSGMKALLD 304
                        250       260
                 ....*....|....*....|...
gi 334185276 262 LMLRKKPEYRPTACELLRNPSLQ 284
Cdd:PTZ00267 305 PLLSKNPALRPTTQQLLHTEFLK 327
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
120-226 9.35e-07

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 51.72  E-value: 9.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 120 KARGKLFPEERIfKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINpekpvsmVSGI--SNSM-- 195
Cdd:NF033483  99 REHGPLSPEEAV-EIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIARALS-------STTMtqTNSVlg 170
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 334185276 196 -----CPEVLEDQPYGYKSDIWSLGCCMYE-ITAHQP 226
Cdd:NF033483 171 tvhylSPEQARGGTVDARSDIYSLGIVLYEmLTGRPP 207
 
Name Accession Description Interval E-value
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
18-283 1.38e-89

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: 277.04  E-value: 1.38e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  18 NYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAKHTDKLKQTALQEIsravinydlmKLLSSLKNPYIVHYEDSWID 97
Cdd:cd08215    1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMSEKEREEALNEV----------KLLSKLKHPNIVKYYESFEE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  98 NDNnACIFTAYYEGGNMANAIKKAR--GKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGL 175
Cdd:cd08215   71 NGK-LCIVMEYADGGDLAQKIKKQKkkGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGI 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 176 AKLINPEKPV--SMVsGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPLPIVYS 253
Cdd:cd08215  150 SKVLESTTDLakTVV-GTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYPPIPSQYS 228
                        250       260       270
                 ....*....|....*....|....*....|
gi 334185276 254 STLKQMIKLMLRKKPEYRPTACELLRNPSL 283
Cdd:cd08215  229 SELRDLVNSMLQKDPEKRPSANEILSSPFI 258
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
19-281 1.23e-60

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: 201.51  E-value: 1.23e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  19 YHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAKHTDKLKQTALQEisravinydlMKLLSSLKNPYIVHYEDSWIDN 98
Cdd:cd08223    2 YQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKAAEQE----------AKLLSKLKHPNIVSYKESFEGE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  99 DNNACIFTAYYEGGNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKL 178
Cdd:cd08223   72 DGFLYIVMGFCEGGDLYTRLKEQKGVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARV 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 179 InpEKPVSMVS---GISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPLPIVYSST 255
Cdd:cd08223  152 L--ESSSDMATtliGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEGKLPPMPKQYSPE 229
                        250       260
                 ....*....|....*....|....*.
gi 334185276 256 LKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd08223  230 LGELIKAMLHQDPEKRPSVKRILRQP 255
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
42-283 1.48e-59

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: 198.79  E-value: 1.48e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  42 DKK-YAMKKICLAKHTDKLKQTALQEISravinydlmkLLSSLKNPYIVHYEDSWIDnDNNACIFTAYYEGGNMANAIKK 120
Cdd:cd08529   24 DGRvYALKQIDISRMSRKMREEAIDEAR----------VLSKLNSPYVIKYYDSFVD-KGKLNIVMEYAENGDLHSLIKS 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 121 ARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSM-VSGISNSMCPEV 199
Cdd:cd08529   93 QRGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAKILSDTTNFAQtIVGTPYYLSPEL 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 200 LEDQPYGYKSDIWSLGCCMYEI-TAHQPaFKAPDMAGLINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELL 278
Cdd:cd08529  173 CEDKPYNEKSDVWALGCVLYELcTGKHP-FEAQNQGALILKIVRGKYPPISASYSQDLSQLIDSCLTKDYRQRPDTTELL 251

                 ....*
gi 334185276 279 RNPSL 283
Cdd:cd08529  252 RNPSL 256
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
18-283 5.16e-57

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: 192.37  E-value: 5.16e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  18 NYHVVEQVRRGKSSSDFVVLHdIEDKK-YAMKKICLAKHTDKLKQTALQEISravinydlmkLLSSLKNPYIVHYEDSWI 96
Cdd:cd08217    1 DYEVLETIGKGSFGTVRKVRR-KSDGKiLVWKEIDYGKMSEKEKQQLVSEVN----------ILRELKHPNIVRYYDRIV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  97 DNDNnACIF--TAYYEGGNMANAIKKAR--GKLFPEERIFKWLAQLLLAVNYLH-----SNRVVHMDLTCSNIFLPKDDH 167
Cdd:cd08217   70 DRAN-TTLYivMEYCEGGDLAQLIKKCKkeNQYIPEEFIWKIFTQLLLALYECHnrsvgGGKILHRDLKPANIFLDSDNN 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 168 VQLGNYGLAKLINPEkpvSMVS----GISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRS 243
Cdd:cd08217  149 VKLGDFGLARVLSHD---SSFAktyvGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAANQLELAKKIKEG 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 334185276 244 LMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRNPSL 283
Cdd:cd08217  226 KFPRIPSRYSSELNEVIKSMLNVDPDKRPSVEELLQLPLI 265
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
19-281 9.19e-56

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 188.51  E-value: 9.19e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276    19 YHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLaKHTDKLKQTALQEIsravinydlmKLLSSLKNPYIVHYEDSWIDN 98
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKK-KKIKKDRERILREI----------KILKKLKHPNIVRLYDVFEDE 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276    99 DNNaCIFTAYYEGGNMANAIKKARGklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKL 178
Cdd:smart00220  70 DKL-YLVMEYCEGGDLFDLLKKRGR--LSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQ 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276   179 INPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPD----MAGLINKINRSLMSPLPIVySS 254
Cdd:smart00220 147 LDPGEKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDqlleLFKKIGKPKPPFPPPEWDI-SP 225
                          250       260
                   ....*....|....*....|....*..
gi 334185276   255 TLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:smart00220 226 EAKDLIRKLLVKDPEKRLTAEEALQHP 252
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
18-283 2.10e-55

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: 187.87  E-value: 2.10e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  18 NYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAKHTDKLKQTALQEIsravinydlmkLLSSLKNPYIVHYEDSWiD 97
Cdd:cd08219    1 QYNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIRLPKSSSAVEDSRKEAV-----------LLAKMKHPNIVAFKESF-E 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  98 NDNNACIFTAYYEGGNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAK 177
Cdd:cd08219   69 ADGHLYIVMEYCDGGDLMQKIKLQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSAR 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 178 LI-NPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPLPIVYSSTL 256
Cdd:cd08219  149 LLtSPGAYACTYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGSYKPLPSHYSYEL 228
                        250       260
                 ....*....|....*....|....*..
gi 334185276 257 KQMIKLMLRKKPEYRPTACELLRNPSL 283
Cdd:cd08219  229 RSLIKQMFKRNPRSRPSATTILSRGSL 255
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
18-283 3.90e-55

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: 187.21  E-value: 3.90e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  18 NYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAKHTDKLKQTALQEIsravinydlmKLLSSLKNPYIVHYEDSWID 97
Cdd:cd08530    1 DFKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLGSLSQKEREDSVNEI----------RLLASVNHPNIIRYKEAFLD 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  98 NdNNACIFTAYYEGGNMANAIKKAR--GKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGL 175
Cdd:cd08530   71 G-NRLCIVMEYAPFGDLSKLISKRKkkRRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGI 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 176 AKLINpEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPLPIVYSST 255
Cdd:cd08530  150 SKVLK-KNLAKTQIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQELRYKVCRGKFPPIPPVYSQD 228
                        250       260
                 ....*....|....*....|....*...
gi 334185276 256 LKQMIKLMLRKKPEYRPTACELLRNPSL 283
Cdd:cd08530  229 LQQIIRSLLQVNPKKRPSCDKLLQSPAV 256
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
19-281 5.52e-50

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: 173.46  E-value: 5.52e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  19 YHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAKHTDKLKQTALQEIsravinydlmKLLSSLKNPYIVHYEDSWIDN 98
Cdd:cd08218    2 YVRIKKIGEGSFGKALLVKSKEDGKQYVIKEINISKMSPKEREESRKEV----------AVLSKMKHPNIVQYQESFEEN 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  99 dNNACIFTAYYEGGNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKL 178
Cdd:cd08218   72 -GNLYIVMDYCDGGDLYKRINAQRGVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARV 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 179 INPEKPVSMVS-GISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPLPIVYSSTLK 257
Cdd:cd08218  151 LNSTVELARTCiGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKIIRGSYPPVPSRYSYDLR 230
                        250       260
                 ....*....|....*....|....
gi 334185276 258 QMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd08218  231 SLVSQLFKRNPRDRPSINSILEKP 254
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
19-281 6.15e-50

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: 173.38  E-value: 6.15e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  19 YHVVEQVRRGKSSSDFVVlhdiEDKKyamkkiclAKHTDKLKqtALQEISRAVINYDLM-------KLLSSLKNPYIVHY 91
Cdd:cd08222    2 YRVVRKLGSGNFGTVYLV----SDLK--------ATADEELK--VLKEISVGELQPDETvdanreaKLLSKLDHPAIVKF 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  92 EDSWIDNDNnACIFTAYYEGGNMANAIK--KARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLpKDDHVQ 169
Cdd:cd08222   68 HDSFVEKES-FCIVTEYCEGGDLDDKISeyKKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFL-KNNVIK 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 170 LGNYGLAK-LINPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPL 248
Cdd:cd08222  146 VGDFGISRiLMGTSDLATTFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVEGETPSL 225
                        250       260       270
                 ....*....|....*....|....*....|...
gi 334185276 249 PIVYSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd08222  226 PDKYSKELNAIYSRMLNKDPALRPSAAEILKIP 258
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
18-278 5.55e-48

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: 168.22  E-value: 5.55e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  18 NYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAKHTD-KLKQTALQEIsravinydlmKLLSSLKNPYIVHYEDSWI 96
Cdd:cd08224    1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQIFEMMDaKARQDCLKEI----------DLLQQLNHPNIIKYLASFI 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  97 DNdNNACIFTAYYEGGNMANAIKKAR--GKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYG 174
Cdd:cd08224   71 EN-NELNIVLELADAGDLSRLIKHFKkqKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 175 LAKLINPEKPV--SMVsGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMA--GLINKINRSLMSPLP- 249
Cdd:cd08224  150 LGRFFSSKTTAahSLV-GTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYGEKMNlySLCKKIEKCEYPPLPa 228
                        250       260
                 ....*....|....*....|....*....
gi 334185276 250 IVYSSTLKQMIKLMLRKKPEYRPTACELL 278
Cdd:cd08224  229 DLYSQELRDLVAACIQPDPEKRPDISYVL 257
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
27-281 3.97e-47

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: 164.37  E-value: 3.97e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  27 RGKSSSDFVVLHDIEDKKYAMKKICLAKhTDKLKQTALQEIsravinydlmKLLSSLKNPYIVHYEDSWIDNDNNaCIFT 106
Cdd:cd00180    3 KGSFGKVYKARDKETGKKVAVKVIPKEK-LKKLLEELLREI----------EILKKLNHPNIVKLYDVFETENFL-YLVM 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 107 AYYEGGNMANAIKKARGKlFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVS 186
Cdd:cd00180   71 EYCEGGSLKDLLKENKGP-LSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLL 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 187 MVSGISNS---MCPEVLEDQPYGYKSDIWSLGCCMYEItahqpafkapdmaglinkinrslmsplpivysSTLKQMIKLM 263
Cdd:cd00180  150 KTTGGTTPpyyAPPELLGGRYYGPKVDIWSLGVILYEL--------------------------------EELKDLIRRM 197
                        250
                 ....*....|....*...
gi 334185276 264 LRKKPEYRPTACELLRNP 281
Cdd:cd00180  198 LQYDPKKRPSAKELLEHL 215
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
43-281 3.48e-45

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: 160.38  E-value: 3.48e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  43 KKYAMKKICLAKHTDKLKQTALQEIsravinydlmKLLSSLKNPYIVHYEDSWIDNdNNACIFTAYYEGGNMANAIKKAR 122
Cdd:cd06606   26 ELMAVKEVELSGDSEEELEALEREI----------RILSSLKHPNIVRYLGTERTE-NTLNIFLEYVPGGSLASLLKKFG 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 123 GklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNS---MCPEV 199
Cdd:cd06606   95 K--LPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKRLAEIATGEGTKSLRGTpywMAPEV 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 200 LEDQPYGYKSDIWSLGCCMYE-ITAHQPAFKAPDMAGLINKINRSLMSP-LPIVYSSTLKQMIKLMLRKKPEYRPTACEL 277
Cdd:cd06606  173 IRGEGYGRAADIWSLGCTVIEmATGKPPWSELGNPVAALFKIGSSGEPPpIPEHLSEEAKDFLRKCLQRDPKKRPTADEL 252

                 ....
gi 334185276 278 LRNP 281
Cdd:cd06606  253 LQHP 256
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
18-281 8.86e-44

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: 156.43  E-value: 8.86e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  18 NYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAKHTDKLKQTALQEIsravinydlmKLLSSLKNPYIVHYEDSWID 97
Cdd:cd08220    1 KYEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIPVEQMTKEERQAALNEV----------KVLSMLHHPNIIEYYESFLE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  98 nDNNACIFTAYYEGGNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDH-VQLGNYGLA 176
Cdd:cd08220   71 -DKALMIVMEYAPGGTLFEYIQQRKGSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTvVKIGDFGIS 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 177 KLINPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPLPIVYSSTL 256
Cdd:cd08220  150 KILSSKSKAYTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMRGTFAPISDRYSEEL 229
                        250       260
                 ....*....|....*....|....*
gi 334185276 257 KQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd08220  230 RHLILSMLHLDPNKRPTLSEIMAQP 254
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
19-281 8.62e-42

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


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 151.20  E-value: 8.62e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  19 YHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKIclaKHTDKLKQTA-LQEIsravinydlmKLLSSLKNPYIVHYEDSWID 97
Cdd:cd05122    2 FEILEKIGKGGFGVVYKARHKKTGQIVAIKKI---NLESKEKKESiLNEI----------AILKKCKHPNIVKYYGSYLK 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  98 NDNnACIFTAYYEGGNMANAIKKaRGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAK 177
Cdd:cd05122   69 KDE-LWIVMEFCSGGSLKDLLKN-TNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSA 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 178 LINPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAF-KAPDMAGLInKINRSLMSPLPI--VYSS 254
Cdd:cd05122  147 QLSDGKTRNTFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYsELPPMKALF-LIATNGPPGLRNpkKWSK 225
                        250       260
                 ....*....|....*....|....*..
gi 334185276 255 TLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd05122  226 EFKDFLKKCLQKDPEKRPTAEQLLKHP 252
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
18-283 2.76e-41

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: 149.72  E-value: 2.76e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  18 NYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAKHTDKLKQTALQEISravinydlmkLLSSLKNPYIVHYEDSWID 97
Cdd:cd08225    1 RYEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKEKEASKKEVI----------LLAKMKHPNIVTFFASFQE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  98 NdNNACIFTAYYEGGNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHV-QLGNYGLA 176
Cdd:cd08225   71 N-GRLFIVMEYCDGGDLMKRINRQRGVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVaKLGDFGIA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 177 KLINPEKPVSMV-SGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPLPIVYSST 255
Cdd:cd08225  150 RQLNDSMELAYTcVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNNLHQLVLKICQGYFAPISPNFSRD 229
                        250       260
                 ....*....|....*....|....*...
gi 334185276 256 LKQMIKLMLRKKPEYRPTACELLRNPSL 283
Cdd:cd08225  230 LRSLISQLFKVSPRDRPSITSILKRPFL 257
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
48-283 1.53e-40

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: 147.96  E-value: 1.53e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  48 KKICLAKHTDKLKQTALQEISravinydlmkLLSSLKNPYIVHYEDSWIDNdNNACIFTAYYEGGNMANAIKKARGKLFP 127
Cdd:cd08221   31 KEVNLSRLSEKERRDALNEID----------ILSLLNHDNIITYYNHFLDG-ESLFIEMEYCNGGNLHDKIAQQKNQLFP 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 128 EERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKpvSMVSGISNS---MCPEVLEDQP 204
Cdd:cd08221  100 EEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVLDSES--SMAESIVGTpyyMSPELVQGVK 177
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185276 205 YGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRNPSL 283
Cdd:cd08221  178 YNFKSDIWAVGCVLYELLTLKRTFDATNPLRLAVKIVQGEYEDIDEQYSEEIIQLVHDCLHQDPEDRPTAEELLERPLL 256
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
46-281 4.41e-40

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: 146.60  E-value: 4.41e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  46 AMKKICLAKHTDKLKQTALQEIsravinydlmKLLSSLKNPYIVHYEDSwIDNDNNACIFTAYYEGGNMANAIKKArGKl 125
Cdd:cd06627   29 AIKQISLEKIPKSDLKSVMGEI----------DLLKKLNHPNIVKYIGS-VKTKDSLYIILEYVENGSLASIIKKF-GK- 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 126 FPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLA-KLINPEKPVSMVSGISNSMCPEVLEDQP 204
Cdd:cd06627   96 FPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVAtKLNEVEKDENSVVGTPYWMAPEVIEMSG 175
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334185276 205 YGYKSDIWSLGCCMYE-ITAHQPAFKAPDMAGLINKINRSLMsPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd06627  176 VTTASDIWSVGCTVIElLTGNPPYYDLQPMAALFRIVQDDHP-PLPENISPELRDFLLQCFQKDPTLRPSAKELLKHP 252
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
45-281 8.61e-40

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: 146.01  E-value: 8.61e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  45 YAMKKICLAKhTDKLKQTALQEISRAVinydlmKLLSSLKNPYIVHYEDSWIDNDNnACIFTAYYEGGNMANAIKKArGK 124
Cdd:cd06632   28 FAVKEVSLVD-DDKKSRESVKQLEQEI------ALLSKLRHPNIVQYYGTEREEDN-LYIFLEYVPGGSIHKLLQRY-GA 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 125 lFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNSMCPEVL--ED 202
Cdd:cd06632   99 -FEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHVEAFSFAKSFKGSPYWMAPEVImqKN 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 203 QPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSP-LPIVYSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd06632  178 SGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIGNSGELPpIPDHLSPDAKDFIRLCLQRDPEDRPTASQLLEHP 257
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
18-277 1.08e-39

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: 146.11  E-value: 1.08e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  18 NYHVVEQVRRGKSSSDFVVL-HDIEDKKYAMKKICLAKHTDKLKQTALQEISRAVINyDLMKLLSSLKNPYIVHYEDSWI 96
Cdd:cd08528    1 EYAVLELLGSGAFGCVYKVRkKSNGQTLLALKEINMTNPAFGRTEQERDKSVGDIIS-EVNIIKEQLRHPNIVRYYKTFL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  97 DNDNnACIFTAYYEG---GNMANAIKKARGKlFPEERIFKWLAQLLLAVNYLHSNR-VVHMDLTCSNIFLPKDDHVQLGN 172
Cdd:cd08528   80 ENDR-LYIVMELIEGaplGEHFSSLKEKNEH-FTEDRIWNIFVQMVLALRYLHKEKqIVHRDLKPNNIMLGEDDKVTITD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 173 YGLAKLINPE--KPVSMVSGISNSmCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPLP- 249
Cdd:cd08528  158 FGLAKQKGPEssKMTSVVGTILYS-CPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIVEAEYEPLPe 236
                        250       260
                 ....*....|....*....|....*...
gi 334185276 250 IVYSSTLKQMIKLMLRKKPEYRPTACEL 277
Cdd:cd08528  237 GMYSDDITFVIRSCLTPDPEARPDIVEV 264
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
42-281 2.77e-37

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: 138.84  E-value: 2.77e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  42 DKKYAMKKIC---LAKHtdKLKQTALQEIsravinydlmKLLSSLKNPYIVHYEDSWIDnDNNACIFTAYYEGGNMaNAI 118
Cdd:cd14099   26 GKVYAGKVVPkssLTKP--KQREKLKSEI----------KIHRSLKHPNIVKFHDCFED-EENVYILLELCSNGSL-MEL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 119 KKARGKLF-PEERIFkwLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINP--EKPVSMVsGISNSM 195
Cdd:cd14099   92 LKRRKALTePEVRYF--MRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAARLEYdgERKKTLC-GTPNYI 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 196 CPEVLE-DQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKI-NRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPT 273
Cdd:cd14099  169 APEVLEkKKGHSFEVDIWSLGVILYTLLVGKPPFETSDVKETYKRIkKNEYSFPSHLSISDEAKDLIRSMLQPDPTKRPS 248

                 ....*...
gi 334185276 274 ACELLRNP 281
Cdd:cd14099  249 LDEILSHP 256
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
18-281 7.57e-37

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: 137.65  E-value: 7.57e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  18 NYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAKHTDKLKQTALQEIsravinyDLMKLLsslKNPYIVHYEDSwID 97
Cdd:cd14003    1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIEEKIKREI-------EIMKLL---NHPNIIKLYEV-IE 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  98 NDNNACIFTAYYEGGNMANAIKKaRGKLFPEE--RIFKwlaQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGL 175
Cdd:cd14003   70 TENKIYLVMEYASGGELFDYIVN-NGRLSEDEarRFFQ---QLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 176 AKLINPEKPVSMVSGISNSMCPEVLEDQPY-GYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMsPLPIVYSS 254
Cdd:cd14003  146 SNEFRGGSLLKTFCGTPAYAAPEVLLGRKYdGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKY-PIPSHLSP 224
                        250       260
                 ....*....|....*....|....*..
gi 334185276 255 TLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd14003  225 DARDLIRRMLVVDPSKRITIEEILNHP 251
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
16-272 1.04e-36

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: 137.85  E-value: 1.04e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  16 LDNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAKHTD-KLKQTALQEISravinydlmkLLSSLKNPYIVHYEDS 94
Cdd:cd08228    1 LANFQIEKKIGRGQFSEVYRATCLLDRKPVALKKVQIFEMMDaKARQDCVKEID----------LLKQLNHPNVIKYLDS 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  95 WIDnDNNACIFTAYYEGGNMANAIK--KARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGN 172
Cdd:cd08228   71 FIE-DNELNIVLELADAGDLSQMIKyfKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGD 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 173 YGLAKLINPEKPV--SMVsGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMA--GLINKINRSLMSPL 248
Cdd:cd08228  150 LGLGRFFSSKTTAahSLV-GTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNlfSLCQKIEQCDYPPL 228
                        250       260
                 ....*....|....*....|....*
gi 334185276 249 PIV-YSSTLKQMIKLMLRKKPEYRP 272
Cdd:cd08228  229 PTEhYSEKLRELVSMCIYPDPDQRP 253
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
18-279 3.72e-36

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: 135.79  E-value: 3.72e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  18 NYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKI--CLAkHTDKLKQTALQEisravinydlMKLLSSLKNPYIVHYEDSW 95
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLrpELA-EDEEFRERFLRE----------ARALARLSHPNIVRVYDVG 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  96 IDNDNnACIFTAYYEGGNMANAIKKaRGKLfPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGL 175
Cdd:cd14014   70 EDDGR-PYIVMEYVEGGSLADLLRE-RGPL-PPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGI 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 176 AKLINPEK--PVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRS---LMSPLPI 250
Cdd:cd14014  147 ARALGDSGltQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEappPPSPLNP 226
                        250       260       270
                 ....*....|....*....|....*....|
gi 334185276 251 VYSSTLKQMIKLMLRKKPEYRP-TACELLR 279
Cdd:cd14014  227 DVPPALDAIILRALAKDPEERPqSAAELLA 256
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
18-281 7.39e-36

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: 134.91  E-value: 7.39e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  18 NYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAKHTDKLKQTALQEISravinydlmkLLSSLKNPYIVHYEDsWID 97
Cdd:cd05117    1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEDEEMLRREIE----------ILKRLDHPNIVKLYE-VFE 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  98 NDNNACIFTAYYEGGNMANAIKKaRGKlFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFL---PKDDHVQLGNYG 174
Cdd:cd05117   70 DDKNLYLVMELCTGGELFDRIVK-KGS-FSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLaskDPDSPIKIIDFG 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 175 LAKLINPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINR---SLMSPLPIV 251
Cdd:cd05117  148 LAKIFEEGEKLKTVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKgkySFDSPEWKN 227
                        250       260       270
                 ....*....|....*....|....*....|
gi 334185276 252 YSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd05117  228 VSEEAKDLIKRLLVVDPKKRLTAAEALNHP 257
Pkinase pfam00069
Protein kinase domain;
19-281 2.52e-35

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 132.37  E-value: 2.52e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276   19 YHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAKHTDKLKQTALQEIsravinydlmKLLSSLKNPYIVHYEDSWIDN 98
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREI----------KILKKLNHPNIVRLYDAFEDK 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276   99 DNnACIFTAYYEGGNMANAIKkaRGKLFPEERIFKWLAQLLLAVNylhsnrvvhmdltcsniflpkddhvqlgnyglakl 178
Cdd:pfam00069  71 DN-LYLVLEYVEGGSLFDLLS--EKGAFSEREAKFIMKQILEGLE----------------------------------- 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  179 iNPEKPVSMVsGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKI--NRSLMSPLPIVYSSTL 256
Cdd:pfam00069 113 -SGSSLTTFV-GTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIidQPYAFPELPSNLSEEA 190
                         250       260
                  ....*....|....*....|....*
gi 334185276  257 KQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:pfam00069 191 KDLLKKLLKKDPSKRLTATQALQHP 215
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
22-274 3.84e-34

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: 129.94  E-value: 3.84e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  22 VEQVRRgKSSsdfvvlhdieDKKYAMKKIclakHTDKLKQTALQEISRAVINydlmkLLSSLKNPYIV--HYedSWIDnD 99
Cdd:cd05123    9 VLLVRK-KDT----------GKLYAMKVL----RKKEIIKRKEVEHTLNERN-----ILERVNHPFIVklHY--AFQT-E 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 100 NNACIFTAYYEGGNMANAIKKARgkLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLI 179
Cdd:cd05123   66 EKLYLVLDYVPGGELFSHLSKEG--RFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKEL 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 180 --NPEKPVSMVsGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKInrsLMSPL--PIVYSST 255
Cdd:cd05123  144 ssDGDRTYTFC-GTPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKI---LKSPLkfPEYVSPE 219
                        250
                 ....*....|....*....
gi 334185276 256 LKQMIKLMLRKKPEYRPTA 274
Cdd:cd05123  220 AKSLISGLLQKDPTKRLGS 238
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
34-281 1.29e-33

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: 128.84  E-value: 1.29e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  34 FVVLHDIEDKKYAmkKICLAKHTDKLKQT--ALQEISRAVINYDL--------MKLLSSLKNPYIVH-YEdsWIDNDNNA 102
Cdd:cd14080    2 YRLGKTIGEGSYS--KVKLAEYTKSGLKEkvACKIIDKKKAPKDFlekflpreLEILRKLRHPNIIQvYS--IFERGSKV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 103 CIFTAYYEGGNMANAIKKaRGKLfPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPE 182
Cdd:cd14080   78 FIFMEYAEHGDLLEYIQK-RGAL-SESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFARLCPDD 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 183 KPVSMvsgiSNSMC-------PEVLEDQPY-GYKSDIWSLGCCMY-EITAHQPaFKAPDMAGLI-NKINRSL-MSPLPIV 251
Cdd:cd14080  156 DGDVL----SKTFCgsaayaaPEILQGIPYdPKKYDIWSLGVILYiMLCGSMP-FDDSNIKKMLkDQQNRKVrFPSSVKK 230
                        250       260       270
                 ....*....|....*....|....*....|
gi 334185276 252 YSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd14080  231 LSPECKDLIDQLLEPDPTKRATIEEILNHP 260
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
17-281 1.76e-33

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: 128.14  E-value: 1.76e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  17 DNYHVVEQVRRG----------KSSSDFVvlhdiedkkyAMKKICLAKHTDKLKQTALQEIsravinyDLMKllsSLKNP 86
Cdd:cd14002    1 ENYHVLELIGEGsfgkvykgrrKYTGQVV----------ALKFIPKRGKSEKELRNLRQEI-------EILR---KLNHP 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  87 YIVHYEDSwIDNDNNACIFTAYyeggnmanaikkARGKLF---------PEERIFKWLAQLLLAVNYLHSNRVVHMDLTC 157
Cdd:cd14002   61 NIIEMLDS-FETKKEFVVVTEY------------AQGELFqileddgtlPEEEVRSIAKQLVSALHYLHSNRIIHRDMKP 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 158 SNIFLPKDDHVQLGNYGLAKLINPEKPV-SMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGL 236
Cdd:cd14002  128 QNILIGKGGVVKLCDFGFARAMSCNTLVlTSIKGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNSIYQL 207
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 334185276 237 INKINRSlmsplPIVY----SSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd14002  208 VQMIVKD-----PVKWpsnmSPEFKSFLQGLLNKDPSKRLSWPDLLEHP 251
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
27-286 3.03e-33

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: 127.71  E-value: 3.03e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  27 RGKSSSDFVVLHDIEDKKYAMKKIcLAKHTDKLKQTALQEIsravinydlmKLLSSLKNPYIVHYEDSWIDNdNNACIFT 106
Cdd:cd06623   11 QGSSGVVYKVRHKPTGKIYALKKI-HVDGDEEFRKQLLREL----------KTLRSCESPYVVKCYGAFYKE-GEISIVL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 107 AYYEGGNMANAIKKArgKLFPEERIFKWLAQLLLAVNYLHSNR-VVHMDLTCSNIFLPKDDHVQLGNYGLAKLINP--EK 183
Cdd:cd06623   79 EYMDGGSLADLLKKV--GKIPEPVLAYIARQILKGLDYLHTKRhIIHRDIKPSNLLINSKGEVKIADFGISKVLENtlDQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 184 PVSMVsGISNSMCPEVLEDQPYGYKSDIWSLGCCMYE-ITAHQPaFKAPDMAGLINKINRSLMSPLP----IVYSSTLKQ 258
Cdd:cd06623  157 CNTFV-GTVTYMSPERIQGESYSYAADIWSLGLTLLEcALGKFP-FLPPGQPSFFELMQAICDGPPPslpaEEFSPEFRD 234
                        250       260
                 ....*....|....*....|....*...
gi 334185276 259 MIKLMLRKKPEYRPTACELLRNPSLQPY 286
Cdd:cd06623  235 FISACLQKDPKKRPSAAELLQHPFIKKA 262
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
18-281 8.83e-33

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: 126.34  E-value: 8.83e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  18 NYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKiclAKH---TDKLKQTALQEISRAVinydlmkllsSLK-NPYIVHYED 93
Cdd:cd13997    1 HFHELEQIGSGSFSEVFKVRSKVDGCLYAVKK---SKKpfrGPKERARALREVEAHA----------ALGqHPNIVRYYS 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  94 SWiDNDNNACIFTAYYEGGNMANAIKKA-RGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGN 172
Cdd:cd13997   68 SW-EEGGHLYIQMELCENGSLQDALEELsPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 173 YGLAKLINPEKPVSmvSGISNSMCPEVLEDQP-YGYKSDIWSLGCCMYEITAhqpAFKAPDMAGLINKINRSLMSPLP-I 250
Cdd:cd13997  147 FGLATRLETSGDVE--EGDSRYLAPELLNENYtHLPKADIFSLGVTVYEAAT---GEPLPRNGQQWQQLRQGKLPLPPgL 221
                        250       260       270
                 ....*....|....*....|....*....|.
gi 334185276 251 VYSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd13997  222 VLSQELTRLLKVMLDPDPTRRPTADQLLAHD 252
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
19-284 3.66e-32

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: 124.63  E-value: 3.66e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  19 YHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLakhTDKLKQTALQEISravinydLMKllsSLKNPYIVHYEDSWIDN 98
Cdd:cd06614    2 YKNLEKIGEGASGEVYKATDRATGKEVAIKKMRL---RKQNKELIINEIL-------IMK---ECKHPNIVDYYDSYLVG 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  99 DnnaCIFTA--YYEGGNMANAIKKARGKLfPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLA 176
Cdd:cd06614   69 D---ELWVVmeYMDGGSLTDIITQNPVRM-NESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFA 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 177 KLINPEKP--VSMVsGISNSMCPEVLEDQPYGYKSDIWSLGC-CMYEITAHQPAFKAPDMAGLInKINRSLMSPL--PIV 251
Cdd:cd06614  145 AQLTKEKSkrNSVV-GTPYWMAPEVIKRKDYGPKVDIWSLGImCIEMAEGEPPYLEEPPLRALF-LITTKGIPPLknPEK 222
                        250       260       270
                 ....*....|....*....|....*....|...
gi 334185276 252 YSSTLKQMIKLMLRKKPEYRPTACELLRNPSLQ 284
Cdd:cd06614  223 WSPEFKDFLNKCLVKDPEKRPSAEELLQHPFLK 255
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
16-280 4.19e-32

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: 125.10  E-value: 4.19e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  16 LDNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKIclaKHTDKLKQ--TALQEIsravinydlmKLLSSLKNPYIVHYED 93
Cdd:cd13996    5 LNDFEEIELLGSGGFGSVYKVRNKVDGVTYAIKKI---RLTEKSSAseKVLREV----------KALAKLNHPNIVRYYT 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  94 SWIDnDNNACIFTAYYEGGNMANAIKKARGKLFPEE----RIFKwlaQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDH-V 168
Cdd:cd13996   72 AWVE-EPPLYIQMELCEGGTLRDWIDRRNSSSKNDRklalELFK---QILKGVSYIHSKGIVHRDLKPSNIFLDNDDLqV 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 169 QLGNYGLAKLINPEKPVSMVSGISNS---------------MCPEVLEDQPYGYKSDIWSLGCCMYEI-----TAHQpaf 228
Cdd:cd13996  148 KIGDFGLATSIGNQKRELNNLNNNNNgntsnnsvgigtplyASPEQLDGENYNEKADIYSLGIILFEMlhpfkTAME--- 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 334185276 229 KAPDMAGLIN-KINRSLMSPLPivyssTLKQMIKLMLRKKPEYRPTACELLRN 280
Cdd:cd13996  225 RSTILTDLRNgILPESFKAKHP-----KEADLIQSLLSKNPEERPSAEQLLRS 272
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
17-281 4.45e-32

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


Pssm-ID: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 124.78  E-value: 4.45e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  17 DNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAKHtdklkQTALQEISRAVinydlmKLLSSLKNPYIVHYEDSWI 96
Cdd:cd06610    1 DDYELIEVIGSGATAVVYAAYCLPKKEKVAIKRIDLEKC-----QTSMDELRKEI------QAMSQCNHPNVVSYYTSFV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  97 DnDNNACIFTAYYEGGNMANAIK-KARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGL 175
Cdd:cd06610   70 V-GDELWLVMPLLSGGSLLDIMKsSYPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGV 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 176 AKLInpEKPVSMVSGISNS-------MCPEVLE-DQPYGYKSDIWSLGCCMYE-ITAHQPAFKAPDMAGLINKINrSLMS 246
Cdd:cd06610  149 SASL--ATGGDRTRKVRKTfvgtpcwMAPEVMEqVRGYDFKADIWSFGITAIElATGAAPYSKYPPMKVLMLTLQ-NDPP 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 334185276 247 PLPI-----VYSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd06610  226 SLETgadykKYSKSFRKMISLCLQKDPSKRPTAEELLKHK 265
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
18-281 2.33e-31

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: 122.20  E-value: 2.33e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  18 NYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKkiCLAKhtDKLKQTALQE-ISRAVinydlmKLLSSLKNPYIVHYEDSWI 96
Cdd:cd14007    1 DFEIGKPLGKGKFGNVYLAREKKSGFIVALK--VISK--SQLQKSGLEHqLRREI------EIQSHLRHPNILRLYGYFE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  97 DNDNnacIFTA--YYEGGNMANAIKKArgKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYG 174
Cdd:cd14007   71 DKKR---IYLIleYAPNGELYKELKKQ--KRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFG 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 175 LAKLINPEKPVSMVsGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSpLPIVYSS 254
Cdd:cd14007  146 WSVHAPSNRRKTFC-GTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDIK-FPSSVSP 223
                        250       260
                 ....*....|....*....|....*..
gi 334185276 255 TLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd14007  224 EAKDLISKLLQKDPSKRLSLEQVLNHP 250
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
46-273 5.32e-30

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: 118.02  E-value: 5.32e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  46 AMKKICLAKHTDKLKQTALQEISravinydlmkLLSSLKNPYIVHYEdSWIDNDNNACIFTAYYEGGNMANAIKKARGKL 125
Cdd:cd13999   20 AIKKLKVEDDNDELLKEFRREVS----------ILSKLRHPNIVQFI-GACLSPPPLCIVTEYMPGGSLYDLLHKKKIPL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 126 FPEERIfKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINpEKPVSMVSGISNS--MCPEVLEDQ 203
Cdd:cd13999   89 SWSLRL-KIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKN-STTEKMTGVVGTPrwMAPEVLRGE 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334185276 204 PYGYKSDIWSLGCCMYEITAHQPAFK-APDMAGLINKINRSLMSPLPivySSTLKQMIKLMLR---KKPEYRPT 273
Cdd:cd13999  167 PYTEKADVYSFGIVLWELLTGEVPFKeLSPIQIAAAVVQKGLRPPIP---PDCPPELSKLIKRcwnEDPEKRPS 237
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
35-281 6.46e-30

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: 118.42  E-value: 6.46e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  35 VVLH-DIED-KKYAMK--------KICLAKHTDKLKQTALQEISRAVinyDLMKllsSLKNPYIVH-YEdsWIDNDNNAC 103
Cdd:cd14008    9 VKLAlDTETgQLYAIKifnksrlrKRREGKNDRGKIKNALDDVRREI---AIMK---KLDHPNIVRlYE--VIDDPESDK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 104 IF--TAYYEGGNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINP 181
Cdd:cd14008   81 LYlvLEYCEGGPVMELDSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGVSEMFED 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 182 EKPvsMVSGISNS---MCPEVL--EDQPY-GYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRS-LMSPLPIVYSS 254
Cdd:cd14008  161 GND--TLQKTAGTpafLAPELCdgDSKTYsGKAADIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQnDEFPIPPELSP 238
                        250       260
                 ....*....|....*....|....*..
gi 334185276 255 TLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd14008  239 ELKDLLRRMLEKDPEKRITLKEIKEHP 265
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
43-281 7.36e-30

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: 118.23  E-value: 7.36e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  43 KKYAMKKIclakHTDKLKQTALQEIsRAVINYdlMKLLSSLKNPYIVHYEDSwIDNDNNACIFTAYYEGGNMANAIKKAr 122
Cdd:cd06625   26 RELAVKQV----EIDPINTEASKEV-KALECE--IQLLKNLQHERIVQYYGC-LQDEKSLSIFMEYMPGGSVKDEIKAY- 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 123 GKLfPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAK---LINPEKPVSMVSGISNSMCPEV 199
Cdd:cd06625   97 GAL-TENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASKrlqTICSSTGMKSVTGTPYWMSPEV 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 200 LEDQPYGYKSDIWSLGCCMYE-ITAHQPAFKAPDMAGLInKINRSLMSP-LPIVYSSTLKQMIKLMLRKKPEYRPTACEL 277
Cdd:cd06625  176 INGEGYGRKADIWSVGCTVVEmLTTKPPWAEFEPMAAIF-KIATQPTNPqLPPHVSEDARDFLSLIFVRNKKQRPSAEEL 254

                 ....
gi 334185276 278 LRNP 281
Cdd:cd06625  255 LSHS 258
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
15-272 8.69e-30

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: 118.98  E-value: 8.69e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  15 TLDNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAKHTD-KLKQTALQEISravinydlmkLLSSLKNPYIVHYED 93
Cdd:cd08229   22 TLANFRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIFDLMDaKARADCIKEID----------LLKQLNHPNVIKYYA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  94 SWIDnDNNACIFTAYYEGGNMANAIK--KARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLG 171
Cdd:cd08229   92 SFIE-DNELNIVLELADAGDLSRMIKhfKKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLG 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 172 NYGLAKLINPEKPVS-MVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMA--GLINKINRSLMSPL 248
Cdd:cd08229  171 DLGLGRFFSSKTTAAhSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNlySLCKKIEQCDYPPL 250
                        250       260
                 ....*....|....*....|....*
gi 334185276 249 PI-VYSSTLKQMIKLMLRKKPEYRP 272
Cdd:cd08229  251 PSdHYSEELRQLVNMCINPDPEKRP 275
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
16-279 3.90e-29

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 120.89  E-value: 3.90e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  16 LDNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAKHTD-KLKQTALQEIsravinydlmKLLSSLKNPYIVHYEDS 94
Cdd:COG0515    6 LGRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADpEARERFRREA----------RALARLNHPNIVRVYDV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  95 WIDnDNNACIFTAYYEGGNMANAIKkARGKLfPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYG 174
Cdd:COG0515   76 GEE-DGRPYLVMEYVEGESLADLLR-RRGPL-PPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 175 LAKLINPE--KPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPLPIV- 251
Cdd:COG0515  153 IARALGGAtlTQTGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELr 232
                        250       260       270
                 ....*....|....*....|....*....|
gi 334185276 252 --YSSTLKQMIKLMLRKKPEYRPTACELLR 279
Cdd:COG0515  233 pdLPPALDAIVLRALAKDPEERYQSAAELA 262
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
46-281 5.02e-29

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: 116.00  E-value: 5.02e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  46 AMKKICLakHTDKlKQTALQEISRAVINYDLMKllsSLKNPYIVHYEDSWIDnDNNACIFTAYYEGGNMANAIkkARGKL 125
Cdd:cd06631   29 AVKQVEL--DTSD-KEKAEKEYEKLQEEVDLLK---TLKHVNIVGYLGTCLE-DNVVSIFMEFVPGGSIASIL--ARFGA 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 126 FPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNS-------MCPE 198
Cdd:cd06631  100 LEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGCAKRLCINLSSGSQSQLLKSmrgtpywMAPE 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 199 VLEDQPYGYKSDIWSLGCCMYEITAHQPAF-KAPDMAGL--INKiNRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTAC 275
Cdd:cd06631  180 VINETGHGRKSDIWSIGCTVFEMATGKPPWaDMNPMAAIfaIGS-GRKPVPRLPDKFSPEARDFVHACLTRDQDERPSAE 258

                 ....*.
gi 334185276 276 ELLRNP 281
Cdd:cd06631  259 QLLKHP 264
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
43-281 1.78e-28

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: 114.32  E-value: 1.78e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  43 KKYAMKKICLAKHTDKLKQTAL-QEIsravinyDLMKllsSLKNPYIVHYEDSwIDNDNNACIFTAYYEGGNMANAIKKA 121
Cdd:cd14162   26 CKVAIKIVSKKKAPEDYLQKFLpREI-------EVIK---GLKHPNLICFYEA-IETTSRVYIIMELAENGDLLDYIRKN 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 122 rgKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKliNPEKPVSMVSGISNSMC----- 196
Cdd:cd14162   95 --GALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFAR--GVMKTKDGKPKLSETYCgsyay 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 197 --PEVLEDQPY-GYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEyRPT 273
Cdd:cd14162  171 asPEILRGIPYdPFLSDIWSMGVVLYTMVYGRLPFDDSNLKVLLKQVQRRVVFPKNPTVSEECKDLILRMLSPVKK-RIT 249

                 ....*...
gi 334185276 274 ACELLRNP 281
Cdd:cd14162  250 IEEIKRDP 257
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
18-281 7.45e-28

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: 112.77  E-value: 7.45e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  18 NYHVVEQVRRGKSSsdfvVLHDIEDKK----YAMKKIclakhtDKLKQTalqEISRAVinydlmKLLSSLKNPYIVH-YE 92
Cdd:cd14010    1 NYVLYDEIGRGKHS----VVYKGRRKGtiefVAIKCV------DKSKRP---EVLNEV------RLTHELKHPNVLKfYE 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  93 dsWIDNDNNACIFTAYYEGGNMANAIKKARGklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGN 172
Cdd:cd14010   62 --WYETSNHLWLVVEYCTGGDLETLLRQDGN--LPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSD 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 173 YGLAKLI--NPEKPVSMVSGISNS---------------MCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAG 235
Cdd:cd14010  138 FGLARREgeILKELFGQFSDEGNVnkvskkqakrgtpyyMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFVAESFTE 217
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 334185276 236 LINKInrsLMSPLP-------IVYSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd14010  218 LVEKI---LNEDPPppppkvsSKPSPDFKSLLKGLLEKDPAKRLSWDELVKHP 267
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
51-271 1.74e-26

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: 108.53  E-value: 1.74e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  51 CLAKhtDKLKQTA----LQEIsravinydlmKLLSSLKNPYIVHYED-SWidNDNNACIFTAYYEGGNMANAIKKaRGKL 125
Cdd:cd14121   28 CVSK--SSLNKAStenlLTEI----------ELLKKLKHPHIVELKDfQW--DEEHIYLIMEYCSGGDLSRFIRS-RRTL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 126 fPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFL--PKDDHVQLGNYGLAKLINPEKPVSMVSGISNSMCPEVLEDQ 203
Cdd:cd14121   93 -PESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLssRYNPVLKLADFGFAQHLKPNDEAHSLRGSPLYMAPEMILKK 171
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 204 PYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKI--NRSLMSPLPIVYSSTLKQMIKLMLRKKPEYR 271
Cdd:cd14121  172 KYDARVDLWSVGVILYECLFGRAPFASRSFEELEEKIrsSKPIEIPTRPELSADCRDLLLRLLQRDPDRR 241
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
19-281 2.53e-26

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: 108.12  E-value: 2.53e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  19 YHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLakhtdklkQTALQEISRAVinyDLMKllsSLKNPYIVHYEDSWIdN 98
Cdd:cd06612    5 FDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPV--------EEDLQEIIKEI---SILK---QCDSPYIVKYYGSYF-K 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  99 DNNACIFTAYYEGGNmANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLA-K 177
Cdd:cd06612   70 NTDLWIVMEYCGAGS-VSDIMKITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSgQ 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 178 LINPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGccmyeITA------HQPAFKAPDMAGLINKINR---SLMSPL 248
Cdd:cd06612  149 LTDTMAKRNTVIGTPFWMAPEVIQEIGYNNKADIWSLG-----ITAiemaegKPPYSDIHPMRAIFMIPNKpppTLSDPE 223
                        250       260       270
                 ....*....|....*....|....*....|...
gi 334185276 249 PivYSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd06612  224 K--WSPEFNDFVKKCLVKDPEERPSAIQLLQHP 254
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
43-281 5.00e-26

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: 107.72  E-value: 5.00e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  43 KKYAMKKICLAKHTDKLkQTALQEISravinydlmkLLSSLKNPYIVHYEDSWIDNdNNACIFTAYYEGGNMANAIKKAR 122
Cdd:cd06609   27 QVVAIKVIDLEEAEDEI-EDIQQEIQ----------FLSQCDSPYITKYYGSFLKG-SKLWIIMEYCGGGSVLDLLKPGP 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 123 gklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLI--NPEKPVSMVsGISNSMCPEVL 200
Cdd:cd06609   95 ---LDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSGQLtsTMSKRNTFV-GTPFWMAPEVI 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 201 EDQPYGYKSDIWSLGCCMYEITAHQP--AFKAPdMAGLINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELL 278
Cdd:cd06609  171 KQSGYDEKADIWSLGITAIELAKGEPplSDLHP-MRVLFLIPKNNPPSLEGNKFSKPFKDFVELCLNKDPKERPSAKELL 249

                 ...
gi 334185276 279 RNP 281
Cdd:cd06609  250 KHK 252
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
77-280 9.45e-26

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: 106.55  E-value: 9.45e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  77 MKLLSSLKNPYIV----HYEDSwidndNNACIFTAYYEGGNMANaIKKARGKLF-PEERIFkwLAQLLLAVNYLHSNRVV 151
Cdd:cd14189   52 IELHRDLHHKHVVkfshHFEDA-----ENIYIFLELCSRKSLAH-IWKARHTLLePEVRYY--LKQIISGLKYLHLKGIL 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 152 HMDLTCSNIFLPKDDHVQLGNYGLA-KLINPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKA 230
Cdd:cd14189  124 HRDLKLGNFFINENMELKVGDFGLAaRLEPPEQRKKTICGTPNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFET 203
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 334185276 231 PDMAGLINKInRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRN 280
Cdd:cd14189  204 LDLKETYRCI-KQVKYTLPASLSLPARHLLAGILKRNPGDRLTLDQILEH 252
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
42-280 9.81e-26

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: 106.25  E-value: 9.81e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  42 DKKYAMKKIclaKHTDKLKQTALQEISRAVinydlmKLLSSLKNPYIVHYEDSWIDNDNnACIFTAYYEGGNMANaIKKA 121
Cdd:cd14188   26 NKVYAAKII---PHSRVSKPHQREKIDKEI------ELHRILHHKHVVQFYHYFEDKEN-IYILLEYCSRRSMAH-ILKA 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 122 RgKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINP-EKPVSMVSGISNSMCPEVL 200
Cdd:cd14188   95 R-KVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLEPlEHRRRTICGTPNYLSPEVL 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 201 EDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSpLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRN 280
Cdd:cd14188  174 NKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYS-LPSSLLAPAKHLIASMLSKNPEDRPSLDEIIRH 252
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
79-281 1.17e-25

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: 106.75  E-value: 1.17e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  79 LLSSLKNPYIVHYEDSWIdNDNNACIFTAYYEGGNMaNAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCS 158
Cdd:cd06611   55 ILSECKHPNIVGLYEAYF-YENKLWILIEFCDGGAL-DSIMLELERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAG 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 159 NIFLPKDDHVQLGNYGL-AKLINPEKPVSMVSGISNSMCPEVL-----EDQPYGYKSDIWSLGCCMYEITAHQPAFKAPD 232
Cdd:cd06611  133 NILLTLDGDVKLADFGVsAKNKSTLQKRDTFIGTPYWMAPEVVacetfKDNPYDYKADIWSLGITLIELAQMEPPHHELN 212
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 334185276 233 MAGLINKINRSLMSPL--PIVYSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd06611  213 PMRVLLKILKSEPPTLdqPSKWSSSFNDFLKSCLVKDPDDRPTAAELLKHP 263
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
43-281 1.28e-25

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: 106.74  E-value: 1.28e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  43 KKYAMKKI--CLAKHTDKLKQtaLQEIsravinyDLMKLLSSLKNPYIVHYEDSWIDNdNNACIFTAYYEGGNMANAIKK 120
Cdd:cd14052   27 KVYAVKKLkpNYAGAKDRLRR--LEEV-------SILRELTLDGHDNIVQLIDSWEYH-GHLYIQTELCENGSLDVFLSE 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 121 -ARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLInpekPVSM---VSGISNSMC 196
Cdd:cd14052   97 lGLLGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMATVW----PLIRgieREGDREYIA 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 197 PEVLEDQPYGYKSDIWSLGCCMYEITA---------HQPAFKAPDMA-------GLINKINRSLMSPLP-----IVYSST 255
Cdd:cd14052  173 PEILSEHMYDKPADIFSLGLILLEAAAnvvlpdngdAWQKLRSGDLSdaprlssTDLHSASSPSSNPPPdppnmPILSGS 252
                        250       260
                 ....*....|....*....|....*.
gi 334185276 256 LKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd14052  253 LDRVVRWMLSPEPDRRPTADDVLATP 278
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
65-281 1.62e-25

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: 105.88  E-value: 1.62e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  65 QEISRAVINYDL-MKLLSSLKNPYIVHYEDSWIDNDNNA-CIFTAYYEGGNMANAIKkARGKLfPEERIFKWLAQLLLAV 142
Cdd:cd06653   42 QETSKEVNALECeIQLLKNLRHDRIVQYYGCLRDPEEKKlSIFVEYMPGGSVKDQLK-AYGAL-TENVTRRYTRQILQGV 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 143 NYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLIN----PEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCM 218
Cdd:cd06653  120 SYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRIQticmSGTGIKSVTGTPYWMSPEVISGEGYGRKADVWSVACTV 199
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334185276 219 YEITAHQPAFKAPDMAGLINKINRSLMSP-LPIVYSSTLKQMIKLMLRKKpEYRPTACELLRNP 281
Cdd:cd06653  200 VEMLTEKPPWAEYEAMAAIFKIATQPTKPqLPDGVSDACRDFLRQIFVEE-KRRPTAEFLLRHP 262
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
19-283 1.83e-25

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: 106.14  E-value: 1.83e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  19 YHVVEQVRRGKSSSDFVVLhDIEDKKYAMKKICLAKHTDKLKQTALQEIsravinydlmKLLSSLK-NPYIVHYEDSWID 97
Cdd:cd14131    3 YEILKQLGKGGSSKVYKVL-NPKKKIYALKRVDLEGADEQTLQSYKNEI----------ELLKKLKgSDRIIQLYDYEVT 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  98 NDNNACIFTAYYEGGNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNiFLPKDDHVQLGNYGLAK 177
Cdd:cd14131   72 DEDDYLYMVMECGEIDLATILKKKRPKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPAN-FLLVKGRLKLIDFGIAK 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 178 LINPEKpVSMVS----GISNSMCPEVLEDQPY----------GYKSDIWSLGCCMYEITAHQPAFkaPDMAGLINKINRs 243
Cdd:cd14131  151 AIQNDT-TSIVRdsqvGTLNYMSPEAIKDTSAsgegkpkskiGRPSDVWSLGCILYQMVYGKTPF--QHITNPIAKLQA- 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 334185276 244 LMSP-----LPIVYSSTLKQMIKLMLRKKPEYRPTACELLRNPSL 283
Cdd:cd14131  227 IIDPnheieFPDIPNPDLIDVMKRCLQRDPKKRPSIPELLNHPFL 271
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
19-279 1.87e-25

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: 106.02  E-value: 1.87e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  19 YHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAKHTDKLkqtalQEISRAVinydlmKLLSSLKN---PYIVHYEDSW 95
Cdd:cd06917    3 YRRLELVGRGSYGAVYRGYHVKTGRVVALKVLNLDTDDDDV-----SDIQKEV------ALLSQLKLgqpKNIIKYYGSY 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  96 IdNDNNACIFTAYYEGGNMANAIKKarGKLfPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGL 175
Cdd:cd06917   72 L-KGPSLWIIMDYCEGGSIRTLMRA--GPI-AERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGV 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 176 AKL--INPEKPVSMVsGISNSMCPEV-LEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPLPI-V 251
Cdd:cd06917  148 AASlnQNSSKRSTFV-GTPYWMAPEViTEGKYYDTKADIWSLGITTYEMATGNPPYSDVDALRAVMLIPKSKPPRLEGnG 226
                        250       260
                 ....*....|....*....|....*...
gi 334185276 252 YSSTLKQMIKLMLRKKPEYRPTACELLR 279
Cdd:cd06917  227 YSPLLKEFVAACLDEEPKDRLSADELLK 254
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
19-281 1.98e-25

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


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 106.20  E-value: 1.98e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  19 YHVVEQVRRGKSSSDFVVLHDIEDKKYAMKkiCLAKHTDKLKQ-TALQEISravinydLMKLLSSlkNPYIVHYEDSWID 97
Cdd:cd07831    1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIK--CMKKHFKSLEQvNNLREIQ-------ALRRLSP--HPNILRLIEVLFD 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  98 NDNNACIFTAYYEGGNMANAIKKaRGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLpKDDHVQLGNYGLAK 177
Cdd:cd07831   70 RKTGRLALVFELMDMNLYELIKG-RKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILI-KDDILKLADFGSCR 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 178 LINPEKPVSMVsgISNS--MCPE-VLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPLPIV--- 251
Cdd:cd07831  148 GIYSKPPYTEY--ISTRwyRAPEcLLTDGYYGPKMDIWAVGCVFFEILSLFPLFPGTNELDQIAKIHDVLGTPDAEVlkk 225
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 334185276 252 --------YSSTLKQ-----------------MIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd07831  226 frksrhmnYNFPSKKgtglrkllpnasaegldLLKKLLAYDPDERITAKQALRHP 280
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
60-281 3.83e-25

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: 105.08  E-value: 3.83e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  60 KQTALQEISRAVIN--YDLMKLLSSLKNPYIVHYEDSWIDNDNnACIFTAYYEGGNMANAIKKarGKLFPEERIFKWLAQ 137
Cdd:cd06626   31 KEIRFQDNDPKTIKeiADEMKVLEGLDHPNLVRYYGVEVHREE-VYIFMEYCQEGTLEELLRH--GRILDEAVIRVYTLQ 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 138 LLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINP------EKPVSMVSGISNSMCPEVLEDQP---YGYK 208
Cdd:cd06626  108 LLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAVKLKNntttmaPGEVNSLVGTPAYMAPEVITGNKgegHGRA 187
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334185276 209 SDIWSLGCCMYE-ITAHQPAFKAPDMAGLINKINRSLMSPLP--IVYSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd06626  188 ADIWSLGCVVLEmATGKRPWSELDNEWAIMYHVGMGHKPPIPdsLQLSPEGKDFLSRCLESDPKKRPTASELLDHP 263
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
43-281 4.36e-25

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: 104.86  E-value: 4.36e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  43 KKYAMKKIclAKHTDKLKQTALQEISRAVinydlmKLLSSLKNPYIVHYEDsWIDNDNNACIFTAYYEGGNMANAIKkAR 122
Cdd:cd14098   26 KMRAIKQI--VKRKVAGNDKNLQLFQREI------NILKSLEHPGIVRLID-WYEDDQHIYLVMEYVEGGDLMDFIM-AW 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 123 GKLfPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDD--HVQLGNYGLAKLINPEKPVSMVSGISNSMCPEVL 200
Cdd:cd14098   96 GAI-PEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDpvIVKISDFGLAKVIHTGTFLVTFCGTMAYLAPEIL 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 201 ------EDQPYGYKSDIWSLGCCMYEI-TAHQPaFKAPDMAGLINKINRSLMSPLPIV---YSSTLKQMIKLMLRKKPEY 270
Cdd:cd14098  175 mskeqnLQGGYSNLVDMWSVGCLVYVMlTGALP-FDGSSQLPVEKRIRKGRYTQPPLVdfnISEEAIDFILRLLDVDPEK 253
                        250
                 ....*....|.
gi 334185276 271 RPTACELLRNP 281
Cdd:cd14098  254 RMTAAQALDHP 264
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
46-271 4.49e-25

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: 104.23  E-value: 4.49e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  46 AMKKICLAKHTDKLKQTALQEISravinydlmkLLSSLKNPYIVHYEDSwIDNDNNACIFTAYYEGGNMANAIKKaRGKL 125
Cdd:cd14009   22 AIKEISRKKLNKKLQENLESEIA----------ILKSIKHPNIVRLYDV-QKTEDFIYLVLEYCAGGDLSQYIRK-RGRL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 126 fPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDH---VQLGNYGLAKLINPEkpvSMVSGISNS---MCPEV 199
Cdd:cd14009   90 -PEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDdpvLKIADFGFARSLQPA---SMAETLCGSplyMAPEI 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334185276 200 LEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRS---LMSPLPIVYSSTLKQMIKLMLRKKPEYR 271
Cdd:cd14009  166 LQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIERSdavIPFPIAAQLSPDCKDLLRRLLRRDPAER 240
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
30-283 4.62e-25

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: 104.70  E-value: 4.62e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  30 SSSDFVVLHDIED---KKYAMKKIclakHTDKLKQTALQEISRAVINYDLmklLSSLKNPYIVHYEDSWIDNDNNACIFT 106
Cdd:cd13994    5 ATSVVRIVTKKNPrsgVLYAVKEY----RRRDDESKRKDYVKRLTSEYII---SSKLHHPNIVKVLDLCQDLHGKWCLVM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 107 AYYEGGNMANAIKKARgKLFPEER--IFKwlaQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLA-KLINP-E 182
Cdd:cd13994   78 EYCPGGDLFTLIEKAD-SLSLEEKdcFFK---QILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAeVFGMPaE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 183 KPVSMVSGISNS---MCPEVLEDQPY-GYKSDIWSLGCCMYEI-TAHQPaFKAPDMAGLINKI-----NRSLMSPLPIVY 252
Cdd:cd13994  154 KESPMSAGLCGSepyMAPEVFTSGSYdGRAVDVWSCGIVLFALfTGRFP-WRSAKKSDSAYKAyeksgDFTNGPYEPIEN 232
                        250       260       270
                 ....*....|....*....|....*....|...
gi 334185276 253 S--STLKQMIKLMLRKKPEYRPTACELLRNPSL 283
Cdd:cd13994  233 LlpSECRRLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
27-275 1.22e-24

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


Pssm-ID: 270731 [Multi-domain]  Cd Length: 272  Bit Score: 103.45  E-value: 1.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  27 RGKSSSDFVVLHDIEDKKYAMKKI-CLAKHTDKLKQTALQEisRAVinydlmklLSSLKNPYIVHYEDSwIDNDNNACIF 105
Cdd:cd05579    3 RGAYGRVYLAKKKSTGDLYAIKVIkKRDMIRKNQVDSVLAE--RNI--------LSQAQNPFVVKLYYS-FQGKKNLYLV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 106 TAYYEGGNMANAIKKArGKlFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAK--LINPEK 183
Cdd:cd05579   72 MEYLPGGDLYSLLENV-GA-LDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKvgLVRRQI 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 184 PVSMVSGISNS--------------MCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKI-NRSLMSPL 248
Cdd:cd05579  150 KLSIQKKSNGApekedrrivgtpdyLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNIlNGKIEWPE 229
                        250       260
                 ....*....|....*....|....*..
gi 334185276 249 PIVYSSTLKQMIKLMLRKKPEYRPTAC 275
Cdd:cd05579  230 DPEVSDEAKDLISKLLTPDPEKRLGAK 256
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
82-280 1.31e-24

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: 103.47  E-value: 1.31e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  82 SLKNPYIVHYEDSWIDNDNnACIFTAYYEGGNMANAIKKARGKLFPEERIFkwLAQLLLAVNYLHSNRVVHMDLTCSNIF 161
Cdd:cd14187   63 SLAHQHVVGFHGFFEDNDF-VYVVLELCRRRSLLELHKRRKALTEPEARYY--LRQIILGCQYLHRNRVIHRDLKLGNLF 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 162 LPKDDHVQLGNYGLAKLINPE-KPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKI 240
Cdd:cd14187  140 LNDDMEVKIGDFGLATKVEYDgERKKTLCGTPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRI 219
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 334185276 241 NRSLMSpLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRN 280
Cdd:cd14187  220 KKNEYS-IPKHINPVAASLIQKMLQTDPTARPTINELLND 258
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
77-281 1.89e-24

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: 103.57  E-value: 1.89e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  77 MKLLSSLKNPYIVHYEDSWIdNDNNACIFTAYYEGGNM-ANAIKKARGKLFPEERIFkwLAQLLLAVNYLHSNRVVHMDL 155
Cdd:cd06644   60 IEILATCNHPYIVKLLGAFY-WDGKLWIMIEFCPGGAVdAIMLELDRGLTEPQIQVI--CRQMLEALQYLHSMKIIHRDL 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 156 TCSNIFLPKDDHVQLGNYGL-AKLINPEKPVSMVSGISNSMCPEV-----LEDQPYGYKSDIWSLGCCMYEITAHQPAFK 229
Cdd:cd06644  137 KAGNVLLTLDGDIKLADFGVsAKNVKTLQRRDSFIGTPYWMAPEVvmcetMKDTPYDYKADIWSLGITLIEMAQIEPPHH 216
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 334185276 230 APDMAGLINKINRSLMSPL--PIVYSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd06644  217 ELNPMRVLLKIAKSEPPTLsqPSKWSMEFRDFLKTALDKHPETRPSAAQLLEHP 270
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
42-281 3.47e-24

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: 102.56  E-value: 3.47e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  42 DKKYAMKKICLAKHTDKLKQTALQEISravinydlmkLLSSLKNPYIVHYEDSWIDNDNNACIFTaYYEGgNMANAIKKA 121
Cdd:cd07829   24 GEIVALKKIRLDNEEEGIPSTALREIS----------LLKELKHPNIVKLLDVIHTENKLYLVFE-YCDQ-DLKKYLDKR 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 122 RGKLfPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEkpvsmvsgiSNSMCPEV-- 199
Cdd:cd07829   92 PGPL-PPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLARAFGIP---------LRTYTHEVvt 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 200 ---------LEDQPYGYKSDIWSLGCCMYEITAHQPAFKA----------------------PDMAGLINKiNRSLMSPL 248
Cdd:cd07829  162 lwyrapeilLGSKHYSTAVDIWSVGCIFAELITGKPLFPGdseidqlfkifqilgtpteeswPGVTKLPDY-KPTFPKWP 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 334185276 249 PIVYSSTLK-------QMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd07829  241 KNDLEKVLPrldpegiDLLSKMLQYNPAKRISAKEALKHP 280
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
34-271 4.27e-24

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: 101.56  E-value: 4.27e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  34 FVVLHDIEDKKYAMKKICLAKHtdkLKQTALQEISRAVinydlmKLLSSLKNPYIVHYEDSWIDNDNnacIFTA--YYEG 111
Cdd:cd05578   17 CIVQKKDTKKMFAMKYMNKQKC---IEKDSVRNVLNEL------EILQELEHPFLVNLWYSFQDEED---MYMVvdLLLG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 112 GNMANAIKkaRGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGI 191
Cdd:cd05578   85 GDLRYHLQ--QKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATKLTDGTLATSTSGT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 192 SNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDmAGLINKINRSLMS---PLPIVYSSTLKQMIKLMLRKKP 268
Cdd:cd05578  163 KPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEIHS-RTSIEEIRAKFETasvLYPAGWSEEAIDLINKLLERDP 241

                 ...
gi 334185276 269 EYR 271
Cdd:cd05578  242 QKR 244
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
29-284 5.70e-24

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 105.48  E-value: 5.70e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  29 KSSSDFVVLHDIEDKKYAMKKI-CLAkhtdklkqtalqeisrAVINYDLMKllsslknpyivHYEDswIDNDNNACIFTA 107
Cdd:PTZ00267  95 KVVAKFVMLNDERQAAYARSELhCLA----------------ACDHFGIVK-----------HFDD--FKSDDKLLLIME 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 108 YYEGGNMANAIKKARGKLFP--EERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPV 185
Cdd:PTZ00267 146 YGSGGDLNKQIKQRLKEHLPfqEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQYSDSVSL 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 186 SMVS---GISNSMCPEVLEDQPYGYKSDIWSLGCCMYE-ITAHQPaFKAPDMAGLINKINRSLMSPLPIVYSSTLKQMIK 261
Cdd:PTZ00267 226 DVASsfcGTPYYLAPELWERKRYSKKADMWSLGVILYElLTLHRP-FKGPSQREIMQQVLYGKYDPFPCPVSSGMKALLD 304
                        250       260
                 ....*....|....*....|...
gi 334185276 262 LMLRKKPEYRPTACELLRNPSLQ 284
Cdd:PTZ00267 305 PLLSKNPALRPTTQQLLHTEFLK 327
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
24-279 6.35e-24

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: 101.46  E-value: 6.35e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  24 QVRRGKsssdfvvLHDIEDKKY--AMKKICLaKHTDKLKQTALQEIsravinydlmKLLSSLKNPYIVHY-----EDSWI 96
Cdd:cd00192   10 EVYKGK-------LKGGDGKTVdvAVKTLKE-DASESERKDFLKEA----------RVMKKLGHPNVVRLlgvctEEEPL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  97 dndnnaCIFTAYYEGGNMANAIKKARGKL-------FPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQ 169
Cdd:cd00192   72 ------YLVMEYMEGGDLLDFLRKSRPVFpspepstLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVK 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 170 LGNYGLAKLINPEKpvsmvSGISNS--------MCPEVLEDQPYGYKSDIWSLGCCMYEITAH--QP--AFKAPDMAGLI 237
Cdd:cd00192  146 ISDFGLSRDIYDDD-----YYRKKTggklpirwMAPESLKDGIFTSKSDVWSFGVLLWEIFTLgaTPypGLSNEEVLEYL 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 334185276 238 NKINRslMsPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLR 279
Cdd:cd00192  221 RKGYR--L-PKPENCPDELYELMLSCWQLDPEDRPTFSELVE 259
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
18-281 8.66e-24

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


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 100.98  E-value: 8.66e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  18 NYHVVEQVRRGkSSSDFVVLHDIEDKKYAMKKICLAKHTDKLKQTA----LQEISRAVINYDLMKLLSSLKNPYIVHYED 93
Cdd:cd14077    2 NWEFVKTIGAG-SMGKVKLAKHIRTGEKCAIKIIPRASNAGLKKERekrlEKEISRDIRTIREAALSSLLNHPHICRLRD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  94 SWIDNDNNACIFTaYYEGGNMANAIKkARGKLfPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNY 173
Cdd:cd14077   81 FLRTPNHYYMLFE-YVDGGQLLDYII-SHGKL-KEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 174 GLAKLINPEKPVSMVSGISNSMCPEVLEDQPY-GYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSpLPIVY 252
Cdd:cd14077  158 GLSNLYDPRRLLRTFCGSLYFAAPELLQAQPYtGPEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKIKKGKVE-YPSYL 236
                        250       260
                 ....*....|....*....|....*....
gi 334185276 253 SSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd14077  237 SSECKSLISRMLVVDPKKRATLEQVLNHP 265
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
17-230 9.05e-24

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


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 101.14  E-value: 9.05e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  17 DNYHVVEQVRRGkSSSDFVVLHDIED-KKYAMKkICLAKHTDKLKQTALQEISRAVinydlmklLSSLKNPYIV----HY 91
Cdd:cd05581    1 NDFKFGKPLGEG-SYSTVVLAKEKETgKEYAIK-VLDKRHIIKEKKVKYVTIEKEV--------LSRLAHPGIVklyyTF 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  92 EDSwidndnnACIFTA--YYEGGNMANAIKKArgKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQ 169
Cdd:cd05581   71 QDE-------SKLYFVleYAPNGDLLEYIRKY--GSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIK 141
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185276 170 LGNYGLAKLINPEKPVSMVSGISNS------------------MCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKA 230
Cdd:cd05581  142 ITDFGTAKVLGPDSSPESTKGDADSqiaynqaraasfvgtaeyVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRG 220
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
77-281 1.05e-23

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


Pssm-ID: 270800 [Multi-domain]  Cd Length: 268  Bit Score: 100.97  E-value: 1.05e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  77 MKLLSSLKNPYIVHYEDSwIDNDNNACIFTAYYEGGNMANAIKKARGklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLT 156
Cdd:cd06630   54 IRMMARLNHPNIVRMLGA-TQHKSHFNIFVEWMAGGSVASLLSKYGA--FSENVIINYTLQILRGLAYLHDNQIIHRDLK 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 157 CSNIFL-PKDDHVQLGNYGLAKLINP------EKPVSMVSGISnSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFK 229
Cdd:cd06630  131 GANLLVdSTGQRLRIADFGAAARLASkgtgagEFQGQLLGTIA-FMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWN 209
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 334185276 230 APDMA---GLINKINRSLMSP-LPIVYSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd06630  210 AEKISnhlALIFKIASATTPPpIPEHLSPGLRDVTLRCLELQPEDRPPARELLKHP 265
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
42-281 5.08e-23

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: 98.63  E-value: 5.08e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  42 DKKYAMKKIclakHTDKLKQTALQE-ISRAVinyDLMKLLsslKNPYIVHYEDSwIDNDNNACIFTAYYEGGNMANAIkk 120
Cdd:cd14663   25 GESVAIKII----DKEQVAREGMVEqIKREI---AIMKLL---RHPNIVELHEV-MATKTKIFFVMELVTGGELFSKI-- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 121 ARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSM---VSGISNSMCP 197
Cdd:cd14663   92 AKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSALSEQFRQDGLlhtTCGTPNYVAP 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 198 EVLEDQPY-GYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMsPLPIVYSSTLKQMIKLMLRKKPEYRPTACE 276
Cdd:cd14663  172 EVLARRGYdGAKADIWSCGVILFVLLAGYLPFDDENLMALYRKIMKGEF-EYPRWFSPGAKSLIKRILDPNPSTRITVEQ 250

                 ....*
gi 334185276 277 LLRNP 281
Cdd:cd14663  251 IMASP 255
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
19-281 7.39e-23

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: 98.08  E-value: 7.39e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  19 YHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAKHtdkLKQTALQEIsravinydlmKLLSSLKN----PYIVHYEDS 94
Cdd:cd05118    1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDFR---HPKAALREI----------KLLKHLNDveghPNIVKLLDV 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  95 WIDND-NNACIFTAYYeGGNMANAIKKaRGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFL-PKDDHVQLGN 172
Cdd:cd05118   68 FEHRGgNHLCLVFELM-GMNLYELIKD-YPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILInLELGQLKLAD 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 173 YGLAKLINPEKPVSMVSGISnSMCPEV-LEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPLpiv 251
Cdd:cd05118  146 FGLARSFTSPPYTPYVATRW-YRAPEVlLGAKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIVRLLGTPE--- 221
                        250       260       270
                 ....*....|....*....|....*....|
gi 334185276 252 ysstLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd05118  222 ----ALDLLSKMLKYDPAKRITASQALAHP 247
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
49-279 8.10e-23

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: 98.00  E-value: 8.10e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276    49 KICLAKHTDKLKQTALQEIsravinydlmKLLSSLKNPYIVHYEdSWIDNDNNACIFTAYYEGGNMANAIKKARGKLFPE 128
Cdd:smart00221  34 KTLKEDASEQQIEEFLREA----------RIMRKLDHPNIVKLL-GVCTEEEPLMIVMEYMPGGDLLDYLRKNRPKELSL 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276   129 ERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKpvSMVSGISNS----MCPEVLEDQP 204
Cdd:smart00221 103 SDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDD--YYKVKGGKLpirwMAPESLKEGK 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276   205 YGYKSDIWSLGCCMYEIT--AHQPafkAPDMAG--LINKINRSLMSPLPivySSTLKQMIKLMLR---KKPEYRPTACEL 277
Cdd:smart00221 181 FTSKSDVWSFGVLLWEIFtlGEEP---YPGMSNaeVLEYLKKGYRLPKP---PNCPPELYKLMLQcwaEDPEDRPTFSEL 254

                   ..
gi 334185276   278 LR 279
Cdd:smart00221 255 VE 256
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
19-280 1.03e-22

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: 98.41  E-value: 1.03e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  19 YHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAKHTDKLKQTALQEIsravinydlmKLLSSLKNPYIVHYED---SW 95
Cdd:cd07840    1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRMENEKEGFPITAIREI----------KLLQKLDHPNVVRLKEivtSK 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  96 IDNDNNACIF--TAYYE---GGNMANAIKKargklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQL 170
Cdd:cd07840   71 GSAKYKGSIYmvFEYMDhdlTGLLDNPEVK-----FTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 171 GNYGLAKLINPEKPVSMvsgiSNSMC------PEVL--EDQpYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINR 242
Cdd:cd07840  146 ADFGLARPYTKENNADY----TNRVItlwyrpPELLlgATR-YGPEVDMWSVGCILAELFTGKPIFQGKTELEQLEKIFE 220
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 334185276 243 SLMSPLPIVYS--STLKQMIKLMLRKKPEYR----------PTACELLRN 280
Cdd:cd07840  221 LCGSPTEENWPgvSDLPWFENLKPKKPYKRRlrevfknvidPSALDLLDK 270
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
19-281 1.17e-22

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: 98.12  E-value: 1.17e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  19 YHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAKHTDKLKQTALQEISravinydLMKLLSSLKNPYIVHYED--SWI 96
Cdd:cd07838    1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKVRVPLSEEGIPLSTIREIA-------LLKQLESFEHPNVVRLLDvcHGP 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  97 DNDNNACIFTAY-YEGGNMANAIKKARGKLFPEERIfKWLA-QLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYG 174
Cdd:cd07838   74 RTDRELKLTLVFeHVDQDLATYLDKCPKPGLPPETI-KDLMrQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 175 LAKLINPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKI-------------- 240
Cdd:cd07838  153 LARIYSFEMALTSVVVTLWYRAPEVLLQSSYATPVDMWSVGCIFAELFNRRPLFRGSSEADQLGKIfdviglpseeewpr 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 334185276 241 ----------NRSLMSPLPIVYSSTL--KQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd07838  233 nsalprssfpSYTPRPFKSFVPEIDEegLDLLKKMLTFNPHKRISAFEALQHP 285
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
18-280 1.25e-22

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: 97.56  E-value: 1.25e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  18 NYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLakHTDKLKQTalqeisravinydlMKLLSSLKNPYIVHY------ 91
Cdd:cd14047    7 DFKEIELIGSGGFGQVFKAKHRIDGKTYAIKRVKL--NNEKAERE--------------VKALAKLDHPNIVRYngcwdg 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  92 EDSWIDND--NNA-----CIFTA--YYEGGNMANAIKKARG-KLFPEE--RIFKwlaQLLLAVNYLHSNRVVHMDLTCSN 159
Cdd:cd14047   71 FDYDPETSssNSSrsktkCLFIQmeFCEKGTLESWIEKRNGeKLDKVLalEIFE---QITKGVEYIHSKKLIHRDLKPSN 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 160 IFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEItahqpaFKAPDMAGLINK 239
Cdd:cd14047  148 IFLVDTGKVKIGDFGLVTSLKNDGKRTKSKGTLSYMSPEQISSQDYGKEVDIYALGLILFEL------LHVCDSAFEKSK 221
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 334185276 240 INRSLMS-PLPIVYSSTLK---QMIKLMLRKKPEYRPTACELLRN 280
Cdd:cd14047  222 FWTDLRNgILPDIFDKRYKiekTIIKKMLSKKPEDRPNASEILRT 266
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
45-271 1.48e-22

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: 98.92  E-value: 1.48e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  45 YAMK----KICLAKhtDKLKQTALQEisravinydlmKLLSSLKNPYIVHYEDSWIDNDNnACIFTAYYEGGNMANAIkk 120
Cdd:cd05595   23 YAMKilrkEVIIAK--DEVAHTVTES-----------RVLQNTRHPFLTALKYAFQTHDR-LCFVMEYANGGELFFHL-- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 121 ARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKL-INPEKPVSMVSGISNSMCPEV 199
Cdd:cd05595   87 SRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEgITDGATMKTFCGTPEYLAPEV 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334185276 200 LEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKInrsLMSPL--PIVYSSTLKQMIKLMLRKKPEYR 271
Cdd:cd05595  167 LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELI---LMEEIrfPRTLSPEAKSLLAGLLKKDPKQR 237
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
45-278 2.12e-22

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


Pssm-ID: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 97.44  E-value: 2.12e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  45 YAMKKIclaKHTDKlkQTALQEISRAVInydlmkLLSSLKNPYIVHYEDSWIDnDNNACIFTAYYEGGNMANAIKkaRGK 124
Cdd:cd14046   34 YAIKKI---KLRSE--SKNNSRILREVM------LLSRLNHQHVVRYYQAWIE-RANLYIQMEYCEKSTLRDLID--SGL 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 125 LFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAK-----------LINPEKPVSMVSGISN 193
Cdd:cd14046  100 FQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLATsnklnvelatqDINKSTSAALGSSGDL 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 194 S--------MCPEVLEDQPYGY--KSDIWSLGC-----CMYEITAHQPAFKapdmagLINKINRSLMSPLPIVYSSTLKQ 258
Cdd:cd14046  180 TgnvgtalyVAPEVQSGTKSTYneKVDMYSLGIiffemCYPFSTGMERVQI------LTALRSVSIEFPPDFDDNKHSKQ 253
                        250       260
                 ....*....|....*....|..
gi 334185276 259 --MIKLMLRKKPEYRPTACELL 278
Cdd:cd14046  254 akLIRWLLNHDPAKRPSAQELL 275
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
17-281 4.32e-22

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: 96.72  E-value: 4.32e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  17 DNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKIclakHTDKLKQTALQEISRAVinydlmKLLSSLKNPYIVHYEDSWI 96
Cdd:cd14086    1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKII----NTKKLSARDHQKLEREA------RICRLLKHPNIVRLHDSIS 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  97 DNDNNACIFTaYYEGGNMANAIKkARgKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLP---KDDHVQLGNY 173
Cdd:cd14086   71 EEGFHYLVFD-LVTGGELFEDIV-AR-EFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLAsksKGAAVKLADF 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 174 GLAKLINPEKPVSM-VSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKI---NRSLMSPLP 249
Cdd:cd14086  148 GLAIEVQGDQQAWFgFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIkagAYDYPSPEW 227
                        250       260       270
                 ....*....|....*....|....*....|..
gi 334185276 250 IVYSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd14086  228 DTVTPEAKDLINQMLTVNPAKRITAAEALKHP 259
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
17-286 4.36e-22

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: 96.52  E-value: 4.36e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  17 DNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAKhTDKLKQTALQEISRAVIN-YDLMKLLSSLKNpyIVHYEDSW 95
Cdd:cd14182    3 EKYEPKEILGRGVSSVVRRCIHKPTRQEYAVKIIDITG-GGSFSPEEVQELREATLKeIDILRKVSGHPN--IIQLKDTY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  96 idnDNNACIFTAYyeggnmaNAIKKarGKLF---------PEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDD 166
Cdd:cd14182   80 ---ETNTFFFLVF-------DLMKK--GELFdyltekvtlSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDM 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 167 HVQLGNYGLAKLINPEKPVSMVSGISNSMCPEVLE------DQPYGYKSDIWSLGCCMYEITAHQPAF---KAPDMAGLI 237
Cdd:cd14182  148 NIKLTDFGFSCQLDPGEKLREVCGTPGYLAPEIIEcsmddnHPGYGKEVDMWSTGVIMYTLLAGSPPFwhrKQMLMLRMI 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 334185276 238 NKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRNPSLQPY 286
Cdd:cd14182  228 MSGNYQFGSPEWDDRSDTVKDLISRFLVVQPQKRYTAEEALAHPFFQQY 276
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
48-281 5.31e-22

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: 96.34  E-value: 5.31e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  48 KKICLAKHTDKLKQTALQEisravinydlMKLLSSLKNPYIVHYEDSWIDN-DNNACIFTAYYEGGNMANAIKK--ARGK 124
Cdd:cd06621   31 LKTITTDPNPDVQKQILRE----------LEINKSCASPYIVKYYGAFLDEqDSSIGIAMEYCEGGSLDSIYKKvkKKGG 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 125 LFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLA-KLINpeKPVSMVSGISNSMCPEVLEDQ 203
Cdd:cd06621  101 RIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVSgELVN--SLAGTFTGTSYYMAPERIQGG 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 204 PYGYKSDIWSLGCCMYEITAHQPAFKA--PDMAGLINKINRSLMSPLP---------IVYSSTLKQMIKLMLRKKPEYRP 272
Cdd:cd06621  179 PYSITSDVWSLGLTLLEVAQNRFPFPPegEPPLGPIELLSYIVNMPNPelkdepengIKWSESFKDFIEKCLEKDGTRRP 258

                 ....*....
gi 334185276 273 TACELLRNP 281
Cdd:cd06621  259 GPWQMLAHP 267
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
16-283 5.32e-22

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: 95.59  E-value: 5.32e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  16 LDNYhvveqVRRGKSSSDFVVL-HDIE-DKKYAMKKIclakhtDKLKQtalqeiSRAVINYDLMKLLSSLKNPYIVHYED 93
Cdd:cd06648    9 LDNF-----VKIGEGSTGIVCIaTDKStGRQVAVKKM------DLRKQ------QRRELLFNEVVIMRDYQHPNIVEMYS 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  94 SWIDNDNnACIFTAYYEGGNMANAIKKARgklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNY 173
Cdd:cd06648   72 SYLVGDE-LWVVMEFLEGGALTDIVTHTR---MNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDF 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 174 GLAKLINPEKP--VSMVsGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAF--KAPDMAglINKInRSLMSPL- 248
Cdd:cd06648  148 GFCAQVSKEVPrrKSLV-GTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYfnEPPLQA--MKRI-RDNEPPKl 223
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 334185276 249 --PIVYSSTLKQMIKLMLRKKPEYRPTACELLRNPSL 283
Cdd:cd06648  224 knLHKVSPRLRSFLDRMLVRDPAQRATAAELLNHPFL 260
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
18-280 5.35e-22

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: 96.24  E-value: 5.35e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  18 NYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAKHTDKLKQTALQEIsravinydlmKLLSSLK-NPYIVHYEDswI 96
Cdd:cd07832    1 RYKILGRIGEGAHGIVFKAKDRETGETVALKKVALRKLEGGIPNQALREI----------KALQACQgHPYVVKLRD--V 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  97 DNDNNACIFTAYYEGGNMANAIKKARgKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLA 176
Cdd:cd07832   69 FPHGTGFVLVFEYMLSSLSEVLRDEE-RPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 177 KLINPEKPVSMVSGISNS--MCPEVL-EDQPYGYKSDIWSLGCCMYEITAHQPAFK-APDMAGLiNKINRSLMSP----- 247
Cdd:cd07832  148 RLFSEEDPRLYSHQVATRwyRAPELLyGSRKYDEGVDLWAVGCIFAELLNGSPLFPgENDIEQL-AIVLRTLGTPnektw 226
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 334185276 248 -----LPIVYSSTLKQMIKLMLRKK-PEYRPTACELLRN 280
Cdd:cd07832  227 peltsLPDYNKITFPESKGIRLEEIfPDCSPEAIDLLKG 265
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
103-273 5.47e-22

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: 95.25  E-value: 5.47e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 103 CIFTAYYEGGNMANAIKkaRGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINpE 182
Cdd:cd14059   57 CILMEYCPYGQLYEVLR--AGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKELS-E 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 183 KPVSM-VSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKI-NRSLMSPLPIVYSSTLKQMI 260
Cdd:cd14059  134 KSTKMsFAGTVAWMAPEVIRNEPCSEKVDIWSFGVVLWELLTGEIPYKDVDSSAIIWGVgSNSLQLPVPSTCPDGFKLLM 213
                        170
                 ....*....|...
gi 334185276 261 KLMLRKKPEYRPT 273
Cdd:cd14059  214 KQCWNSKPRNRPS 226
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
77-281 7.99e-22

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: 94.93  E-value: 7.99e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  77 MKLLSSLKNPYIV----HYEDSwidndNNACIFTAYYEGGNMANAIKKaRGKLFPEERIFKWLAQLLLAVNYLHSNRVVH 152
Cdd:cd14186   52 VEIHCQLKHPSILelynYFEDS-----NYVYLVLEMCHNGEMSRYLKN-RKKPFTEDEARHFMHQIVTGMLYLHSHGILH 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 153 MDLTCSNIFLPKDDHVQLGNYGLA-KLINPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFkap 231
Cdd:cd14186  126 RDLTLSNLLLTRNMNIKIADFGLAtQLKMPHEKHFTMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPF--- 202
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 334185276 232 DMAGLINKINRSLMSP--LPIVYSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd14186  203 DTDTVKNTLNKVVLADyeMPAFLSREAQDLIHQLLRKNPADRLSLSSVLDHP 254
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
2-271 8.04e-22

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: 97.07  E-value: 8.04e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276   2 QMEANDCQEEHKfTLDNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMK----KICLAKhtDKLKQTALQEisravinydlm 77
Cdd:cd05593    1 EMDASTTHHKRK-TMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKilkkEVIIAK--DEVAHTLTES----------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  78 KLLSSLKNPYIVHYEDSWIDNDNnACIFTAYYEGGNMANAIkkARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTC 157
Cdd:cd05593   67 RVLKNTRHPFLTSLKYSFQTKDR-LCFVMEYVNGGELFFHL--SRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKL 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 158 SNIFLPKDDHVQLGNYGLAKL-INPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGL 236
Cdd:cd05593  144 ENLMLDKDGHIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKL 223
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 334185276 237 INKInrsLMSPL--PIVYSSTLKQMIKLMLRKKPEYR 271
Cdd:cd05593  224 FELI---LMEDIkfPRTLSADAKSLLSGLLIKDPNKR 257
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
77-280 1.08e-21

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: 95.11  E-value: 1.08e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  77 MKLLSSLKNPYIVHYEDSWIDN-DNNACIFTAYYEGGNMANAIKkARGKLfPEERIFKWLAQLLLAVNYLHSNRVVHMDL 155
Cdd:cd06652   55 IQLLKNLLHERIVQYYGCLRDPqERTLSIFMEYMPGGSIKDQLK-SYGAL-TENVTRKYTRQILEGVHYLHSNMIVHRDI 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 156 TCSNIFLPKDDHVQLGNYGLAKLIN----PEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAP 231
Cdd:cd06652  133 KGANILRDSVGNVKLGDFGASKRLQticlSGTGMKSVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPWAEF 212
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 334185276 232 DMAGLINKINRSLMSP-LPIVYSSTLKQMIKLMLrKKPEYRPTACELLRN 280
Cdd:cd06652  213 EAMAAIFKIATQPTNPqLPAHVSDHCRDFLKRIF-VEAKLRPSADELLRH 261
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
49-279 1.12e-21

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 94.52  E-value: 1.12e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276    49 KICLAKHTDKLKQTALQEIsravinydlmKLLSSLKNPYIVHYEdSWIDNDNNACIFTAYYEGGNMANAIKKARGKLFPE 128
Cdd:smart00219  34 KTLKEDASEQQIEEFLREA----------RIMRKLDHPNVVKLL-GVCTEEEPLYIVMEYMEGGDLLSYLRKNRPKLSLS 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276   129 ERIfKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNS--MCPEVLEDQPYG 206
Cdd:smart00219 103 DLL-SFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDYYRKRGGKLPIrwMAPESLKEGKFT 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276   207 YKSDIWSLGCCMYEIT--AHQPafkAPDMAG--LINKINRSLMSPLPivySSTLKQMIKLMLR---KKPEYRPTACELLR 279
Cdd:smart00219 182 SKSDVWSFGVLLWEIFtlGEQP---YPGMSNeeVLEYLKNGYRLPQP---PNCPPELYDLMLQcwaEDPEDRPTFSELVE 255
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
18-281 1.16e-21

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: 94.70  E-value: 1.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  18 NYHVVEQVRrgksssdfvvlHDIEDKKYAMKKIclAKHTDKLKQTALQ-EISravinydlmkLLSSLKNPYIVHYEDSWi 96
Cdd:cd14095   12 NFAVVKECR-----------DKATDKEYALKII--DKAKCKGKEHMIEnEVA----------ILRRVKHPNIVQLIEEY- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  97 DNDNNACIFTAYYEGGNMANAIKKARGklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDD----HVQLGN 172
Cdd:cd14095   68 DTDTELYLVMELVKGGDLFDAITSSTK--FTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHEdgskSLKLAD 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 173 YGLAKLInpEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPD--MAGLINKINR---SLMSP 247
Cdd:cd14095  146 FGLATEV--KEPLFTVCGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRSPDrdQEELFDLILAgefEFLSP 223
                        250       260       270
                 ....*....|....*....|....*....|....
gi 334185276 248 LPIVYSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd14095  224 YWDNISDSAKDLISRMLVVDPEKRYSAGQVLDHP 257
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
58-281 1.68e-21

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


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 94.21  E-value: 1.68e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  58 KLKQTALQEISRAvinYDLMKLLSSLKNPYIVHYEDSWIDNDNNACIF-TAYYEGGNMANAIKKARgklFPEERIFK-WL 135
Cdd:cd13983   35 KLRKLPKAERQRF---KQEIEILKSLKHPNIIKFYDSWESKSKKEVIFiTELMTSGTLKQYLKRFK---RLKLKVIKsWC 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 136 AQLLLAVNYLHSNR--VVHMDLTCSNIFLP-KDDHVQLGNYGLAKLINPEKPVSmVSGISNSMCPEVLEDQpYGYKSDIW 212
Cdd:cd13983  109 RQILEGLNYLHTRDppIIHRDLKCDNIFINgNTGEVKIGDLGLATLLRQSFAKS-VIGTPEFMAPEMYEEH-YDEKVDIY 186
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334185276 213 SLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSP--LPIVYSSTLKQMIKLMLRKKPEyRPTACELLRNP 281
Cdd:cd13983  187 AFGMCLLEMATGEYPYSECTNAAQIYKKVTSGIKPesLSKVKDPELKDFIEKCLKPPDE-RPSARELLEHP 256
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
19-284 2.49e-21

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


Pssm-ID: 270814 [Multi-domain]  Cd Length: 261  Bit Score: 93.84  E-value: 2.49e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  19 YHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAKHTDKlkqtalqeisRAVINYDLmkLLSSLKNPYIVHYEDSWIDN 98
Cdd:cd06647    9 YTRFEKIGQGASGTVYTAIDVATGQEVAIKQMNLQQQPKK----------ELIINEIL--VMRENKNPNIVNYLDSYLVG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  99 DNnACIFTAYYEGGNMANAIKKArgkLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKL 178
Cdd:cd06647   77 DE-LWVVMEYLAGGSLTDVVTET---CMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQ 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 179 INPE--KPVSMVsGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAF--KAPDMAGLINKINRSLMSPLPIVYSS 254
Cdd:cd06647  153 ITPEqsKRSTMV-GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYlnENPLRALYLIATNGTPELQNPEKLSA 231
                        250       260       270
                 ....*....|....*....|....*....|
gi 334185276 255 TLKQMIKLMLRKKPEYRPTACELLRNPSLQ 284
Cdd:cd06647  232 IFRDFLNRCLEMDVEKRGSAKELLQHPFLK 261
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
77-281 3.87e-21

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: 93.94  E-value: 3.87e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  77 MKLLSSLKNPYIVHYEDSWIdNDNNACIFTAYYEGGNMaNAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLT 156
Cdd:cd06643   53 IDILASCDHPNIVKLLDAFY-YENNLWILIEFCAGGAV-DAVMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLK 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 157 CSNIFLPKDDHVQLGNYGL-AKLINPEKPVSMVSGISNSMCPEVL-----EDQPYGYKSDIWSLGCCMYEITAHQPAFKA 230
Cdd:cd06643  131 AGNILFTLDGDIKLADFGVsAKNTRTLQRRDSFIGTPYWMAPEVVmcetsKDRPYDYKADVWSLGVTLIEMAQIEPPHHE 210
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 334185276 231 PDMAGLINKINRSLMSPL--PIVYSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd06643  211 LNPMRVLLKIAKSEPPTLaqPSRWSPEFKDFLRKCLEKNVDARWTTSQLLQHP 263
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
50-284 4.24e-21

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: 93.95  E-value: 4.24e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  50 ICLA--KHTDK---LKQTALQEISRAVINYDLMKLLSSLKNPYIVHYEDSWIDNDNnACIFTAYYEGGNMANAIKKARgk 124
Cdd:cd06658   38 VCIAteKHTGKqvaVKKMDLRKQQRRELLFNEVVIMRDYHHENVVDMYNSYLVGDE-LWVVMEFLEGGALTDIVTHTR-- 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 125 lFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPV-SMVSGISNSMCPEVLEDQ 203
Cdd:cd06658  115 -MNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQVSKEVPKrKSLVGTPYWMAPEVISRL 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 204 PYGYKSDIWSLGCCMYE-ITAHQPAFKAPDMAGLiNKINRSLMSPLPIVY--SSTLKQMIKLMLRKKPEYRPTACELLRN 280
Cdd:cd06658  194 PYGTEVDIWSLGIMVIEmIDGEPPYFNEPPLQAM-RRIRDNLPPRVKDSHkvSSVLRGFLDLMLVREPSQRATAQELLQH 272

                 ....
gi 334185276 281 PSLQ 284
Cdd:cd06658  273 PFLK 276
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
42-281 4.37e-21

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: 92.76  E-value: 4.37e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  42 DKKYAMKKICLAKHTDKLKQTALQEIsravinYDLMKLLSslkNPYIVHYEDSWIDNDNnACIFTAYYEGGNMANAIKKA 121
Cdd:cd14050   26 GKLYAVKRSRSRFRGEKDRKRKLEEV------ERHEKLGE---HPNCVRFIKAWEEKGI-LYIQTELCDTSLQQYCEETH 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 122 RgklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNSMCPEVLe 201
Cdd:cd14050   96 S---LPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLVVELDKEDIHDAQEGDPRYMAPELL- 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 202 DQPYGYKSDIWSLGCCMYEITA--HQPAFkAPDMAGLinkinRSLMSPLPIV--YSSTLKQMIKLMLRKKPEYRPTACEL 277
Cdd:cd14050  172 QGSFTKAADIFSLGITILELACnlELPSG-GDGWHQL-----RQGYLPEEFTagLSPELRSIIKLMMDPDPERRPTAEDL 245

                 ....
gi 334185276 278 LRNP 281
Cdd:cd14050  246 LALP 249
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
77-284 4.47e-21

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: 93.22  E-value: 4.47e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  77 MKLLSSLKNPYIVHYEDSWIDN-DNNACIFTAYYEGGNMANAIKkARGKLfPEERIFKWLAQLLLAVNYLHSNRVVHMDL 155
Cdd:cd06651   60 IQLLKNLQHERIVQYYGCLRDRaEKTLTIFMEYMPGGSVKDQLK-AYGAL-TESVTRKYTRQILEGMSYLHSNMIVHRDI 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 156 TCSNIFLPKDDHVQLGNYGLAKLIN----PEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAP 231
Cdd:cd06651  138 KGANILRDSAGNVKLGDFGASKRLQticmSGTGIRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEY 217
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 334185276 232 D-MAGLINKINRSLMSPLPIVYSSTLKQMIKLMLrKKPEYRPTACELLRNPSLQ 284
Cdd:cd06651  218 EaMAAIFKIATQPTNPQLPSHISEHARDFLGCIF-VEARHRPSAEELLRHPFAQ 270
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
77-283 4.68e-21

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: 92.98  E-value: 4.68e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  77 MKLLSSLKNPYIVHYEDSWIDnDNNACIFTAYYEGGNMAnAIKKARGKlFPEERIFKWLAQLLLAVNYLHSNRVVHMDLT 156
Cdd:cd06628   57 IALLRELQHENIVQYLGSSSD-ANHLNIFLEYVPGGSVA-TLLNNYGA-FEESLVRNFVRQILKGLNYLHNRGIIHRDIK 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 157 CSNIFLPKDDHVQLGNYGLAKLI---------NPEKPvsMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPA 227
Cdd:cd06628  134 GANILVDNKGGIKISDFGISKKLeanslstknNGARP--SLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHP 211
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 334185276 228 FkaPDMAGL--INKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRNPSL 283
Cdd:cd06628  212 F--PDCTQMqaIFKIGENASPTIPSNISSEARDFLEKTFEIDHNKRPTADELLKHPFL 267
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
28-281 6.87e-21

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: 92.32  E-value: 6.87e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  28 GKSSSDFVVL--HDIEDKKYAMKKICLAKhtdKLKQTALQEISRAVInydLMKLLsslKNPYIVHYEDSWiDNDNNACIF 105
Cdd:cd14081   10 GKGQTGLVKLakHCVTGQKVAIKIVNKEK---LSKESVLMKVEREIA---IMKLI---EHPNVLKLYDVY-ENKKYLYLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 106 TAYYEGGNMANAIKKaRGKLFPEE--RIFKwlaQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEK 183
Cdd:cd14081   80 LEYVSGGELFDYLVK-KGRLTEKEarKFFR---QIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMASLQPEGS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 184 PVSMVSGISNSMCPEVLEDQPY-GYKSDIWSLGCCMYE-ITAHQPaFKAPDMAGLINKINRSLMSpLPIVYSSTLKQMIK 261
Cdd:cd14081  156 LLETSCGSPHYACPEVIKGEKYdGRKADIWSCGVILYAlLVGALP-FDDDNLRQLLEKVKRGVFH-IPHFISPDAQDLLR 233
                        250       260
                 ....*....|....*....|
gi 334185276 262 LMLRKKPEYRPTACELLRNP 281
Cdd:cd14081  234 RMLEVNPEKRITIEEIKKHP 253
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
17-271 9.12e-21

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: 93.46  E-value: 9.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  17 DNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMK---KICLAKHtDKLKQ-TALQEIsravinydlmklLSSLKNPYIVHYE 92
Cdd:cd05574    1 DHFKKIKLLGKGDVGRVYLVRLKGTGKLFAMKvldKEEMIKR-NKVKRvLTEREI------------LATLDHPFLPTLY 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  93 DSwIDNDNNACIFTAYYEGGNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGN 172
Cdd:cd05574   68 AS-FQTSTHLCFVMDYCPGGELFRLLQKQPGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 173 YGLAKLINPEKPVSMVSGI-----------------------SNS-------MCPEVLEDQPYGYKSDIWSLGCCMYEI- 221
Cdd:cd05574  147 FDLSKQSSVTPPPVRKSLRkgsrrssvksieketfvaepsarSNSfvgteeyIAPEVIKGDGHGSAVDWWTLGILLYEMl 226
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 334185276 222 TAHQPaFKAPDM-AGLINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYR 271
Cdd:cd05574  227 YGTTP-FKGSNRdETFSNILKKELTFPESPPVSSEAKDLIRKLLVKDPSKR 276
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
2-271 1.14e-20

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: 93.94  E-value: 1.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276   2 QMEANDCQEEHKFTLDNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMK----KICLAKhtDKLKQTALQEisravinydlm 77
Cdd:cd05594   10 EMEVSLTKPKHKVTMNDFEYLKLLGKGTFGKVILVKEKATGRYYAMKilkkEVIVAK--DEVAHTLTEN----------- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  78 KLLSSLKNPYIVHYEDSWIDNDNnACIFTAYYEGGNMANAIkkARGKLFPEERIFKWLAQLLLAVNYLHSNR-VVHMDLT 156
Cdd:cd05594   77 RVLQNSRHPFLTALKYSFQTHDR-LCFVMEYANGGELFFHL--SRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 157 CSNIFLPKDDHVQLGNYGLAKL-INPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAG 235
Cdd:cd05594  154 LENLMLDKDGHIKITDFGLCKEgIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEK 233
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 334185276 236 LINKInrsLMSPL--PIVYSSTLKQMIKLMLRKKPEYR 271
Cdd:cd05594  234 LFELI---LMEEIrfPRTLSPEAKSLLSGLLKKDPKQR 268
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
17-240 1.27e-20

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: 93.50  E-value: 1.27e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  17 DNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKIclaKHTDKLK--QTALQEISRavinyDLMkllSSLKNPYIVHYEDS 94
Cdd:cd05573    1 DDFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKIL---RKSDMLKreQIAHVRAER-----DIL---ADADSPWIVRLHYA 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  95 WIDNDNnACIFTAYYEGGNMANA-IKKARgklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNY 173
Cdd:cd05573   70 FQDEDH-LYLVMEYMPGGDLMNLlIKYDV---FPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADF 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 174 GLAKLINPEKPVSMVS------------------------------GISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITA 223
Cdd:cd05573  146 GLCTKMNKSGDRESYLndsvntlfqdnvlarrrphkqrrvraysavGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLY 225
                        250
                 ....*....|....*..
gi 334185276 224 HQPAFKAPDMAGLINKI 240
Cdd:cd05573  226 GFPPFYSDSLVETYSKI 242
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
19-284 1.44e-20

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: 92.48  E-value: 1.44e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  19 YHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKIclakhtdKLKQTALQEIsraVINYDLmkLLSSLKNPYIVHYEDSWIDN 98
Cdd:cd06656   21 YTRFEKIGQGASGTVYTAIDIATGQEVAIKQM-------NLQQQPKKEL---IINEIL--VMRENKNPNIVNYLDSYLVG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  99 DNnACIFTAYYEGGNMANAIKKArgkLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKL 178
Cdd:cd06656   89 DE-LWVVMEYLAGGSLTDVVTET---CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQ 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 179 INPEKPV-SMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAF--KAPDMAGLINKINRSLMSPLPIVYSST 255
Cdd:cd06656  165 ITPEQSKrSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYlnENPLRALYLIATNGTPELQNPERLSAV 244
                        250       260
                 ....*....|....*....|....*....
gi 334185276 256 LKQMIKLMLRKKPEYRPTACELLRNPSLQ 284
Cdd:cd06656  245 FRDFLNRCLEMDVDRRGSAKELLQHPFLK 273
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
49-279 1.82e-20

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


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 91.02  E-value: 1.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276   49 KICLAKHTDKLKQTALQEISravinydlmkLLSSLKNPYIVHYEdSWIDNDNNACIFTAYYEGGNMANAIKKARGKLfPE 128
Cdd:pfam07714  34 KTLKEGADEEEREDFLEEAS----------IMKKLDHPNIVKLL-GVCTQGEPLYIVTEYMPGGDLLDFLRKHKRKL-TL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  129 ERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLI-NPEKPVSMVSGISNS--MCPEVLEDQPY 205
Cdd:pfam07714 102 KDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDIyDDDYYRKRGGGKLPIkwMAPESLKDGKF 181
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334185276  206 GYKSDIWSLGCCMYEITAH----QPAFKAPDMAGLINKINRslmSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLR 279
Cdd:pfam07714 182 TSKSDVWSFGVLLWEIFTLgeqpYPGMSNEEVLEFLEDGYR---LPQPENCPDELYDLMKQCWAYDPEDRPTFSELVE 256
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
77-286 1.84e-20

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: 91.66  E-value: 1.84e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  77 MKLLSSLKNPYIVHYEDSWIDNdNNACIFTAYYEGGNMANAIKKARgklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLT 156
Cdd:cd06642   53 ITVLSQCDSPYITRYYGSYLKG-TKLWIIMEYLGGGSALDLLKPGP---LEETYIATILREILKGLDYLHSERKIHRDIK 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 157 CSNIFLPKDDHVQLGNYGLA-KLINPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAG 235
Cdd:cd06642  129 AANVLLSEQGDVKLADFGVAgQLTDTQIKRNTFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDLHPMR 208
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 334185276 236 LINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRNPSLQPY 286
Cdd:cd06642  209 VLFLIPKNSPPTLEGQHSKPFKEFVEACLNKDPRFRPTAKELLKHKFITRY 259
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
19-280 2.63e-20

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: 91.29  E-value: 2.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  19 YHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAKHTDKLKQTAlQEISravinydlmkLLSSLKNPYIVHYEDSWIdN 98
Cdd:cd06641    6 FTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAEDEIEDIQ-QEIT----------VLSQCDSPYVTKYYGSYL-K 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  99 DNNACIFTAYYEGGNMANAIKKARgklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLA-K 177
Cdd:cd06641   74 DTKLWIIMEYLGGGSALDLLEPGP---LDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAgQ 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 178 LINPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPLPIVYSSTLK 257
Cdd:cd06641  151 LTDTQIKRN*FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIPKNNPPTLEGNYSKPLK 230
                        250       260
                 ....*....|....*....|...
gi 334185276 258 QMIKLMLRKKPEYRPTACELLRN 280
Cdd:cd06641  231 EFVEACLNKEPSFRPTAKELLKH 253
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
44-283 3.84e-20

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: 90.37  E-value: 3.84e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  44 KYAMKKICLAKHTDK------LKQTALQEISRAVINYDLMKLLSSLKNPYIVHYEDSWiDNDNNACIFTAYYEGGNMANA 117
Cdd:cd14198   20 KFAVVRQCISKSTGQeyaakfLKKRRRGQDCRAEILHEIAVLELAKSNPRVVNLHEVY-ETTSEIILILEYAAGGEIFNL 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 118 IKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFL----PKDDhVQLGNYGLAKLINPEKPVSMVSGISN 193
Cdd:cd14198   99 CVPDLAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLssiyPLGD-IKIVDFGMSRKIGHACELREIMGTPE 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 194 SMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGL---INKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEY 270
Cdd:cd14198  178 YLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDNQETflnISQVNVDYSEETFSSVSQLATDFIQKLLVKNPEK 257
                        250
                 ....*....|...
gi 334185276 271 RPTACELLRNPSL 283
Cdd:cd14198  258 RPTAEICLSHSWL 270
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
108-271 3.86e-20

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: 91.51  E-value: 3.86e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 108 YYEGGNMANAIKKARgkLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKL-INPEKPVS 186
Cdd:cd05570   77 YVNGGDLMFHIQRAR--RFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCKEgIWGGNTTS 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 187 MVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKInrsLMSPL--PIVYSSTLKQMIKLML 264
Cdd:cd05570  155 TFCGTPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAI---LNDEVlyPRWLSREAVSILKGLL 231

                 ....*..
gi 334185276 265 RKKPEYR 271
Cdd:cd05570  232 TKDPARR 238
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
19-284 6.45e-20

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: 90.55  E-value: 6.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  19 YHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAKHTDKlkqtalqeisRAVINYDLmkLLSSLKNPYIVHYEDSWIDN 98
Cdd:cd06655   21 YTRYEKIGQGASGTVFTAIDVATGQEVAIKQINLQKQPKK----------ELIINEIL--VMKELKNPNIVNFLDSFLVG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  99 DNnACIFTAYYEGGNMANAIKKArgkLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKL 178
Cdd:cd06655   89 DE-LFVVMEYLAGGSLTDVVTET---CMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQ 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 179 INPEKPV-SMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAF--KAPDMAGLINKINRSLMSPLPIVYSST 255
Cdd:cd06655  165 ITPEQSKrSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYlnENPLRALYLIATNGTPELQNPEKLSPI 244
                        250       260
                 ....*....|....*....|....*....
gi 334185276 256 LKQMIKLMLRKKPEYRPTACELLRNPSLQ 284
Cdd:cd06655  245 FRDFLNRCLEMDVEKRGSAKELLQHPFLK 273
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
78-281 7.18e-20

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: 89.90  E-value: 7.18e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  78 KLLSSLK-NPYIVHYEDSWIDNDnnaCIFTAY-YEGGNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDL 155
Cdd:cd07830   49 KSLRKLNeHPNIVKLKEVFREND---ELYFVFeYMEGNLYQLMKDRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDL 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 156 TCSNIFLPKDDHVQLGNYGLAKLINPEKP----VSmvsgisnsmcPEVLEDQPYgYKS--DIWSLGCCMYEITAHQPAFK 229
Cdd:cd07830  126 KPENLLVSGPEVVKIADFGLAREIRSRPPytdyVStrw----yraPEILLRSTS-YSSpvDIWALGCIMAELYTLRPLFP 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 230 A----------------------PDMAGLINKINRSL--MSPLPIVY-----SSTLKQMIKLMLRKKPEYRPTACELLRN 280
Cdd:cd07830  201 GsseidqlykicsvlgtptkqdwPEGYKLASKLGFRFpqFAPTSLHQlipnaSPEAIDLIKDMLRWDPKKRPTASQALQH 280

                 .
gi 334185276 281 P 281
Cdd:cd07830  281 P 281
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
49-273 7.49e-20

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: 89.37  E-value: 7.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  49 KICLAKHTDKLKQTALQEISRAVINYDL--------MKLLSSLKNPYIVH-YEdsWIDNDNNACIFTAYYEGGNMANAIK 119
Cdd:cd14073   16 KVKLAIERATGREVAIKSIKKDKIEDEQdmvrirreIEIMSSLNHPHIIRiYE--VFENKDKIVIVMEYASGGELYDYIS 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 120 KaRGKLFPEE--RIFKwlaQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNSMCP 197
Cdd:cd14073   94 E-RRRLPEREarRIFR---QIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSNLYSKDKLLQTFCGSPLYASP 169
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334185276 198 EVLEDQPY-GYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINR-SLMSPLPivySSTLKQMIKLMLRKKPEYRPT 273
Cdd:cd14073  170 EIVNGTPYqGPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISSgDYREPTQ---PSDASGLIRWMLTVNPKRRAT 244
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
40-281 7.96e-20

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: 89.24  E-value: 7.96e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  40 IEDKKYAMKKIClaKHTDKLKQTALQEISRAVI--NYDLMK----LLSSLKNPYIVHYEDSWiDNDNNACIFTAYYEGGN 113
Cdd:cd14185    8 IGDGNFAVVKEC--RHWNENQEYAMKIIDKSKLkgKEDMIEseilIIKSLSHPNIVKLFEVY-ETEKEIYLILEYVRGGD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 114 MANAIKKARGklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLP----KDDHVQLGNYGLAKLINpeKPVSMVS 189
Cdd:cd14185   85 LFDAIIESVK--FTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQhnpdKSTTLKLADFGLAKYVT--GPIFTVC 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 190 GISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAP--DMAGLINKINRSLMSPLPIVY---SSTLKQMIKLML 264
Cdd:cd14185  161 GTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRSPerDQEELFQIIQLGHYEFLPPYWdniSEAAKDLISRLL 240
                        250
                 ....*....|....*..
gi 334185276 265 RKKPEYRPTACELLRNP 281
Cdd:cd14185  241 VVDPEKRYTAKQVLQHP 257
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
50-290 8.30e-20

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: 90.04  E-value: 8.30e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  50 ICLAKHTDKLKQTA-----LQEISRAVINYDLMKLLSSLKNPYIVHYEDSWIDNDNnACIFTAYYEGGNMANAIKKARgk 124
Cdd:cd06659   37 VCIAREKHSGRQVAvkmmdLRKQQRRELLFNEVVIMRDYQHPNVVEMYKSYLVGEE-LWVLMEYLQGGALTDIVSQTR-- 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 125 lFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPV--SMVsGISNSMCPEVLED 202
Cdd:cd06659  114 -LNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFCAQISKDVPKrkSLV-GTPYWMAPEVISR 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 203 QPYGYKSDIWSLGCCMYEITAHQPAF--KAPdmaglINKINRSLMSPLPIV-----YSSTLKQMIKLMLRKKPEYRPTAC 275
Cdd:cd06659  192 CPYGTEVDIWSLGIMVIEMVDGEPPYfsDSP-----VQAMKRLRDSPPPKLknshkASPVLRDFLERMLVRDPQERATAQ 266
                        250
                 ....*....|....*
gi 334185276 276 ELLRNpslqPYLLQC 290
Cdd:cd06659  267 ELLDH----PFLLQT 277
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
16-278 1.06e-19

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 93.65  E-value: 1.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276   16 LDNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAKhtdkLKQtalQEISRAVINYDLMKllsSLKNPYIVHYEDSW 95
Cdd:PTZ00266   12 LNEYEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISYRG----LKE---REKSQLVIEVNVMR---ELKHKNIVRYIDRF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276   96 IDNDNNAC-IFTAYYEGGNMANAIKKARgKLF---PEERIFKWLAQLLLAVNYLHS-------NRVVHMDLTCSNIFLPK 164
Cdd:PTZ00266   82 LNKANQKLyILMEFCDAGDLSRNIQKCY-KMFgkiEEHAIVDITRQLLHALAYCHNlkdgpngERVLHRDLKPQNIFLST 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  165 D-DHV----------------QLGNYGLAKLINPEKPVSMVSGISNSMCPEVL--EDQPYGYKSDIWSLGCCMYEI-TAH 224
Cdd:PTZ00266  161 GiRHIgkitaqannlngrpiaKIGDFGLSKNIGIESMAHSCVGTPYYWSPELLlhETKSYDDKSDMWALGCIIYELcSGK 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 334185276  225 QPAFKAPDMAGLINKINRSlmSPLPIV-YSSTLKQMIKLMLRKKPEYRPTACELL 278
Cdd:PTZ00266  241 TPFHKANNFSQLISELKRG--PDLPIKgKSKELNILIKNLLNLSAKERPSALQCL 293
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
22-280 1.10e-19

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: 89.34  E-value: 1.10e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  22 VEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAKHTDKLKQTAlQEISravinydlmkLLSSLKNPYIVHYEDSWIDNdNN 101
Cdd:cd06640    9 LERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEEAEDEIEDIQ-QEIT----------VLSQCDSPYVTKYYGSYLKG-TK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 102 ACIFTAYYEGGNmanAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLA-KLIN 180
Cdd:cd06640   77 LWIIMEYLGGGS---ALDLLRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAgQLTD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 181 PEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPLPIVYSSTLKQMI 260
Cdd:cd06640  154 TQIKRNTFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPPNSDMHPMRVLFLIPKNNPPTLVGDFSKPFKEFI 233
                        250       260
                 ....*....|....*....|
gi 334185276 261 KLMLRKKPEYRPTACELLRN 280
Cdd:cd06640  234 DACLNKDPSFRPTAKELLKH 253
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
17-281 1.51e-19

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: 88.95  E-value: 1.51e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  17 DNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAkhTDKLKQTALQEISRAVIN-YDLMKLLSslKNPYIVHYEDSW 95
Cdd:cd14093    3 AKYEPKEILGRGVSSTVRRCIEKETGQEFAVKIIDIT--GEKSSENEAEELREATRReIEILRQVS--GHPNIIELHDVF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  96 idnDNNACIFTAYyeggNMANaikkaRGKLF---------PEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDD 166
Cdd:cd14093   79 ---ESPTFIFLVF----ELCR-----KGELFdyltevvtlSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 167 HVQLGNYGLAKLINPEKPVSMVSGISNSMCPEVL-----EDQP-YGYKSDIWSLGCCMYEITAHQPAF---KAPDMAGLI 237
Cdd:cd14093  147 NVKISDFGFATRLDEGEKLRELCGTPGYLAPEVLkcsmyDNAPgYGKEVDMWACGVIMYTLLAGCPPFwhrKQMVMLRNI 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 334185276 238 NKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd14093  227 MEGKYEFGSPEWDDISDTAKDLISKLLVVDPKKRLTAEEALEHP 270
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
43-271 1.60e-19

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: 88.74  E-value: 1.60e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  43 KKYAMKkiCLAKHTDKLKQ---TALQEisravinydlMKLLSSLKNPYIVHYEDSWiDNDNNACIFTAYYEGGNMANAIK 119
Cdd:cd05577   19 KMYACK--KLDKKRIKKKKgetMALNE----------KIILEKVSSPFIVSLAYAF-ETKDKLCLVLTLMNGGDLKYHIY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 120 KARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNSMCPEV 199
Cdd:cd05577   86 NVGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVEFKGGKKIKGRVGTHGYMAPEV 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334185276 200 L-EDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMS---PLPIVYSSTLKQMIKLMLRKKPEYR 271
Cdd:cd05577  166 LqKEVAYDFSVDWFALGCMLYEMIAGRSPFRQRKEKVDKEELKRRTLEmavEYPDSFSPEARSLCEGLLQKDPERR 241
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
108-240 1.75e-19

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: 89.47  E-value: 1.75e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 108 YYEGGNMANAIKKARGklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKL-INPEKPVS 186
Cdd:cd05591   77 YVNGGDLMFQIQRARK--FDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgILNGKTTT 154
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 334185276 187 MVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKI 240
Cdd:cd05591  155 TFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESI 208
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
43-283 1.91e-19

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: 88.60  E-value: 1.91e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  43 KKYAMKKIclAKHTDKLKQTALQEISRAVINYdlMKLLSSLKNPYIVHYEDsWIDNDNNACIFTAYYEGGNMANAIKKAr 122
Cdd:cd14084   32 KKVAIKII--NKRKFTIGSRREINKPRNIETE--IEILKKLSHPCIIKIED-FFDAEDDYYIVLELMEGGELFDRVVSN- 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 123 gKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDH---VQLGNYGLAKLINPEKPVSMVSGISNSMCPEV 199
Cdd:cd14084  106 -KRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEeclIKITDFGLSKILGETSLMKTLCGTPTYLAPEV 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 200 LE---DQPYGYKSDIWSLGCCMYEITAHQPAF--KAPDMAgLINKINRSLMSPLPIVY---SSTLKQMIKLMLRKKPEYR 271
Cdd:cd14084  185 LRsfgTEGYTRAVDCWSLGVILFICLSGYPPFseEYTQMS-LKEQILSGKYTFIPKAWknvSEEAKDLVKKMLVVDPSRR 263
                        250
                 ....*....|..
gi 334185276 272 PTACELLRNPSL 283
Cdd:cd14084  264 PSIEEALEHPWL 275
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
17-281 2.11e-19

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: 88.16  E-value: 2.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  17 DNYHVVEQVRRGKSSSdfVVLHDIEDKKYAMKKICLAKHTDKLKQTALQ-EISravinydlmkLLSSLKNPYIVHYEDSW 95
Cdd:cd14167    3 DIYDFREVLGTGAFSE--VVLAEEKRTQKLVAIKCIAKKALEGKETSIEnEIA----------VLHKIKHPNIVALDDIY 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  96 iDNDNNACIFTAYYEGGNMANAIKKaRGkLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIF---LPKDDHVQLGN 172
Cdd:cd14167   71 -ESGGHLYLIMQLVSGGELFDRIVE-KG-FYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISD 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 173 YGLAKLINPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRS---LMSPLP 249
Cdd:cd14167  148 FGLSKIEGSGSVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAeyeFDSPYW 227
                        250       260       270
                 ....*....|....*....|....*....|..
gi 334185276 250 IVYSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd14167  228 DDISDSAKDFIQHLMEKDPEKRFTCEQALQHP 259
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
97-232 2.52e-19

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: 87.92  E-value: 2.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  97 DNDNNACIFTAYYEGGNMANAIKKARGklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLA 176
Cdd:cd05611   67 QSKDYLYLVMEYLNGGDCASLIKTLGG--LPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLS 144
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 177 K--LINPEKPvsMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKA--PD 232
Cdd:cd05611  145 RngLEKRHNK--KFVGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAetPD 202
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
19-301 2.60e-19

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: 88.46  E-value: 2.60e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  19 YHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKIclakhtDKLKQTALQEISravInydlmkLLSSLKNPYIVHYEDSWiDN 98
Cdd:cd14091    2 YEIKEEIGKGSYSVCKRCIHKATGKEYAVKII------DKSKRDPSEEIE---I------LLRYGQHPNIITLRDVY-DD 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  99 DNNACIFTAYYEGGNMANAIkkARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDH----VQLGNYG 174
Cdd:cd14091   66 GNSVYLVTELLRGGELLDRI--LRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGdpesLRICDFG 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 175 LAKLINPEKPVSMVSG-ISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKA-----PDMagLINKINR---SLM 245
Cdd:cd14091  144 FAKQLRAENGLLMTPCyTANFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPFASgpndtPEV--ILARIGSgkiDLS 221
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 334185276 246 SPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRnpslQPYLLQCQNLSPIYLPVF 301
Cdd:cd14091  222 GGNWDHVSDSAKDLVRKMLHVDPSQRPTAAQVLQ----HPWIRNRDSLPQRQLTDP 273
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
19-281 2.63e-19

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: 88.16  E-value: 2.63e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  19 YHVVEQVRRGKSSSDFVVLHDIEDKKYAMK--KICLAKHTDKlkQTALQEI-SRAVINydlmkllsslKNPYIVHYEDSW 95
Cdd:cd14138    7 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKrsKKPLAGSVDE--QNALREVyAHAVLG----------QHSHVVRYYSAW 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  96 IDNDNnACIFTAYYEGGNMANAIKK--ARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPK--------- 164
Cdd:cd14138   75 AEDDH-MLIQNEYCNGGSLADAISEnyRIMSYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFISRtsipnaase 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 165 ---DDH-------VQLGNYG-LAKLINPEkpvsMVSGISNSMCPEVL-EDQPYGYKSDIWSLGCCMYEITAHQPAfkaPD 232
Cdd:cd14138  154 egdEDEwasnkviFKIGDLGhVTRVSSPQ----VEEGDSRFLANEVLqENYTHLPKADIFALALTVVCAAGAEPL---PT 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 334185276 233 MAGLINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd14138  227 NGDQWHEIRQGKLPRIPQVLSQEFLDLLKVMIHPDPERRPSAVALVKHS 275
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
38-283 2.96e-19

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: 88.07  E-value: 2.96e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  38 HDIEDKKYAMKKICLAKHTDK------LKQTALQEISRAVINYDLMKLLSSLKNPYIVHYEDSWiDNDNNACIFTAYYEG 111
Cdd:cd14197   15 RELGRGKFAVVRKCVEKDSGKefaakfMRKRRKGQDCRMEIIHEIAVLELAQANPWVINLHEVY-ETASEMILVLEYAAG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 112 GNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDD---HVQLGNYGLAKLINPEKPVSMV 188
Cdd:cd14197   94 GEIFNQCVADREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESplgDIKIVDFGLSRILKNSEELREI 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 189 SGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGL---INKINRSLMSPLPIVYSSTLKQMIKLMLR 265
Cdd:cd14197  174 MGTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDKQETflnISQMNVSYSEEEFEHLSESAIDFIKTLLI 253
                        250
                 ....*....|....*...
gi 334185276 266 KKPEYRPTACELLRNPSL 283
Cdd:cd14197  254 KKPENRATAEDCLKHPWL 271
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
34-281 4.63e-19

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: 86.94  E-value: 4.63e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  34 FVVLHDIEDKkyAMKKICLAK---HTDKLKQTALQEISravinydlmkLLSSLKNPYIVHYEDSWiDNDNNACIFTAYYE 110
Cdd:cd14006    6 FGVVKRCIEK--ATGREFAAKfipKRDKKKEAVLREIS----------ILNQLQHPRIIQLHEAY-ESPTELVLILELCS 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 111 GGNMANAIKKaRGKLfPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFL--PKDDHVQLGNYGLAKLINPEKPVSMV 188
Cdd:cd14006   73 GGELLDRLAE-RGSL-SEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLadRPSPQIKIIDFGLARKLNPGEELKEI 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 189 SGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMS---PLPIVYSSTLKQMIKLMLR 265
Cdd:cd14006  151 FGTPEFVAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVDfseEYFSSVSQEAKDFIRKLLV 230
                        250
                 ....*....|....*.
gi 334185276 266 KKPEYRPTACELLRNP 281
Cdd:cd14006  231 KEPRKRPTAQEALQHP 246
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
60-250 5.24e-19

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: 88.10  E-value: 5.24e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  60 KQTALQEISRAVINYDLMKLLSSLKNPYIV--HYEdswIDNDNNACIFTAYYEGGNMANAIKKARGKLFPEERIFKwlAQ 137
Cdd:cd05603   30 KKTILKKKEQNHIMAERNVLLKNLKHPFLVglHYS---FQTSEKLYFVLDYVNGGELFFHLQRERCFLEPRARFYA--AE 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 138 LLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKL-INPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGC 216
Cdd:cd05603  105 VASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEgMEPEETTSTFCGTPEYLAPEVLRKEPYDRTVDWWCLGA 184
                        170       180       190
                 ....*....|....*....|....*....|....
gi 334185276 217 CMYEITAHQPAFKAPDMAGLINKInrsLMSPLPI 250
Cdd:cd05603  185 VLYEMLYGLPPFYSRDVSQMYDNI---LHKPLHL 215
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
59-317 6.02e-19

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: 87.47  E-value: 6.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  59 LKQTALQEISRAVINYDLMKLLSSLKNPYIVHYEDSWIDNDNnACIFTAYYEGGNMANAIKKArgkLFPEERIFKWLAQL 138
Cdd:cd06654   50 IRQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDE-LWVVMEYLAGGSLTDVVTET---CMDEGQIAAVCREC 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 139 LLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPV-SMVSGISNSMCPEVLEDQPYGYKSDIWSLGCC 217
Cdd:cd06654  126 LQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKrSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIM 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 218 MYEITAHQPAF--KAPDMAGLINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRNPSLQpyllqcqnlsp 295
Cdd:cd06654  206 AIEMIEGEPPYlnENPLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLK----------- 274
                        250       260
                 ....*....|....*....|..
gi 334185276 296 IYLPVFPIKPVNSPKDKARRNS 317
Cdd:cd06654  275 IAKPLSSLTPLIAAAKEATKNN 296
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
83-280 6.42e-19

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: 86.79  E-value: 6.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  83 LKNPYIVHYEDSwIDNDNNACIFTAYYEGGNMANAI-KKARgklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIF 161
Cdd:cd14070   60 IRHPNITQLLDI-LETENSYYLVMELCPGGNLMHRIyDKKR---LEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLL 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 162 LPKDDHVQLGNYGL---AKLINPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYE-ITAHQPAFKAP-DMAGL 236
Cdd:cd14070  136 LDENDNIKLIDFGLsncAGILGYSDPFSTQCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAmLTGTLPFTVEPfSLRAL 215
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 334185276 237 INKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRN 280
Cdd:cd14070  216 HQKMVDKEMNPLPTDLSPGAISFLRSLLEPDPLKRPNIKQALAN 259
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
9-293 7.42e-19

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: 88.15  E-value: 7.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276   9 QEEHKFTL---DNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKIclakhtDKLKQTALQEISravinydlmKLLSSLKN 85
Cdd:cd14176    8 QQLHRNSIqftDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKII------DKSKRDPTEEIE---------ILLRYGQH 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  86 PYIVHYEDSWiDNDNNACIFTAYYEGGNMANAIkkARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKD 165
Cdd:cd14176   73 PNIITLKDVY-DDGKYVYVVTELMKGGELLDKI--LRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDE 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 166 ----DHVQLGNYGLAKLINPEKPVSMVSG-ISNSMCPEVLEDQPYGYKSDIWSLGCCMYE-ITAHQPAFKAPD-----MA 234
Cdd:cd14176  150 sgnpESIRICDFGFAKQLRAENGLLMTPCyTANFVAPEVLERQGYDAACDIWSLGVLLYTmLTGYTPFANGPDdtpeeIL 229
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 334185276 235 GLINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRNpslqPYLLQCQNL 293
Cdd:cd14176  230 ARIGSGKFSLSGGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRH----PWIVHWDQL 284
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
28-271 9.39e-19

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: 87.37  E-value: 9.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  28 GKSSSDFVVL--HDIEDKKYAMKkICLAKHTDKLKQTALQEISRAVinydlmkLLSSLKNPYIV--HYedSWIDNDNNAC 103
Cdd:cd05575    4 GKGSFGKVLLarHKAEGKLYAVK-VLQKKAILKRNEVKHIMAERNV-------LLKNVKHPFLVglHY--SFQTKDKLYF 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 104 IFTaYYEGGNMANAIKKARgkLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKL-INPE 182
Cdd:cd05575   74 VLD-YVNGGELFFHLQRER--HFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKEgIEPS 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 183 KPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKInrsLMSPL--PIVYSSTLKQMI 260
Cdd:cd05575  151 DTTSTFCGTPEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNI---LHKPLrlRTNVSPSARDLL 227
                        250
                 ....*....|.
gi 334185276 261 KLMLRKKPEYR 271
Cdd:cd05575  228 EGLLQKDRTKR 238
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
27-286 1.06e-18

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


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 86.24  E-value: 1.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  27 RGKSSSDFVVLHDIEDKKYAMKKICLAKHTDKLKQTaLQEisravinydlMKLLSSLKNPYIVHYEDSWIDNdNNACIFT 106
Cdd:cd06605   11 EGNGGVVSKVRHRPSGQIMAVKVIRLEIDEALQKQI-LRE----------LDVLHKCNSPYIVGFYGAFYSE-GDISICM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 107 AYYEGGNMAnAIKKaRGKLFPEERIFKWLAQLLLAVNYLHSNR-VVHMDLTCSNIFLPKDDHVQLGNYGLA-KLINpekp 184
Cdd:cd06605   79 EYMDGGSLD-KILK-EVGRIPERILGKIAVAVVKGLIYLHEKHkIIHRDVKPSNILVNSRGQVKLCDFGVSgQLVD---- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 185 vSMV---SGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKInrSLMS-----PLPI----VY 252
Cdd:cd06605  153 -SLAktfVGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPYPPPNAKPSMMIF--ELLSyivdePPPLlpsgKF 229
                        250       260       270
                 ....*....|....*....|....*....|....
gi 334185276 253 SSTLKQMIKLMLRKKPEYRPTACELLRNPSLQPY 286
Cdd:cd06605  230 SPDFQDFVSQCLQKDPTERPSYKELMEHPFIKRY 263
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
77-281 1.09e-18

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: 85.77  E-value: 1.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  77 MKLLSSLKNPYIVHYEDSwIDNDNNACIFTAY-YEGGNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDL 155
Cdd:cd14119   45 IQILRRLNHRNVIKLVDV-LYNEEKQKLYMVMeYCVGGLQEMLDSAPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDI 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 156 TCSNIFLPKDDHVQLGNYGLAKLIN---PEKPVSMVSGISNSMCPEVLEDQPY--GYKSDIWSLGCCMYEITAHQPAFKA 230
Cdd:cd14119  124 KPGNLLLTTDGTLKISDFGVAEALDlfaEDDTCTTSQGSPAFQPPEIANGQDSfsGFKVDIWSAGVTLYNMTTGKYPFEG 203
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 334185276 231 PDMAGLINKINRSLMSpLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd14119  204 DNIYKLFENIGKGEYT-IPDDVDPDLQDLLRGMLEKDPEKRFTIEQIRQHP 253
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
19-281 1.31e-18

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: 86.30  E-value: 1.31e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  19 YHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKI--CLAKHTDKlkQTALQEI-SRAVINydlmkllsslKNPYIVHYEDSW 95
Cdd:cd14051    2 FHEVEKIGSGEFGSVYKCINRLDGCVYAIKKSkkPVAGSVDE--QNALNEVyAHAVLG----------KHPHVVRYYSAW 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  96 IDNDNnACIFTAYYEGGNMANAIK--KARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPK----DDHVQ 169
Cdd:cd14051   70 AEDDH-MIIQNEYCNGGSLADAISenEKAGERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFISRtpnpVSSEE 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 170 LGNYGLAKLINPEKPVSM--------VSGISNS---------MCPEVL-EDQPYGYKSDIWSLGCCMYEITAHQPAFK-A 230
Cdd:cd14051  149 EEEDFEGEEDNPESNEVTykigdlghVTSISNPqveegdcrfLANEILqENYSHLPKADIFALALTVYEAAGGGPLPKnG 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 334185276 231 PDMagliNKINRSLMSPLPIVySSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd14051  229 DEW----HEIRQGNLPPLPQC-SPEFNELLRSMIHPDPEKRPSAAALLQHP 274
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
78-271 1.41e-18

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: 86.11  E-value: 1.41e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  78 KLLSSLKNPYIVHYEDSWiDNDNNACIFTAYYEGGNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTC 157
Cdd:cd05607   54 EILEKVNSPFIVSLAYAF-ETKTHLCLVMSLMNGGDLKYHIYNVGERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKP 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 158 SNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLI 237
Cdd:cd05607  133 ENVLLDDNGNCRLSDLGLAVEVKEGKPITQRAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRDHKEKVSK 212
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 334185276 238 NKINRSLMSPLPI----VYSSTLKQMIKLMLRKKPEYR 271
Cdd:cd05607  213 EELKRRTLEDEVKfehqNFTEEAKDICRLFLAKKPENR 250
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
16-277 1.65e-18

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: 87.38  E-value: 1.65e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  16 LDNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLA-KHTDklkqtalQEISRAVINYDLMKLLSSlkNPYIVHYEdS 94
Cdd:cd05617   14 LQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKElVHDD-------EDIDWVQTEKHVFEQASS--NPFLVGLH-S 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  95 WIDNDNNACIFTAYYEGGNMANAIKKARGklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYG 174
Cdd:cd05617   84 CFQTTSRLFLVIEYVNGGDLMFHMQRQRK--LPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 175 LAKL-INPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKA----PDMAGLINKINRSLMSPLP 249
Cdd:cd05617  162 MCKEgLGPGDTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIitdnPDMNTEDYLFQVILEKPIR 241
                        250       260       270
                 ....*....|....*....|....*....|
gi 334185276 250 IVYSSTLK--QMIKLMLRKKPEYRpTACEL 277
Cdd:cd05617  242 IPRFLSVKasHVLKGFLNKDPKER-LGCQP 270
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
49-240 1.71e-18

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: 86.09  E-value: 1.71e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  49 KICLAKHTDKLKQTALQEISRA----------VINYDlmKLLSSLKNPYIVHYEDSWIDnDNNACIFTAYYEGGNMANAI 118
Cdd:cd05580   16 RVRLVKHKDSGKYYALKILKKAkiiklkqvehVLNEK--RILSEVRHPFIVNLLGSFQD-DRNLYMVMEYVPGGELFSLL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 119 KKARgkLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLInPEKPVSMVsGISNSMCPE 198
Cdd:cd05580   93 RRSG--RFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKRV-KDRTYTLC-GTPEYLAPE 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 334185276 199 VLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKI 240
Cdd:cd05580  169 IILSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKI 210
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
108-287 1.86e-18

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 88.39  E-value: 1.86e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 108 YYEGGNMANAIK-KAR-GKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINpekpv 185
Cdd:PTZ00283 120 YANAGDLRQEIKsRAKtNRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDFGFSKMYA----- 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 186 SMVSG-ISNSMC-------PEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPLPIVYSSTLK 257
Cdd:PTZ00283 195 ATVSDdVGRTFCgtpyyvaPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGENMEEVMHKTLAGRYDPLPPSISPEMQ 274
                        170       180       190
                 ....*....|....*....|....*....|
gi 334185276 258 QMIKLMLRKKPEYRPTACELLRNPSLQPYL 287
Cdd:PTZ00283 275 EIVTALLSSDPKRRPSSSKLLNMPICKLFI 304
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
77-284 2.57e-18

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


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 85.06  E-value: 2.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  77 MKLLSSLKNPYIVHYEDsWIDNDNNACIFTAYYEGGNMANAIKKARgkLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLT 156
Cdd:cd14202   52 IKILKELKHENIVALYD-FQEIANSVYLVMEYCNGGDLADYLHTMR--TLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLK 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 157 CSNIFL---------PKDDHVQLGNYGLAKLINPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPA 227
Cdd:cd14202  129 PQNILLsysggrksnPNNIRIKIADFGFARYLQNNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAP 208
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 334185276 228 FKA--PDMAGLINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRNPSLQ 284
Cdd:cd14202  209 FQAssPQDLRLFYEKNKSLSPNIPRETSSHLRQLLLGLLQRNQKDRMDFDEFFHHPFLD 267
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
19-278 3.00e-18

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: 85.04  E-value: 3.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  19 YHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKI-ClakHTDKLKQTALQEISraviNYDLmkllssLKNPYIVHYEDSWI- 96
Cdd:cd13986    2 YRIQRLLGEGGFSFVYLVEDLSTGRLYALKKIlC---HSKEDVKEAMREIE----NYRL------FNHPNILRLLDSQIv 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  97 ---DNDNNACIFTAYYEGGNMANAIKKAR--GKLFPEERIFKWLAQLLLAVNYLHSNRVV---HMDLTCSNIFLPKDDHV 168
Cdd:cd13986   69 keaGGKKEVYLLLPYYKRGSLQDEIERRLvkGTFFPEDRILHIFLGICRGLKAMHEPELVpyaHRDIKPGNVLLSEDDEP 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 169 QLGNYGLA----KLINPEKPVSMVSGISNSMC------PE---VLEDQPYGYKSDIWSLGC----CMYEITAHQPAFKAP 231
Cdd:cd13986  149 ILMDLGSMnparIEIEGRREALALQDWAAEHCtmpyraPElfdVKSHCTIDEKTDIWSLGCtlyaLMYGESPFERIFQKG 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 334185276 232 D---MAGLINKINrslmSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELL 278
Cdd:cd13986  229 DslaLAVLSGNYS----FPDNSRYSEELHQLVKSMLVVNPAERPSIDDLL 274
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
126-283 3.22e-18

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: 84.71  E-value: 3.22e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 126 FPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFL----PKDDhVQLGNYGLAKLINPEKPVSMVSGISNSMCPEVLE 201
Cdd:cd14106  105 LTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLtsefPLGD-IKLCDFGISRVIGEGEEIREILGTPDYVAPEILS 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 202 DQPYGYKSDIWSLGCCMYE-ITAHQPaFKAPDMAGL---INKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACEL 277
Cdd:cd14106  184 YEPISLATDMWSIGVLTYVlLTGHSP-FGGDDKQETflnISQCNLDFPEELFKDVSPLAIDFIKRLLVKDPEKRLTAKEC 262

                 ....*.
gi 334185276 278 LRNPSL 283
Cdd:cd14106  263 LEHPWL 268
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
10-240 3.69e-18

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: 86.99  E-value: 3.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  10 EEHKFTLDNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAKHTDKLKQTALQEISRAVINYDLMKLLSslknpyiV 89
Cdd:cd05624   65 KEMQLHRDDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRAETACFREERNVLVNGDCQWITT-------L 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  90 HYEdswIDNDNNACIFTAYYEGGNMANAIKKARGKLfPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQ 169
Cdd:cd05624  138 HYA---FQDENYLYLVMDYYVGGDLLTLLSKFEDKL-PEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIR 213
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334185276 170 LGNYGLAKLINPEKPV--SMVSGISNSMCPEVL---EDQ--PYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKI 240
Cdd:cd05624  214 LADFGSCLKMNDDGTVqsSVAVGTPDYISPEILqamEDGmgKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKI 291
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
37-279 4.15e-18

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: 84.31  E-value: 4.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  37 LHDIEDKKYAMKKICLAKHTDKLKQTALQEISRavinydlmklLSSLKNPYIVH-YEdsWIDNDNNACIFTAYYEGGNMA 115
Cdd:cd14075   22 IHQLTKEKVAIKILDKTKLDQKTQRLLSREISS----------MEKLHHPNIIRlYE--VVETLSKLHLVMEYASGGELY 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 116 NAIKKaRGKLfPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNSM 195
Cdd:cd14075   90 TKIST-EGKL-SESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFSTHAKRGETLNTFCGSPPYA 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 196 CPEVLEDQPY-GYKSDIWSLGCCMY-EITAHQPaFKAPDMAGLINKINRSLMSpLPIVYSSTLKQMIKLMLRKKPEYRPT 273
Cdd:cd14075  168 APELFKDEHYiGIYVDIWALGVLLYfMVTGVMP-FRAETVAKLKKCILEGTYT-IPSYVSEPCQELIRGILQPVPSDRYS 245

                 ....*.
gi 334185276 274 ACELLR 279
Cdd:cd14075  246 IDEIKN 251
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
18-266 4.60e-18

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: 85.84  E-value: 4.60e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  18 NYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKIclakhtdkLKQTALQEISRAVINYDLMKLLSSLKNPYIVHYEDSWID 97
Cdd:cd05602    8 DFHFLKVIGKGSFGKVLLARHKSDEKFYAVKVL--------QKKAILKKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  98 NDNNACIFTaYYEGGNMANAIKKARGKLFPEERIFKwlAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAK 177
Cdd:cd05602   80 TDKLYFVLD-YINGGELFYHLQRERCFLEPRARFYA--AEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 178 L-INPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPLPIVySSTL 256
Cdd:cd05602  157 EnIEPNGTTSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLKPNI-TNSA 235
                        250
                 ....*....|
gi 334185276 257 KQMIKLMLRK 266
Cdd:cd05602  236 RHLLEGLLQK 245
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
19-271 5.21e-18

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: 85.15  E-value: 5.21e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  19 YHVVEQVRRgKSSSDfvvlhdiEDKKYAMKKICLAKHTDKLKQTALQEISRAVinydlmklLSSLKNPYIV--HYEdswI 96
Cdd:cd05584    9 YGKVFQVRK-TTGSD-------KGKIFAMKVLKKASIVRNQKDTAHTKAERNI--------LEAVKHPFIVdlHYA---F 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  97 DNDNNACIFTAYYEGGNMANAIKkaRGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLA 176
Cdd:cd05584   70 QTGGKLYLILEYLSGGELFMHLE--REGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLC 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 177 K-LINPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSpLPIVYSST 255
Cdd:cd05584  148 KeSIHDGTVTHTFCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGKLN-LPPYLTNE 226
                        250
                 ....*....|....*.
gi 334185276 256 LKQMIKLMLRKKPEYR 271
Cdd:cd05584  227 ARDLLKKLLKRNVSSR 242
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
21-287 5.32e-18

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: 84.41  E-value: 5.32e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  21 VVEQVRRGKSSSDFVVLHdIEDKKYAMKKICLAKHTDKLKQTALQEISravinydlmkLLSSLKNPYIVHYEDSWIDNDN 100
Cdd:cd06620    9 TLKDLGAGNGGSVSKVLH-IPTGTIMAKKVIHIDAKSSVRKQILRELQ----------ILHECHSPYIVSFYGAFLNENN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 101 NACIFTAYYEGGNMANAIKKarGKLFPEERIFKWLAQLLLAVNYLHS-NRVVHMDLTCSNIFLPKDDHVQLGNYGLA-KL 178
Cdd:cd06620   78 NIIICMEYMDCGSLDKILKK--KGPFPEEVLGKIAVAVLEGLTYLYNvHRIIHRDIKPSNILVNSKGQIKLCDFGVSgEL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 179 INPekpVSMV-SGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMA--------GLINKINRSLMSPLP 249
Cdd:cd06620  156 INS---IADTfVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFAGSNDDddgyngpmGILDLLQRIVNEPPP 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 334185276 250 -----IVYSSTLKQMIKLMLRKKPEYRPTACELLRNPSLQPYL 287
Cdd:cd06620  233 rlpkdRIFPKDLRDFVDRCLLKDPRERPSPQLLLDHDPFIQAV 275
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
45-281 5.89e-18

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: 85.31  E-value: 5.89e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  45 YAMKKIclakhtDKLKQTALQEISRAVINYDLMKLLSSLKNPYIVHYEDSWiDNDNNACIFTAYYEGGNMANAIKKaRGK 124
Cdd:cd05586   21 YAMKVL------SKKVIVAKKEVAHTIGERNILVRTALDESPFIVGLKFSF-QTPTDLYLVTDYMSGGELFWHLQK-EGR 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 125 lFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKL-INPEKPVSMVSGISNSMCPEV-LED 202
Cdd:cd05586   93 -FSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSKAdLTDNKTTNTFCGTTEYLAPEVlLDE 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 203 QPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYR----PTACELL 278
Cdd:cd05586  172 KGYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKVRFPKDVLSDEGRSFVKGLLNRNPKHRlgahDDAVELK 251

                 ...
gi 334185276 279 RNP 281
Cdd:cd05586  252 EHP 254
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
19-281 6.06e-18

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: 84.25  E-value: 6.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  19 YHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAkhTDKLKQTALQEISRAVINYdlMKLLSSLKN-PYIVHYEDSWid 97
Cdd:cd14181   12 YDPKEVIGRGVSSVVRRCVHRHTGQEFAVKIIEVT--AERLSPEQLEEVRSSTLKE--IHILRQVSGhPSIITLIDSY-- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  98 nDNNACIFTAYyeggnmaNAIKkaRGKLF---------PEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHV 168
Cdd:cd14181   86 -ESSTFIFLVF-------DLMR--RGELFdyltekvtlSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 169 QLGNYGLAKLINPEKPVSMVSGISNSMCPEVL-----EDQP-YGYKSDIWSLGCCMYEITAHQPAF---KAPDMAGLINK 239
Cdd:cd14181  156 KLSDFGFSCHLEPGEKLRELCGTPGYLAPEILkcsmdETHPgYGKEVDLWACGVILFTLLAGSPPFwhrRQMLMLRMIME 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 334185276 240 INRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd14181  236 GRYQFSSPEWDDRSSTVKDLISRLLVVDPEIRLTAEQALQHP 277
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
134-281 6.65e-18

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: 83.79  E-value: 6.65e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 134 WLAQLLLAVNYLHSNRVVHMDLTCSNIFL--PKDDHVQLGNYGLAKLINPEKPVSMVSGISNSMCPEVLEDQPYGYKSDI 211
Cdd:cd14107  103 YIQQVLEGIGYLHGMNILHLDIKPDNILMvsPTREDIKICDFGFAQEITPSEHQFSKYGSPEFVAPEIVHQEPVSAATDI 182
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334185276 212 WSLGCCMY-EITAHQPAFKAPDMAGLINkINRSLMS---PLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd14107  183 WALGVIAYlSLTCHSPFAGENDRATLLN-VAEGVVSwdtPEITHLSEDAKDFIKRVLQPDPEKRPSASECLSHE 255
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
77-283 8.67e-18

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: 83.29  E-value: 8.67e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  77 MKLLSSLKNPYIVHYEDSWIDNDNNACIFTAYYEGGNMANAIKKaRGKLfPEERIFKWLAQLLLAVNYLHSNRVVHMDLT 156
Cdd:cd14165   52 LEILARLNHKSIIKTYEIFETSDGKVYIVMELGVQGDLLEFIKL-RGAL-PEDVARKMFHQLSSAIKYCHELDIVHRDLK 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 157 CSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVsgISNSMC-------PEVLEDQPYGYK-SDIWSLGCCMYEIT-AHQPa 227
Cdd:cd14165  130 CENLLLDKDFNIKLTDFGFSKRCLRDENGRIV--LSKTFCgsaayaaPEVLQGIPYDPRiYDIWSLGVILYIMVcGSMP- 206
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 334185276 228 FKAPDMAGL--INKINRsLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRNPSL 283
Cdd:cd14165  207 YDDSNVKKMlkIQKEHR-VRFPRSKNLTSECKDLIYRLLQPDVSQRLCIDEVLSHPWL 263
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
28-271 9.30e-18

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: 84.36  E-value: 9.30e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  28 GKSSSDFVVLHDIEDKK--YAMKkiCLAKHT----DKLKQTAlqeISRAVinydlmkLLSSLKNPYIVHYEDSWIDNDNn 101
Cdd:cd05592    4 GKGSFGKVMLAELKGTNqyFAIK--ALKKDVvledDDVECTM---IERRV-------LALASQHPFLTHLFCTFQTESH- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 102 acIF--TAYYEGGNMANAIKKArGKlFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKL- 178
Cdd:cd05592   71 --LFfvMEYLNGGDLMFHIQQS-GR-FDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCKEn 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 179 INPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKI-NRSLMSPLPIvySSTLK 257
Cdd:cd05592  147 IYGENKASTFCGTPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSIcNDTPHYPRWL--TKEAA 224
                        250
                 ....*....|....
gi 334185276 258 QMIKLMLRKKPEYR 271
Cdd:cd05592  225 SCLSLLLERNPEKR 238
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
65-281 1.12e-17

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: 83.12  E-value: 1.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  65 QEISravinydlmkLLSSLKNPYIVHYEDSWIDNDNnACIFTAYYEGGNMANAIKKARGklFPEERIFKWLAQLLLAVNY 144
Cdd:cd06613   46 QEIS----------MLKECRHPNIVAYFGSYLRRDK-LWIVMEYCGGGSLQDIYQVTGP--LSELQIAYVCRETLKGLAY 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 145 LHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINP--EKPVSMVsGISNSMCPEVLEDQ---PYGYKSDIWSLGccmy 219
Cdd:cd06613  113 LHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQLTAtiAKRKSFI-GTPYWMAPEVAAVErkgGYDGKCDIWALG---- 187
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334185276 220 eITAHQPAFKAPDMAGL-----INKINRSLMSPlPIV-----YSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd06613  188 -ITAIELAELQPPMFDLhpmraLFLIPKSNFDP-PKLkdkekWSPDFHDFIKKCLTKNPKKRPTATKLLQHP 257
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
17-291 1.21e-17

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: 83.53  E-value: 1.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  17 DNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKIclakhtDKLKQTALQEISravinydlmKLLSSLKNPYIVHYEDSWi 96
Cdd:cd14178    3 DGYEIKEDIGIGSYSVCKRCVHKATSTEYAVKII------DKSKRDPSEEIE---------ILLRYGQHPNIITLKDVY- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  97 DNDNNACIFTAYYEGGNMANAIkkARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKD----DHVQLGN 172
Cdd:cd14178   67 DDGKFVYLVMELMRGGELLDRI--LRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDEsgnpESIRICD 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 173 YGLAKLINPEKPVSMVSG-ISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITA-HQPAFKAPD-----MAGLINKINRSLM 245
Cdd:cd14178  145 FGFAKQLRAENGLLMTPCyTANFVAPEVLKRQGYDAACDIWSLGILLYTMLAgFTPFANGPDdtpeeILARIGSGKYALS 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 334185276 246 SPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRNPSL--QPYLLQCQ 291
Cdd:cd14178  225 GGNWDSISDAAKDIVSKMLHVDPHQRLTAPQVLRHPWIvnREYLSQNQ 272
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
35-271 1.36e-17

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


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 83.04  E-value: 1.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  35 VVLHDIEDKKYAMKkiCLAKHtdKLKQTALQE-IsravinYDLMKLLSSLKNPYIVHYEDSWIDNdNNACIFTAYYEGGN 113
Cdd:cd05572   11 LVQLKSKGRTFALK--CVKKR--HIVQTRQQEhI------FSEKEILEECNSPFIVKLYRTFKDK-KYLYMLMEYCLGGE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 114 MANAIKKaRGkLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISN 193
Cdd:cd05572   80 LWTILRD-RG-LFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKKLGSGRKTWTFCGTPE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 194 SMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMA-----GLINKINRSLMSPLPIvySSTLKQMIKLMLRKKP 268
Cdd:cd05572  158 YVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFGGDDEDpmkiyNIILKGIDKIEFPKYI--DKNAKNLIKQLLRRNP 235

                 ...
gi 334185276 269 EYR 271
Cdd:cd05572  236 EER 238
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
17-281 1.36e-17

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


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 83.54  E-value: 1.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  17 DNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKIclakhtDKLKQTALQEISravinydlmKLLSSLKNPYIVHYEDSWi 96
Cdd:cd14175    1 DGYVVKETIGVGSYSVCKRCVHKATNMEYAVKVI------DKSKRDPSEEIE---------ILLRYGQHPNIITLKDVY- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  97 DNDNNACIFTAYYEGGNMANAIkkARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKD----DHVQLGN 172
Cdd:cd14175   65 DDGKHVYLVTELMRGGELLDKI--LRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVDEsgnpESLRICD 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 173 YGLAKLINPEKPVSMVSG-ISNSMCPEVLEDQPYGYKSDIWSLGCCMYEIT------AHQPAFKAPDMAGLINKINRSLM 245
Cdd:cd14175  143 FGFAKQLRAENGLLMTPCyTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLagytpfANGPSDTPEEILTRIGSGKFTLS 222
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 334185276 246 SPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd14175  223 GGNWNTVSDAAKDLVSKMLHVDPHQRLTAKQVLQHP 258
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
18-281 1.46e-17

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: 83.64  E-value: 1.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  18 NYHVVEQVRRGKSSSDFVVLHDIED-KKYAMKKICLAK-HTDKLKQTALQEISRAVinyDLMKLLSslkNPYIVHYEDSw 95
Cdd:cd14096    2 NYRLINKIGEGAFSNVYKAVPLRNTgKPVAIKVVRKADlSSDNLKGSSRANILKEV---QIMKRLS---HPNIVKLLDF- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  96 IDNDNNACIFTAYYEGGNMANAIkkARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSN-IFLP----------- 163
Cdd:cd14096   75 QESDEYYYIVLELADGGEIFHQI--VRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENlLFEPipfipsivklr 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 164 -------KDDH--------------VQLGNYGLAKLINPEKPVSmVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEIT 222
Cdd:cd14096  153 kadddetKVDEgefipgvggggigiVKLADFGLSKQVWDSNTKT-PCGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLL 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334185276 223 AHQPAFKAPDMAGLINKINR---SLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd14096  232 CGFPPFYDESIETLTEKISRgdyTFLSPWWDEISKSAKDLISHLLTVDPAKRYDIDEFLAHP 293
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
79-311 1.78e-17

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: 83.86  E-value: 1.78e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  79 LLSSLKNPYIVHYEDSWIDNDNNACIFTaYYEGGNMANAIKKARGklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCS 158
Cdd:cd05604   50 LLKNVKHPFLVGLHYSFQTTDKLYFVLD-FVNGGELFFHLQRERS--FPEPRARFYAAEIASALGYLHSINIVYRDLKPE 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 159 NIFLPKDDHVQLGNYGLAKL-INPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLI 237
Cdd:cd05604  127 NILLDSQGHIVLTDFGLCKEgISNSDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMY 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 238 NKINRSLMSPLPIVySSTLKQMIKLMLRKKPE----YRPTACELLRNP---SLQPYLLQCQNLSPIYLPvfpikPVNSPK 310
Cdd:cd05604  207 ENILHKPLVLRPGI-SLTAWSILEELLEKDRQlrlgAKEDFLEIKNHPffeSINWTDLVQKKIPPPFNP-----NVNGPD 280

                 .
gi 334185276 311 D 311
Cdd:cd05604  281 D 281
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
42-281 1.98e-17

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


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 82.60  E-value: 1.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  42 DKKYAMKKIClakhTDKLKQTALQEISRAVinydlmKLLSSLKNPYIVHYEDSWiDNDNNACIFTAYYEGGNMANAIKka 121
Cdd:cd14097   26 QTKWAIKKIN----REKAGSSAVKLLEREV------DILKHVNHAHIIHLEEVF-ETPKRMYLVMELCEDGELKELLL-- 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 122 RGKLFPEERIfKWLAQLLL-AVNYLHSNRVVHMDLTCSNIFLPKDD-------HVQLGNYGLA--KLINPEKPVSMVSGI 191
Cdd:cd14097   93 RKGFFSENET-RHIIQSLAsAVAYLHKNDIVHRDLKLENILVKSSIidnndklNIKVTDFGLSvqKYGLGEDMLQETCGT 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 192 SNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPLPIVY---SSTLKQMIKLMLRKKP 268
Cdd:cd14097  172 PIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDLTFTQSVWqsvSDAAKNVLQQLLKVDP 251
                        250
                 ....*....|...
gi 334185276 269 EYRPTACELLRNP 281
Cdd:cd14097  252 AHRMTASELLDNP 264
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
17-279 2.03e-17

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: 82.72  E-value: 2.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  17 DNYHV--VEQVRRGKSSSDFVVLHDIEDKKYAMKKIcLAKHTDKLkQTALQEISravinydLMKLLSslKNPYIVHYEDS 94
Cdd:cd14037    1 GSHHVtiEKYLAEGGFAHVYLVKTSNGGNRAALKRV-YVNDEHDL-NVCKREIE-------IMKRLS--GHKNIVGYIDS 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  95 WIDND-NNAC---IFTAYYEGGNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNR--VVHMDLTCSNIFLPKDDHV 168
Cdd:cd14037   70 SANRSgNGVYevlLLMEYCKGGGVIDLMNQRLQTGLTESEILKIFCDVCEAVAAMHYLKppLIHRDLKVENVLISDSGNY 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 169 QLGNYGLA--KLINPEKP--VSMV-SGIS--NSMC---PEVLE---DQPYGYKSDIWSLGCCMYEITAHQPAFkapDMAG 235
Cdd:cd14037  150 KLCDFGSAttKILPPQTKqgVTYVeEDIKkyTTLQyraPEMIDlyrGKPITEKSDIWALGCLLYKLCFYTTPF---EESG 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 334185276 236 LINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLR 279
Cdd:cd14037  227 QLAILNGNFTFPDNSRYSKRLHKLIRYMLEEDPEKRPNIYQVSY 270
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
17-281 2.12e-17

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


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 82.97  E-value: 2.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  17 DNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAKHTDKLKQTaLQEISRAVinydlmKLLSSLKNPYIVHYEDSwI 96
Cdd:cd14094    3 DVYELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFTSSPGLS-TEDLKREA------SICHMLKHPHIVELLET-Y 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  97 DNDNNACIFTAYYEGGNMANAIKK--ARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDH---VQLG 171
Cdd:cd14094   75 SSDGMLYMVFEFMDGADLCFEIVKraDAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 172 NYGLAKLInPEKPvSMVSG---ISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAF--KAPDMAGLINKINRSLMS 246
Cdd:cd14094  155 GFGVAIQL-GESG-LVAGGrvgTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFygTKERLFEGIIKGKYKMNP 232
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 334185276 247 PLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd14094  233 RQWSHISESAKDLVRRMLMLDPAERITVYEALNHP 267
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
34-280 2.17e-17

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: 83.16  E-value: 2.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  34 FVVLHDIEDKKYAMKKICLAKHTDKL----------KQT--ALQEISRAVinydlmKLLSSLKNPYIVHYEDSWIdNDNN 101
Cdd:cd06633   23 FVDLHEIGHGSFGAVYFATNSHTNEVvaikkmsysgKQTneKWQDIIKEV------KFLQQLKHPNTIEYKGCYL-KDHT 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 102 ACIFTAYYEGGnmANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINP 181
Cdd:cd06633   96 AWLVMEYCLGS--ASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIASP 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 182 EKpvSMVsGISNSMCPEV---LEDQPYGYKSDIWSLGCCMYEITAHQPA-FKAPDMAGLINKINRSLMSPLPIVYSSTLK 257
Cdd:cd06633  174 AN--SFV-GTPYWMAPEVilaMDEGQYDGKVDIWSLGITCIELAERKPPlFNMNAMSALYHIAQNDSPTLQSNEWTDSFR 250
                        250       260
                 ....*....|....*....|...
gi 334185276 258 QMIKLMLRKKPEYRPTACELLRN 280
Cdd:cd06633  251 GFVDYCLQKIPQERPSSAELLRH 273
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
43-271 2.30e-17

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: 82.76  E-value: 2.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  43 KKYAMKKIcLAKHTDKLKQTALQEISRAVINYDLMKLLSSLKNPYivhyedswiDNDNNACIFTAYYEGGNMANAIKKAR 122
Cdd:cd05630   26 KMYACKKL-EKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAY---------ETKDALCLVLTLMNGGDLKFHIYHMG 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 123 GKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNSMCPEVLED 202
Cdd:cd05630   96 QAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPEGQTIKGRVGTVGYMAPEVVKN 175
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334185276 203 QPYGYKSDIWSLGCCMYEITAHQPAFKAPDmagliNKINRS----LMSPLPIVYSSTL----KQMIKLMLRKKPEYR 271
Cdd:cd05630  176 ERYTFSPDWWALGCLLYEMIAGQSPFQQRK-----KKIKREeverLVKEVPEEYSEKFspqaRSLCSMLLCKDPAER 247
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
46-281 3.06e-17

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: 82.04  E-value: 3.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  46 AMKKICLAKHTDKLKQTALQEISRAvINYDLmKLLSSLKNPYIVHY---EDSwidnDNNACIFTAYYEGGNMANAIKKAR 122
Cdd:cd06629   30 AVKQVELPKTSSDRADSRQKTVVDA-LKSEI-DTLKDLDHPNIVQYlgfEET----EDYFSIFLEYVPGGSIGSCLRKYG 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 123 GklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAK----LINPEKPVSMvSGISNSMCPE 198
Cdd:cd06629  104 K--FEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISKksddIYGNNGATSM-QGSVFWMAPE 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 199 VLEDQPYGY--KSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPlPIVYSSTLKQMIKLMLRKK----PEYRP 272
Cdd:cd06629  181 VIHSQGQGYsaKVDIWSLGCVVLEMLAGRRPWSDDEAIAAMFKLGNKRSAP-PVPEDVNLSPEALDFLNACfaidPRDRP 259

                 ....*....
gi 334185276 273 TACELLRNP 281
Cdd:cd06629  260 TAAELLSHP 268
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
23-281 3.54e-17

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: 81.96  E-value: 3.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  23 EQVRRGKSSSDFVVLHDIEDKKYAMKkiCLAKHTDKLKQTALQEISravinydlmkLLSSLKNPYIVHYEDSWiDNDNNA 102
Cdd:cd14166    9 EVLGSGAFSEVYLVKQRSTGKLYALK--CIKKSPLSRDSSLENEIA----------VLKRIKHENIVTLEDIY-ESTTHY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 103 CIFTAYYEGGNMANAIKKaRGkLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNI-FLPKDDH--VQLGNYGLAKLi 179
Cdd:cd14166   76 YLVMQLVSGGELFDRILE-RG-VYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLlYLTPDENskIMITDFGLSKM- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 180 NPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINR---SLMSPLPIVYSSTL 256
Cdd:cd14166  153 EQNGIMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEgyyEFESPFWDDISESA 232
                        250       260
                 ....*....|....*....|....*
gi 334185276 257 KQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd14166  233 KDFIRHLLEKNPSKRYTCEKALSHP 257
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
103-299 4.28e-17

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: 82.33  E-value: 4.28e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 103 CIFTAYYEGGNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPE 182
Cdd:cd05632   78 CLVLTIMNGGDLKFHIYNMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKIPEG 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 183 KPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPLPiVYSSTL----KQ 258
Cdd:cd05632  158 ESIRGRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKREEVDRRVLETEE-VYSAKFseeaKS 236
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 334185276 259 MIKLMLRKKPEYR-----PTACELLRNPSLQPY---LLQCQNLSPIYLP 299
Cdd:cd05632  237 ICKMLLTKDPKQRlgcqeEGAGEVKRHPFFRNMnfkRLEAGMLDPPFVP 285
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
38-228 4.52e-17

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 82.56  E-value: 4.52e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  38 HDIEDKKYAMKkiCLAKHTD-KLKQT--ALQEISravinydlmkLLSSLKNPYIVHYEDSWIDnDNNACIFTAYYEGGNM 114
Cdd:PTZ00263  39 HKGTGEYYAIK--CLKKREIlKMKQVqhVAQEKS----------ILMELSHPFIVNMMCSFQD-ENRVYFLLEFVVGGEL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 115 ANAIKKArGKlFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLInPEKPVSMVsGISNS 194
Cdd:PTZ00263 106 FTHLRKA-GR-FPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKV-PDRTFTLC-GTPEY 181
                        170       180       190
                 ....*....|....*....|....*....|....
gi 334185276 195 MCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAF 228
Cdd:PTZ00263 182 LAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPF 215
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
18-279 6.14e-17

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: 81.23  E-value: 6.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  18 NYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKIcLAKHTDKLKQtALQEISravinydLMKLLSslKNPYIVHYEDSWID 97
Cdd:cd13985    1 RYQVTKQLGEGGFSYVYLAHDVNTGRRYALKRM-YFNDEEQLRV-AIKEIE-------IMKRLC--GHPNIVQYYDSAIL 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  98 NDNN--ACIFTAYYEGGNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSN--RVVHMDLTCSNIFLPKDDHVQLGNY 173
Cdd:cd13985   70 SSEGrkEVLLLMEYCPGSLVDILEKSPPSPLSEEEVLRIFYQICQAVGHLHSQspPIIHRDIKIENILFSNTGRFKLCDF 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 174 GLA----KLINPEKPVSMVSGISNSMC------PEVL---EDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKi 240
Cdd:cd13985  150 GSAttehYPLERAEEVNIIEEEIQKNTtpmyraPEMIdlySKKPIGEKADIWALGCLLYKLCFFKLPFDESSKLAIVAG- 228
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 334185276 241 nrSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLR 279
Cdd:cd13985  229 --KYSIPEQPRYSPELHDLIRHMLTPDPAERPDIFQVIN 265
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
49-283 6.18e-17

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: 80.92  E-value: 6.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  49 KICLAKHT--------DKLKQT--ALQEISRAVINY-----DLMKLLSSLKNPYIVHYEDSwiDNDNNAC-IFTAYYEGG 112
Cdd:cd06624   13 RVVLGKGTfgvvyaarDLSTQVriAIKEIPERDSREvqplhEEIALHSRLSHKNIVQYLGS--VSEDGFFkIFMEQVPGG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 113 NMANAIKKARGKLFPEERIFKWLA-QLLLAVNYLHSNRVVHMDLtcsniflpKDDHVQLGNY-GLAKL-----------I 179
Cdd:cd06624   91 SLSALLRSKWGPLKDNENTIGYYTkQILEGLKYLHDNKIVHRDI--------KGDNVLVNTYsGVVKIsdfgtskrlagI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 180 NPEkpVSMVSGISNSMCPEVLEDQPYGY--KSDIWSLGCCMYEITAHQPAF---KAPDMAglINKINRSLMSP-LPIVYS 253
Cdd:cd06624  163 NPC--TETFTGTLQYMAPEVIDKGQRGYgpPADIWSLGCTIIEMATGKPPFielGEPQAA--MFKVGMFKIHPeIPESLS 238
                        250       260       270
                 ....*....|....*....|....*....|
gi 334185276 254 STLKQMIKLMLRKKPEYRPTACELLRNPSL 283
Cdd:cd06624  239 EEAKSFILRCFEPDPDKRATASDLLQDPFL 268
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
46-284 6.38e-17

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: 80.96  E-value: 6.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  46 AMKKIclaKHTDKLKQTALQEISRAVinydlmKLLSSLKNPYIVHYEDSWIdNDNNACIFTAYYEGGnmANAIKKARGKL 125
Cdd:cd06607   30 AIKKM---SYSGKQSTEKWQDIIKEV------KFLRQLRHPNTIEYKGCYL-REHTAWLVMEYCLGS--ASDIVEVHKKP 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 126 FPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKpvSMVsGISNSMCPEV---LED 202
Cdd:cd06607   98 LQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFGSASLVCPAN--SFV-GTPYWMAPEVilaMDE 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 203 QPYGYKSDIWSLGCCMYEITAHQPA-FKAPDMAGLINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd06607  175 GQYDGKVDVWSLGITCIELAERKPPlFNMNAMSALYHIAQNDSPTLSSGEWSDDFRNFVDSCLQKIPQDRPSAEDLLKHP 254

                 ...
gi 334185276 282 SLQ 284
Cdd:cd06607  255 FVT 257
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
108-281 6.58e-17

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: 81.19  E-value: 6.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 108 YYEGGNMANAIKKAR--GKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGL-AKLINPEKP 184
Cdd:cd06608   90 YCGGGSVTDLVKGLRkkGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGVsAQLDSTLGR 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 185 VSMVSGISNSMCPEVL--EDQP---YGYKSDIWSLGccmyeITA------HQPAFKAPDMAGLInKINRS----LMSPLP 249
Cdd:cd06608  170 RNTFIGTPYWMAPEVIacDQQPdasYDARCDVWSLG-----ITAieladgKPPLCDMHPMRALF-KIPRNppptLKSPEK 243
                        170       180       190
                 ....*....|....*....|....*....|..
gi 334185276 250 ivYSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd06608  244 --WSKEFNDFISECLIKNYEQRPFTEELLEHP 273
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
33-283 6.76e-17

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: 80.51  E-value: 6.76e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  33 DFVVLHDIEDKKYAmkKICLAKHTDKLKQTALQEISRAVINYDLMK-------------LLSSLK---NPYIVHYEDSWI 96
Cdd:cd14004    1 DYTILKEMGEGAYG--QVNLAIYKSKGKEVVIKFIFKERILVDTWVrdrklgtvpleihILDTLNkrsHPNIVKLLDFFE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  97 DNDNNACIFTAYYEGGNMANAIKKARGKLFPEER-IFKwlaQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGL 175
Cdd:cd14004   79 DDEFYYLVMEKHGSGMDLFDFIERKPNMDEKEAKyIFR---QVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFGS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 176 AKLINPeKPVSMVSGISNSMCPEVLEDQPYGYKS-DIWSLGCCMYEITAHQPAFKAPD--MAGLINkinrslmspLPIVY 252
Cdd:cd14004  156 AAYIKS-GPFDTFVGTIDYAAPEVLRGNPYGGKEqDIWALGVLLYTLVFKENPFYNIEeiLEADLR---------IPYAV 225
                        250       260       270
                 ....*....|....*....|....*....|.
gi 334185276 253 SSTLKQMIKLMLRKKPEYRPTACELLRNPSL 283
Cdd:cd14004  226 SEDLIDLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
18-221 8.51e-17

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: 80.91  E-value: 8.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  18 NYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKIClaKHTDKLKQtalqEISRAVINYDLmklLSSLKNPYIVHYEDSWiD 97
Cdd:cd05609    1 DFETIKLISNGAYGAVYLVRHRETRQRFAMKKIN--KQNLILRN----QIQQVFVERDI---LTFAENPFVVSMYCSF-E 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  98 NDNNACIFTAYYEGGNMANAIKKArGKLfPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAK 177
Cdd:cd05609   71 TKRHLCMVMEYVEGGDCATLLKNI-GPL-PVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSK 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 178 L-------------INPEKPVSM---VSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEI 221
Cdd:cd05609  149 IglmslttnlyeghIEKDTREFLdkqVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEF 208
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
17-240 1.15e-16

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: 82.37  E-value: 1.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  17 DNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAKHTDKLKQTALQEISRAVINYDlMKLLSSLknpyivHYEdswI 96
Cdd:cd05623   72 EDFEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAETACFREERDVLVNGD-SQWITTL------HYA---F 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  97 DNDNNACIFTAYYEGGNMANAIKKARGKLfPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLA 176
Cdd:cd05623  142 QDDNNLYLVMDYYVGGDLLTLLSKFEDRL-PEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGSC 220
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334185276 177 KLINPEKPV--SMVSGISNSMCPEVLEDQP-----YGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKI 240
Cdd:cd05623  221 LKLMEDGTVqsSVAVGTPDYISPEILQAMEdgkgkYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKI 291
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
16-283 1.39e-16

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


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 79.94  E-value: 1.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  16 LDNYHVVEQVRRGKsssdFVVLHDIEDKK----YAMKKICLAKHTDKlkQTALQEISravinydlmkLLSSLKNPYIVHY 91
Cdd:cd14114    1 YDHYDILEELGTGA----FGVVHRCTERAtgnnFAAKFIMTPHESDK--ETVRKEIQ----------IMNQLHHPKLINL 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  92 EDSWIDNDNNACIFTaYYEGGNMANAIKkARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLP--KDDHVQ 169
Cdd:cd14114   65 HDAFEDDNEMVLILE-FLSGGELFERIA-AEHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTtkRSNEVK 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 170 LGNYGLAKLINPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINR------- 242
Cdd:cd14114  143 LIDFGLATHLDPKESVKVTTGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKScdwnfdd 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 334185276 243 SLMSPLpivySSTLKQMIKLMLRKKPEYRPTACELLRNPSL 283
Cdd:cd14114  223 SAFSGI----SEEAKDFIRKLLLADPNKRMTIHQALEHPWL 259
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
126-281 1.69e-16

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: 80.10  E-value: 1.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 126 FPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLIN-PEKPVSMVSGISNSMCPEVL---E 201
Cdd:cd14118  112 LSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIADFGVSNEFEgDDALLSSTAGTPAFMAPEALsesR 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 202 DQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKI-NRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRN 280
Cdd:cd14118  192 KKFSGKALDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIkTDPVVFPDDPVVSEQLKDLILRMLDKNPSERITLPEIKEH 271

                 .
gi 334185276 281 P 281
Cdd:cd14118  272 P 272
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
28-228 1.71e-16

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


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 81.23  E-value: 1.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  28 GKSSS-----DFVVLHDIEDKKYAMKKICLAKHTDKLkqTALQEISRAVINYDL-MKLLSSLKN--------PYIVHYEd 93
Cdd:cd05618   11 GKASSslglqDFDLLRVIGRGSYAKVLLVRLKKTERI--YAMKVVKKELVNDDEdIDWVQTEKHvfeqasnhPFLVGLH- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  94 SWIDNDNNACIFTAYYEGGNMANAIKKARGklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNY 173
Cdd:cd05618   88 SCFQTESRLFFVIEYVNGGDLMFHMQRQRK--LPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDY 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 334185276 174 GLAKL-INPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAF 228
Cdd:cd05618  166 GMCKEgLRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPF 221
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
100-278 1.72e-16

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: 79.36  E-value: 1.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 100 NNACIFTAYYEGGNMANAIKKARGKlFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLI 179
Cdd:cd14062   61 PQLAIVTQWCEGSSLYKHLHVLETK-FEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLATVK 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 180 ---NPEKPVSMVSGISNSMCPEVL---EDQPYGYKSDIWSLGCCMYEITAHQPAF---KAPDMagLINKINRSLMSP-LP 249
Cdd:cd14062  140 trwSGSQQFEQPTGSILWMAPEVIrmqDENPYSFQSDVYAFGIVLYELLTGQLPYshiNNRDQ--ILFMVGRGYLRPdLS 217
                        170       180       190
                 ....*....|....*....|....*....|..
gi 334185276 250 IVYSSTLKQMIKLM---LRKKPEYRPTACELL 278
Cdd:cd14062  218 KVRSDTPKALRRLMedcIKFQRDERPLFPQIL 249
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
17-265 1.76e-16

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: 80.14  E-value: 1.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  17 DNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKkICLAKHTDKLKQTA--LQEisravinydlMKLLSSLKNPYIVHYEDS 94
Cdd:cd14209    1 DDFDRIKTLGTGSFGRVMLVRHKETGNYYAMK-ILDKQKVVKLKQVEhtLNE----------KRILQAINFPFLVKLEYS 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  95 WIDNDNNACIFtAYYEGGNMANAIKKARGklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYG 174
Cdd:cd14209   70 FKDNSNLYMVM-EYVPGGEMFSHLRRIGR--FSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFG 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 175 LAKLInpEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSpLPIVYSS 254
Cdd:cd14209  147 FAKRV--KGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVR-FPSHFSS 223
                        250
                 ....*....|.
gi 334185276 255 TLKQMIKLMLR 265
Cdd:cd14209  224 DLKDLLRNLLQ 234
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
43-271 1.78e-16

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: 80.09  E-value: 1.78e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  43 KKYAMKKIcLAKHTDKLKQTALQEISRavinydlmKLLSSLKNPYIVH----YEdswidNDNNACIFTAYYEGGNMANAI 118
Cdd:cd05605   26 KMYACKKL-EKKRIKKRKGEAMALNEK--------QILEKVNSRFVVSlayaYE-----TKDALCLVLTIMNGGDLKFHI 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 119 KKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNSMCPE 198
Cdd:cd05605   92 YNMGNPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVEIPEGETIRGRVGTVGYMAPE 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 199 VLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDmagliNKINRSLMSPL----PIVYSSTL----KQMIKLMLRKKPEY 270
Cdd:cd05605  172 VVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARK-----EKVKREEVDRRvkedQEEYSEKFseeaKSICSQLLQKDPKT 246

                 .
gi 334185276 271 R 271
Cdd:cd05605  247 R 247
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
34-278 1.92e-16

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: 79.86  E-value: 1.92e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  34 FVVLHDIEDKKYAMKKICLAKHTDKLKQTALQEIsravinydlmKLLSSLKNPYIVHYEDSW------------------ 95
Cdd:cd14049   23 YKVRNKLDGQYYAIKKILIKKVTKRDCMKVLREV----------KVLAGLQHPNIVGYHTAWmehvqlmlyiqmqlcels 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  96 ----IDNDNNACIFTAYyeggnmanaiKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLP-KDDHVQL 170
Cdd:cd14049   93 lwdwIVERNKRPCEEEF----------KSAPYTPVDVDVTTKILQQLLEGVTYIHSMGIVHRDLKPRNIFLHgSDIHVRI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 171 GNYGLA-KLI----------NPEKPVSMVSGISNSM--CPEVLEDQPYGYKSDIWSLGCCMYEItaHQPAFKAPDMAGLI 237
Cdd:cd14049  163 GDFGLAcPDIlqdgndsttmSRLNGLTHTSGVGTCLyaAPEQLEGSHYDFKSDMYSIGVILLEL--FQPFGTEMERAEVL 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 334185276 238 N-----KINRSLMSPLPIvysstLKQMIKLMLRKKPEYRPTACELL 278
Cdd:cd14049  241 TqlrngQIPKSLCKRWPV-----QAKYIKLLTSTEPSERPSASQLL 281
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
59-283 2.15e-16

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


Pssm-ID: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 79.45  E-value: 2.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  59 LKQTALQEISRAVINYDLMKLLSSLKNPYIVHYEDsWIDNDNNACIFTAYYEGGNMANAI-KKARGKLFPEERIFkwlAQ 137
Cdd:cd14076   39 IRRDTQQENCQTSKIMREINILKGLTHPNIVRLLD-VLKTKKYIGIVLEFVSGGELFDYIlARRRLKDSVACRLF---AQ 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 138 LLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPvSMVSGISNSMC---PE-VLEDQPY-GYKSDIW 212
Cdd:cd14076  115 LISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANTFDHFNG-DLMSTSCGSPCyaaPElVVSDSMYaGRKADIW 193
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334185276 213 SLGCCMYEITA-HQPAFKAPD--MAGLINKINRSLMS-PL--PIVYSSTLKQMIKLMLRKKPEYRPTACELLRNPSL 283
Cdd:cd14076  194 SCGVILYAMLAgYLPFDDDPHnpNGDNVPRLYRYICNtPLifPEYVTPKARDLLRRILVPNPRKRIRLSAIMRHAWL 270
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
78-271 2.17e-16

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: 80.48  E-value: 2.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  78 KLLSSLKNPYIVHYEDSWIDNDNnACIFTAYYEGGNMANAIKKARgkLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTC 157
Cdd:cd05571   47 RVLQNTRHPFLTSLKYSFQTNDR-LCFVMEYVNGGELFFHLSRER--VFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKL 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 158 SNIFLPKDDHVQLGNYGLAKL-INPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGL 236
Cdd:cd05571  124 ENLLLDKDGHIKITDFGLCKEeISYGATTKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVL 203
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 334185276 237 INKInrsLMSPL--PIVYSSTLKQMIKLMLRKKPEYR 271
Cdd:cd05571  204 FELI---LMEEVrfPSTLSPEAKSLLAGLLKKDPKKR 237
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
45-271 2.42e-16

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: 80.14  E-value: 2.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  45 YAMKkiCLAKHTDKLKQTALQEISRavinydlmKLLSSLKNPYIV--HYEdswIDNDNNACIFTAYYEGGNMANAIKKAr 122
Cdd:cd05582   26 YAMK--VLKKATLKVRDRVRTKMER--------DILADVNHPFIVklHYA---FQTEGKLYLILDFLRGGDLFTRLSKE- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 123 gKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAK-LINPEKPVSMVSGISNSMCPEVLE 201
Cdd:cd05582   92 -VMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKeSIDHEKKAYSFCGTVEYMAPEVVN 170
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334185276 202 DQPYGYKSDIWSLGCCMYE-ITAHQPaFKAPDMAGLINKINRSLMSpLPIVYSSTLKQMIKLMLRKKPEYR 271
Cdd:cd05582  171 RRGHTQSADWWSFGVLMFEmLTGSLP-FQGKDRKETMTMILKAKLG-MPQFLSPEAQSLLRALFKRNPANR 239
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
39-273 2.94e-16

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: 78.84  E-value: 2.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  39 DIEDKKYAMKKIclakHTDKLK-QTALQEISRAVinydlmKLLSSLKNPYIVHYEDSWiDNDNNACIFTAYYEGGNMANA 117
Cdd:cd14161   24 DSSGRLVAIKSI----RKDRIKdEQDLLHIRREI------EIMSSLNHPHIISVYEVF-ENSSKIVIVMEYASRGDLYDY 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 118 IKKARGKLFPEERIFkwLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNSMCP 197
Cdd:cd14161   93 ISERQRLSELEARHF--FRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSNLYNQDKFLQTYCGSPLYASP 170
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334185276 198 EVLEDQPY-GYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKI-NRSLMSPlpiVYSSTLKQMIKLMLRKKPEYRPT 273
Cdd:cd14161  171 EIVNGRPYiGPEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQIsSGAYREP---TKPSDACGLIRWLLMVNPERRAT 245
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
38-281 3.33e-16

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: 78.59  E-value: 3.33e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  38 HDIEDKKYAMKKIclakhtDK--LKQTALQEISRAVinyDLMKLLSslkNPYIVH-YEdsWIDNDNNACIFTAYYEGGNM 114
Cdd:cd14071   21 HRITKTEVAIKII------DKsqLDEENLKKIYREV---QIMKMLN---HPHIIKlYQ--VMETKDMLYLVTEYASNGEI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 115 ANAIKKaRGKLfPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNS 194
Cdd:cd14071   87 FDYLAQ-HGRM-SEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSNFFKPGELLKTWCGSPPY 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 195 MCPEVLEDQPY-GYKSDIWSLGCCMYEITAHQPAFKAPDMAGLinkINRSLMSPLPIVY--SSTLKQMIKLMLRKKPEYR 271
Cdd:cd14071  165 AAPEVFEGKEYeGPQLDIWSLGVVLYVLVCGALPFDGSTLQTL---RDRVLSGRFRIPFfmSTDCEHLIRRMLVLDPSKR 241
                        250
                 ....*....|
gi 334185276 272 PTACELLRNP 281
Cdd:cd14071  242 LTIEQIKKHK 251
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
46-302 3.64e-16

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: 79.72  E-value: 3.64e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  46 AMKKICLAKHTDKLKQTALQEISravinydlmkLLSSLKNPYIVHYEDSWIDNDNNACIFTAYYEGGNMANAIKKARGKl 125
Cdd:cd07845   36 ALKKVRMDNERDGIPISSLREIT----------LLLNLRHPNIVELKEVVVGKHLDSIFLVMEYCEQDLASLLDNMPTP- 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 126 FPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLI-NPEKPVS--MVSGISNSmcPEVL-E 201
Cdd:cd07845  105 FSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLARTYgLPAKPMTpkVVTLWYRA--PELLlG 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 202 DQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSP----------LPIVYSSTLKQ------------- 258
Cdd:cd07845  183 CTTYTTAIDMWAVGCILAELLAHKPLLPGKSEIEQLDLIIQLLGTPnesiwpgfsdLPLVGKFTLPKqpynnlkhkfpwl 262
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 334185276 259 ------MIKLMLRKKPEYRPTACELLRNPSLQPYLLQCQnlsPIYLPVFP 302
Cdd:cd07845  263 seaglrLLNFLLMYDPKKRATAEEALESSYFKEKPLPCE---PEMMPTFP 309
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
77-271 4.37e-16

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: 78.51  E-value: 4.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  77 MKLLSSLKNPYIVHYEDSWiDNDNNACIFTAYYEGGNMANAIKkARGKLfPEERIFKWLAQLLLAVNYLHSNRVVHMDLT 156
Cdd:cd14201   56 IKILKELQHENIVALYDVQ-EMPNSVFLVMEYCNGGDLADYLQ-AKGTL-SEDTIRVFLQQIAAAMRILHSKGIIHRDLK 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 157 CSNIFLPKDDH---------VQLGNYGLAKLINPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPA 227
Cdd:cd14201  133 PQNILLSYASRkkssvsgirIKIADFGFARYLQSNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPP 212
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 334185276 228 FKA--PDMAGLINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYR 271
Cdd:cd14201  213 FQAnsPQDLRMFYEKNKNLQPSIPRETSPYLADLLLGLLQRNQKDR 258
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
24-264 6.25e-16

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: 79.28  E-value: 6.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  24 QVRRGKSSSDFvvlhdiedkkYAMKKIclaKHTDKLKQ--TALQEISRavinyDLMKLLSSlknPYI--VHYedSWIDND 99
Cdd:cd05601   18 QVVKEKATGDI----------YAMKVL---KKSETLAQeeVSFFEEER-----DIMAKANS---PWItkLQY--AFQDSE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 100 NNACIFTaYYEGGNMANAIKKaRGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLI 179
Cdd:cd05601   75 NLYLVME-YHPGGDLLSLLSR-YDDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSAAKL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 180 NPEKPVS--MVSGISNSMCPEVLE------DQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKI---NRSLMSPL 248
Cdd:cd05601  153 SSDKTVTskMPVGTPDYIAPEVLTsmnggsKGTYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNImnfKKFLKFPE 232
                        250
                 ....*....|....*.
gi 334185276 249 PIVYSSTLKQMIKLML 264
Cdd:cd05601  233 DPKVSESAVDLIKGLL 248
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
50-283 6.48e-16

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: 78.53  E-value: 6.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  50 ICLA--KHTDKL---KQTALQEISRAVINYDLMKLLSSLKNPYIVHYEDSWIDNDNnACIFTAYYEGGNMANAIKKARgk 124
Cdd:cd06657   36 VCIAtvKSSGKLvavKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDE-LWVVMEFLEGGALTDIVTHTR-- 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 125 lFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKP-VSMVSGISNSMCPEVLEDQ 203
Cdd:cd06657  113 -MNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPrRKSLVGTPYWMAPELISRL 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 204 PYGYKSDIWSLGCCMYE-ITAHQPAFKAPDMAGLinKINRSLMSP-LPIVY--SSTLKQMIKLMLRKKPEYRPTACELLR 279
Cdd:cd06657  192 PYGPEVDIWSLGIMVIEmVDGEPPYFNEPPLKAM--KMIRDNLPPkLKNLHkvSPSLKGFLDRLLVRDPAQRATAAELLK 269

                 ....
gi 334185276 280 NPSL 283
Cdd:cd06657  270 HPFL 273
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
40-281 6.81e-16

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: 77.76  E-value: 6.81e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  40 IEDKKYAMKKICLAKHTDKlkQTALQEISRA-------VINYDLmKLLSSLKNPYIVHYEDSwIDNDNNACIFTAYYEGG 112
Cdd:cd14184    9 IGDGNFAVVKECVERSTGK--EFALKIIDKAkccgkehLIENEV-SILRRVKHPNIIMLIEE-MDTPAELYLVMELVKGG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 113 NMANAIKKARGklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFL----PKDDHVQLGNYGLAKLInpEKPVSMV 188
Cdd:cd14184   85 DLFDAITSSTK--YTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVceypDGTKSLKLGDFGLATVV--EGPLYTV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 189 SGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPD--MAGLINKI---NRSLMSPLPIVYSSTLKQMIKLM 263
Cdd:cd14184  161 CGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSENnlQEDLFDQIllgKLEFPSPYWDNITDSAKELISHM 240
                        250
                 ....*....|....*...
gi 334185276 264 LRKKPEYRPTACELLRNP 281
Cdd:cd14184  241 LQVNVEARYTAEQILSHP 258
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
60-281 7.30e-16

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: 78.05  E-value: 7.30e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  60 KQTALQEI-SRAVINYdlmkllsslkNPYIVHYEDSWIDNDNnACIFTAYYEGGNMANAI--KKARGKLFPEERIFKWLA 136
Cdd:cd14139   43 EQLALHEVyAHAVLGH----------HPHVVRYYSAWAEDDH-MIIQNEYCNGGSLQDAIseNTKSGNHFEEPELKDILL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 137 QLLLAVNYLHSNRVVHMDLTCSNIF----------------------LPKDDHVQLGNYGLAKLINPEKpvsMVSGISNS 194
Cdd:cd14139  112 QVSMGLKYIHNSGLVHLDIKPSNIFichkmqsssgvgeevsneedefLSANVVYKIGDLGHVTSINKPQ---VEEGDSRF 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 195 MCPEVL-EDQPYGYKSDIWSLGCCMYEITAHQPafkAPDMAGLINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPT 273
Cdd:cd14139  189 LANEILqEDYRHLPKADIFALGLTVALAAGAEP---LPTNGAAWHHIRKGNFPDVPQELPESFSSLLKNMIQPDPEQRPS 265

                 ....*...
gi 334185276 274 ACELLRNP 281
Cdd:cd14139  266 ATALARHT 273
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
104-278 8.89e-16

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: 77.79  E-value: 8.89e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 104 IFTAYYEGGNMANAIKKARGKlFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEK 183
Cdd:cd14151   80 IVTQWCEGSSLYHHLHIIETK-FEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWS 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 184 PVSMVSGISNS---MCPEVLEDQ---PYGYKSDIWSLGCCMYEITAHQ-PAFKAPDMAGLINKINRSLMSP-LPIVYSST 255
Cdd:cd14151  159 GSHQFEQLSGSilwMAPEVIRMQdknPYSFQSDVYAFGIVLYELMTGQlPYSNINNRDQIIFMVGRGYLSPdLSKVRSNC 238
                        170       180
                 ....*....|....*....|....*.
gi 334185276 256 LKQMIKLM---LRKKPEYRPTACELL 278
Cdd:cd14151  239 PKAMKRLMaecLKKKRDERPLFPQIL 264
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
17-281 1.17e-15

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


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 77.37  E-value: 1.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  17 DNYHVVEQVRRGKsssdFVVLHDIEDK----KYAMKKICLAKHTDKLKQTALQEISRAVinydlmKLLSSLKNPYIVHYE 92
Cdd:cd14194    5 DYYDTGEELGSGQ----FAVVKKCREKstglQYAAKFIKKRRTKSSRRGVSREDIEREV------SILKEIQHPNVITLH 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  93 DSWiDNDNNACIFTAYYEGGNMANAIkkARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFL-----PKdDH 167
Cdd:cd14194   75 EVY-ENKTDVILILELVAGGELFDFL--AEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLldrnvPK-PR 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 168 VQLGNYGLAKLINPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAF----KAPDMAGlINKINRS 243
Cdd:cd14194  151 IKIIDFGLAHKIDFGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFlgdtKQETLAN-VSAVNYE 229
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 334185276 244 LMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd14194  230 FEDEYFSNTSALAKDFIRRLLVKDPKKRMTIQDSLQHP 267
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
46-281 1.38e-15

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: 77.36  E-value: 1.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  46 AMKKICLAKHTDKLKQTALQEIsravinydlmKLLSSLKNPYIVHYEDSWIDNDNNACIFTayYEGGNMANAIKKARGKL 125
Cdd:cd07833   30 AIKKFKESEDDEDVKKTALREV----------KVLRQLRHENIVNLKEAFRRKGRLYLVFE--YVERTLLELLEASPGGL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 126 fPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNS--MCPEVL-ED 202
Cdd:cd07833   98 -PPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARALTARPASPLTDYVATRwyRAPELLvGD 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 203 QPYGYKSDIWSLGCCMYEITAHQPAF----------------------------KAPDMAGLInKINRSLMSPL----PI 250
Cdd:cd07833  177 TNYGKPVDVWAIGCIMAELLDGEPLFpgdsdidqlyliqkclgplppshqelfsSNPRFAGVA-FPEPSQPESLerryPG 255
                        250       260       270
                 ....*....|....*....|....*....|.
gi 334185276 251 VYSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd07833  256 KVSSPALDFLKACLRMDPKERLTCDELLQHP 286
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
61-279 1.45e-15

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: 77.17  E-value: 1.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  61 QTALQEISRAVINYDLMKLLSSLKNPYIVHY-----EDSWIDndnnacIFTAYYEGGNMANAIKKaRGKLfPEERIFKWL 135
Cdd:cd13991   33 QCAVKKVRLEVFRAEELMACAGLTSPRVVPLygavrEGPWVN------IFMDLKEGGSLGQLIKE-QGCL-PEDRALHYL 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 136 AQLLLAVNYLHSNRVVHMDLTCSNIFLPKD-DHVQLGNYGLAKLINPE---KPV---SMVSGISNSMCPEVLEDQPYGYK 208
Cdd:cd13991  105 GQALEGLEYLHSRKILHGDVKADNVLLSSDgSDAFLCDFGHAECLDPDglgKSLftgDYIPGTETHMAPEVVLGKPCDAK 184
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185276 209 SDIWSlGCCM--YEITAHQP---AFKAPdmagLINKInRSLMSPL---PIVYSSTLKQMIKLMLRKKPEYRPTACELLR 279
Cdd:cd13991  185 VDVWS-SCCMmlHMLNGCHPwtqYYSGP----LCLKI-ANEPPPLreiPPSCAPLTAQAIQAGLRKEPVHRASAAELRR 257
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
38-305 1.48e-15

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: 77.35  E-value: 1.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  38 HDiEDKKYAMKKICLAKHTDKLKQTALQEISRAVINYdlmkllsSLKNPYIV--HYEdswIDNDNNACIFTAYYEGGNM- 114
Cdd:cd05613   25 HD-AGKLYAMKVLKKATIVQKAKTAEHTRTERQVLEH-------IRQSPFLVtlHYA---FQTDTKLHLILDYINGGELf 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 115 ANAIKKARgklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAK--LINPEKPVSMVSGIS 192
Cdd:cd05613   94 THLSQRER---FTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKefLLDENERAYSFCGTI 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 193 NSMCPEVLEDQPYGYKS--DIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMS---PLPIVYSSTLKQMIKLMLRKK 267
Cdd:cd05613  171 EYMAPEIVRGGDSGHDKavDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKsepPYPQEMSALAKDIIQRLLMKD 250
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 334185276 268 PEYR----PTAC-ELLRNPSLQPylLQCQNLSPIYLPVfPIKP 305
Cdd:cd05613  251 PKKRlgcgPNGAdEIKKHPFFQK--INWDDLAAKKVPA-PFKP 290
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
46-249 1.51e-15

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: 77.34  E-value: 1.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  46 AMKKICLAKHTDKLKQTALQEisravinydlMKLLSSLKNPYIVHYEDSWIDNDNNACIFTayYEGGNMANAIKKARGKL 125
Cdd:cd07848   30 AIKKFKDSEENEEVKETTLRE----------LKMLRTLKQENIVELKEAFRRRGKLYLVFE--YVEKNMLELLEEMPNGV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 126 FPEeRIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNS--MCPEVLEDQ 203
Cdd:cd07848   98 PPE-KVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLSEGSNANYTEYVATRwyRSPELLLGA 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 334185276 204 PYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRsLMSPLP 249
Cdd:cd07848  177 PYGKAVDMWSVGCILGELSDGQPLFPGESEIDQLFTIQK-VLGPLP 221
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
38-283 1.55e-15

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: 76.68  E-value: 1.55e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  38 HDIEDKKYAMKKIclakhtDKLKqtaLQEISRAVINYDL--MKLLSslkNPYIVH-YEdsWIDNDNNACIFTAYYEGGNM 114
Cdd:cd14074   24 HVFTGEKVAVKVI------DKTK---LDDVSKAHLFQEVrcMKLVQ---HPNVVRlYE--VIDTQTKLYLILELGDGGDM 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 115 ANAIKKARGKLfPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSN-IFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISN 193
Cdd:cd14074   90 YDYIMKHENGL-NEDLARKYFRQIVSAISYCHKLHVVHRDLKPENvVFFEKQGLVKLTDFGFSNKFQPGEKLETSCGSLA 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 194 SMCPEVLEDQPY-GYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSpLPIVYSSTLKQMIKLMLRKKPEYRP 272
Cdd:cd14074  169 YSAPEILLGDEYdAPAVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCKYT-VPAHVSPECKDLIRRMLIRDPKKRA 247
                        250
                 ....*....|.
gi 334185276 273 TACELLRNPSL 283
Cdd:cd14074  248 SLEEIENHPWL 258
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
43-271 1.73e-15

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: 76.66  E-value: 1.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  43 KKYAMKKICLAKHTDKLKQTALQEISRAVinydlmkLLSSLKNPYIV--HYEdswIDNDNNACIFTAYYEGGNMANAIKK 120
Cdd:cd05583   23 KLYAMKVLKKATIVQKAKTAEHTMTERQV-------LEAVRQSPFLVtlHYA---FQTDAKLHLILDYVNGGELFTHLYQ 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 121 aRGKlFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVS--GISNSMCPE 198
Cdd:cd05583   93 -REH-FTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKEFLPGENDRAYSfcGTIEYMAPE 170
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334185276 199 VLEDQPYGYKS--DIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMS---PLPIVYSSTLKQMIKLMLRKKPEYR 271
Cdd:cd05583  171 VVRGGSDGHDKavDWWSLGVLTYELLTGASPFTVDGERNSQSEISKRILKshpPIPKTFSAEAKDFILKLLEKDPKKR 248
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
40-281 1.87e-15

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: 76.57  E-value: 1.87e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  40 IEDKKYAMKKICLAKHTDKlkQTALQEISRAVIN------YDLMKLLSSLKNPYIVHYEDSwIDNDNNACIFTAYYEGGN 113
Cdd:cd14183   14 IGDGNFAVVKECVERSTGR--EYALKIINKSKCRgkehmiQNEVSILRRVKHPNIVLLIEE-MDMPTELYLVMELVKGGD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 114 MANAIKKARGklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPK----DDHVQLGNYGLAKLInpEKPVSMVS 189
Cdd:cd14183   91 LFDAITSTNK--YTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEhqdgSKSLKLGDFGLATVV--DGPLYTVC 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 190 GISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAP--DMAGLINKInrsLMSPL--PIVY----SSTLKQMIK 261
Cdd:cd14183  167 GTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGSgdDQEVLFDQI---LMGQVdfPSPYwdnvSDSAKELIT 243
                        250       260
                 ....*....|....*....|
gi 334185276 262 LMLRKKPEYRPTACELLRNP 281
Cdd:cd14183  244 MMLQVDVDQRYSALQVLEHP 263
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
62-274 2.27e-15

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: 76.75  E-value: 2.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  62 TALQEISravinydLMKllsSLKNPYIVHYEDSwIDNDNNACIFTAYyeggnMANAIKK------ARGKLFPEE-RIFKW 134
Cdd:cd07836   44 TAIREIS-------LMK---ELKHENIVRLHDV-IHTENKLMLVFEY-----MDKDLKKymdthgVRGALDPNTvKSFTY 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 135 laQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINpeKPVSMVSGISNSM---CPEVL-EDQPYGYKSD 210
Cdd:cd07836  108 --QLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARAFG--IPVNTFSNEVVTLwyrAPDVLlGSRTYSTSID 183
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334185276 211 IWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPlpivYSSTLKQMIKLmlrkkPEYRPTA 274
Cdd:cd07836  184 IWSVGCIMAEMITGRPLFPGTNNEDQLLKIFRIMGTP----TESTWPGISQL-----PEYKPTF 238
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
18-280 2.28e-15

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: 76.23  E-value: 2.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  18 NYHVVEQVrrGKSSSDFVVL-HDIEDK-KYAMKkiCLAKHT-------DKLKQTALQEIsravinyDLMKLLSSlkNPYI 88
Cdd:cd13993    1 RYQLISPI--GEGAYGVVYLaVDLRTGrKYAIK--CLYKSGpnskdgnDFQKLPQLREI-------DLHRRVSR--HPNI 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  89 VHYEDSWidnDNNACIFTA--YYEGGNMANAIK-KARGKLFPE--ERIFKwlaQLLLAVNYLHSNRVVHMDLTCSNIFLP 163
Cdd:cd13993   68 ITLHDVF---ETEVAIYIVleYCPNGDLFEAITeNRIYVGKTEliKNVFL---QLIDAVKHCHSLGIYHRDIKPENILLS 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 164 KDD-HVQLGNYGLAKlinpEKPVSMVSGISNS--MCPEVLEDQPYGYKS------DIWSLGCCMYEITAHQPAFKAPDMA 234
Cdd:cd13993  142 QDEgTVKLCDFGLAT----TEKISMDFGVGSEfyMAPECFDEVGRSLKGypcaagDIWSLGIILLNLTFGRNPWKIASES 217
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 334185276 235 gliNKINRSLMSPLPIVY------SSTLKQMIKLMLRKKPEYRPTACELLRN 280
Cdd:cd13993  218 ---DPIFYDYYLNSPNLFdvilpmSDDFYNLLRQIFTVNPNNRILLPELQLL 266
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
136-280 2.48e-15

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: 76.05  E-value: 2.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 136 AQLLLAVNYLHSNRVVHMDLTCSNIFL-PKDDHVQLGNYGLAKLINPEKPVSMV-SGISNSMCPEVLEDQPYGYKS-DIW 212
Cdd:cd14164  107 AQMVGAVNYLHDMNIVHRDLKCENILLsADDRKIKIADFGFARFVEDYPELSTTfCGSRAYTPPEVILGTPYDPKKyDVW 186
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185276 213 SLGCCMYE-ITAHQPAFKapDMAGLINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRN 280
Cdd:cd14164  187 SLGVVLYVmVTGTMPFDE--TNVRRLRLQQRGVLYPSGVALEEPCRALIRTLLQFNPSTRPSIQQVAGN 253
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
126-283 2.61e-15

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: 76.01  E-value: 2.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 126 FPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPE--KPVSMVSGISNSMCPEVLEDQ 203
Cdd:cd14111   96 YSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSAQSFNPLslRQLGRRTGTLEYMAPEMVKGE 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 204 PYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPL---PIVySSTLKQMIKLMLRKKPEYRPTACELLRN 280
Cdd:cd14111  176 PVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKILVAKFDAFklyPNV-SQSASLFLKKVLSSYPWSRPTTKDCFAH 254

                 ...
gi 334185276 281 PSL 283
Cdd:cd14111  255 AWL 257
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
126-271 2.62e-15

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: 76.77  E-value: 2.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 126 FPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISN--SMCPE-VLED 202
Cdd:cd07864  113 FSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADFGLARLYNSEESRPYTNKVITlwYRPPElLLGE 192
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185276 203 QPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYR 271
Cdd:cd07864  193 ERYGPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRLCGSPCPAVWPDVIKLPYFNTMKPKKQYR 261
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
49-281 2.83e-15

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: 75.77  E-value: 2.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  49 KICLAKHTDKLKQTALQEISRAVI-NYDL-------MKLLSSLKNPYIVH-YEdsWIDNDNNACIFTAYYEGGNMANAIK 119
Cdd:cd14079   17 KVKLAEHELTGHKVAVKILNRQKIkSLDMeekirreIQILKLFRHPHIIRlYE--VIETPTDIFMVMEYVSGGELFDYIV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 120 KaRGKLFPEE--RIFKwlaQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNSMCP 197
Cdd:cd14079   95 Q-KGRLSEDEarRFFQ---QIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLSNIMRDGEFLKTSCGSPNYAAP 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 198 EVLEDQPY-GYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKInRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACE 276
Cdd:cd14079  171 EVISGKLYaGPEVDVWSCGVILYALLCGSLPFDDEHIPNLFKKI-KSGIYTIPSHLSPGARDLIKRMLVVDPLKRITIPE 249

                 ....*
gi 334185276 277 LLRNP 281
Cdd:cd14079  250 IRQHP 254
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
22-281 3.31e-15

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 77.17  E-value: 3.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  22 VEQVRR---GKSSSDFVVLHDIEDKKYAMKKIcLAKHTDKLKQTALQEISravinydlmkLLSSLKNPYIVHYEDSWiDN 98
Cdd:PLN00034  76 LERVNRigsGAGGTVYKVIHRPTGRLYALKVI-YGNHEDTVRRQICREIE----------ILRDVNHPNVVKCHDMF-DH 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  99 DNNACIFTAYYEGGNManaikkaRGKLFPEERIFKWLA-QLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAK 177
Cdd:PLN00034 144 NGEIQVLLEFMDGGSL-------EGTHIADEQFLADVArQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSR 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 178 LINPE-KPVSMVSGISNSMCPEV----LEDQPY-GYKSDIWSLGCCMYEITAHQPAF---KAPDMAGLINKINRSLMSPL 248
Cdd:PLN00034 217 ILAQTmDPCNSSVGTIAYMSPERintdLNHGAYdGYAGDIWSLGVSILEFYLGRFPFgvgRQGDWASLMCAICMSQPPEA 296
                        250       260       270
                 ....*....|....*....|....*....|...
gi 334185276 249 PIVYSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:PLN00034 297 PATASREFRHFISCCLQREPAKRWSAMQLLQHP 329
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
126-281 3.46e-15

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: 76.14  E-value: 3.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 126 FPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLA-KLINPEKPVSMVSGISNSMCPEVLEDQP 204
Cdd:cd14200  121 FSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDDGHVKIADFGVSnQFEGNDALLSSTAGTPAFMAPETLSDSG 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 205 YGYKS---DIWSLGCCMYEITAHQPAFKAPDMAGLINKI-NRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRN 280
Cdd:cd14200  201 QSFSGkalDVWAMGVTLYCFVYGKCPFIDEFILALHNKIkNKPVEFPEEPEISEELKDLILKMLDKNPETRITVPEIKVH 280

                 .
gi 334185276 281 P 281
Cdd:cd14200  281 P 281
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
126-279 3.58e-15

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: 76.07  E-value: 3.58e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 126 FPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLA-KLINPEKPVSMVSGISNSMCPEVLEDQP 204
Cdd:cd05608  102 FQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAvELKDGQTKTKGYAGTPGFMAPELLLGEE 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 205 YGYKSDIWSLGCCMYEITAHQPAFKAPDmAGLINK--INRSLMSPL--PIVYSSTLKQMIKLMLRKKPE----YRPTACE 276
Cdd:cd05608  182 YDYSVDYFTLGVTLYEMIAARGPFRARG-EKVENKelKQRILNDSVtySEKFSPASKSICEALLAKDPEkrlgFRDGNCD 260

                 ...
gi 334185276 277 LLR 279
Cdd:cd05608  261 GLR 263
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
84-341 4.09e-15

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


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 76.52  E-value: 4.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  84 KNPYIVHYEDSWIDNDNNACIFTaYYEGGNMANAIK-KARGKLFpeeRIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFL 162
Cdd:cd05620   54 ENPFLTHLYCTFQTKEHLFFVME-FLNGGDLMFHIQdKGRFDLY---RATFYAAEIVCGLQFLHSKGIIYRDLKLDNVML 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 163 PKDDHVQLGNYGLAKL-INPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKIn 241
Cdd:cd05620  130 DRDGHIKIADFGMCKEnVFGDNRASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESI- 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 242 RSLMSPLPIVYSSTLKQMIKLMLRKKPEYRptaCELLRNPSLQPY-------LLQCQNLSPiylpvfPIKP-VNSPKDKA 313
Cdd:cd05620  209 RVDTPHYPRWITKESKDILEKLFERDPTRR---LGVVGNIRGHPFfktinwtALEKRELDP------PFKPkVKSPSDYS 279
                        250       260
                 ....*....|....*....|....*...
gi 334185276 314 rrnslpgKFGKERVSrEKSEVSRSLENL 341
Cdd:cd05620  280 -------NFDREFLS-EKPRLSYSDKNL 299
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
77-283 4.20e-15

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


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 75.41  E-value: 4.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  77 MKLLSSLKNPYIVHYEDSWIDNDNNACIFTAYYEGGNMANAIkkARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLT 156
Cdd:cd14163   51 LQIVERLDHKNIIHVYEMLESADGKIYLVMELAEDGDVFDCV--LHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLK 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 157 CSNIFLPKDDhVQLGNYGLAKLInpekPVSMVSgISNSMC-------PEVLEDQPY-GYKSDIWSLGCCMYEITAHQPAF 228
Cdd:cd14163  129 CENALLQGFT-LKLTDFGFAKQL----PKGGRE-LSQTFCgstayaaPEVLQGVPHdSRKGDIWSMGVVLYVMLCAQLPF 202
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 334185276 229 KAPDMAGLINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRNPSL 283
Cdd:cd14163  203 DDTDIPKMLCQQQKGVSLPGHLGVSRTCQDLLKRLLEPDMVLRPSIEEVSWHPWL 257
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
17-281 4.44e-15

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: 75.76  E-value: 4.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  17 DNYHVVEQVRRGKsssdFVVLHDIEDKK----YAMKKICLAKHTDKLKQTALQEISRAVinydlmKLLSSLKNPYIVHYE 92
Cdd:cd14196    5 DFYDIGEELGSGQ----FAIVKKCREKStgleYAAKFIKKRQSRASRRGVSREEIEREV------SILRQVLHPNIITLH 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  93 DSWiDNDNNACIFTAYYEGGNMANAIkkARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDD----HV 168
Cdd:cd14196   75 DVY-ENRTDVVLILELVSGGELFDFL--AQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHI 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 169 QLGNYGLAKLINPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAF---KAPDMAGLINKINRSLM 245
Cdd:cd14196  152 KLIDFGLAHEIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFlgdTKQETLANITAVSYDFD 231
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 334185276 246 SPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd14196  232 EEFFSHTSELAKDFIRKLLVKETRKRLTIQEALRHP 267
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
19-247 5.65e-15

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: 75.40  E-value: 5.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  19 YHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAKHTDKLKQTALQEISravinydlmkLLSSLKNPYIVHYEDSWIDN 98
Cdd:cd07835    1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKIRLETEDEGVPSTAIREIS----------LLKELNHPNIVRLLDVVHSE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  99 DNNACIFTayYEGGNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKL 178
Cdd:cd07835   71 NKLYLVFE--FLDLDLKKYMDSSPLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLARA 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334185276 179 INpeKPV-----SMVSGISNSmcPEVLEDQP-YGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSP 247
Cdd:cd07835  149 FG--VPVrtythEVVTLWYRA--PEILLGSKhYSTPVDIWSVGCIFAEMVTRRPLFPGDSEIDQLFRIFRTLGTP 219
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
35-281 5.80e-15

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: 75.10  E-value: 5.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  35 VVLhdIEDKK----YAMKkiCLAKHTDKLKQTALQ-EIsravinydlmKLLSSLKNPYIVHYEDSWidnDNNACIFTAY- 108
Cdd:cd14083   19 VVL--AEDKAtgklVAIK--CIDKKALKGKEDSLEnEI----------AVLRKIKHPNIVQLLDIY---ESKSHLYLVMe 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 109 -YEGGNMANAIKkARGKlFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNI--FLPKDD-HVQLGNYGLAKLINPEKp 184
Cdd:cd14083   82 lVTGGELFDRIV-EKGS-YTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLlyYSPDEDsKIMISDFGLSKMEDSGV- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 185 VSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRS---LMSPLPIVYSSTLKQMIK 261
Cdd:cd14083  159 MSTACGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILKAeyeFDSPYWDDISDSAKDFIR 238
                        250       260
                 ....*....|....*....|
gi 334185276 262 LMLRKKPEYRPTACELLRNP 281
Cdd:cd14083  239 HLMEKDPNKRYTCEQALEHP 258
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
19-281 6.28e-15

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: 75.31  E-value: 6.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  19 YHVVEQVRRGKSSSDFVVLHDIEDKKYAMKkiCLAKHTDKLKQTALQ-EISravinydlmkLLSSLKNPYIVHYEDSWiD 97
Cdd:cd14169    5 YELKEKLGEGAFSEVVLAQERGSQRLVALK--CIPKKALRGKEAMVEnEIA----------VLRRINHENIVSLEDIY-E 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  98 NDNNACIFTAYYEGGNMANAIKKaRGKlFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLP---KDDHVQLGNYG 174
Cdd:cd14169   72 SPTHLYLAMELVTGGELFDRIIE-RGS-YTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYAtpfEDSKIMISDFG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 175 LAKlINPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAF---KAPDMAGLINKINRSLMSPLPIV 251
Cdd:cd14169  150 LSK-IEAQGMLSTACGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFydeNDSELFNQILKAEYEFDSPYWDD 228
                        250       260       270
                 ....*....|....*....|....*....|
gi 334185276 252 YSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd14169  229 ISESAKDFIRHLLERDPEKRFTCEQALQHP 258
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
17-248 6.32e-15

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: 76.23  E-value: 6.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  17 DNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKicLAKHtDKLK--QTALQEISRAVINYDLMKLLSSLknpyivHYEds 94
Cdd:cd05597    1 DDFEILKVIGRGAFGEVAVVKLKSTEKVYAMKI--LNKW-EMLKraETACFREERDVLVNGDRRWITKL------HYA-- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  95 wIDNDNNACIFTAYYEGGNMANAIKKARGKLfPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYG 174
Cdd:cd05597   70 -FQDENYLYLVMDYYCGGDLLTLLSKFEDRL-PEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFG 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 175 -LAKLINPEKPVSMVS-GISNSMCPEVL---EDQ--PYGYKSDIWSLGCCMYE-------------------ITAHQPAF 228
Cdd:cd05597  148 sCLKLREDGTVQSSVAvGTPDYISPEILqamEDGkgRYGPECDWWSLGVCMYEmlygetpfyaeslvetygkIMNHKEHF 227
                        250       260
                 ....*....|....*....|
gi 334185276 229 KAPDMAGLINKINRSLMSPL 248
Cdd:cd05597  228 SFPDDEDDVSEEAKDLIRRL 247
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
43-271 6.59e-15

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: 75.41  E-value: 6.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  43 KKYAMKKIcLAKHTDKLKQTALQEISRAVINYDLMKLLSSLKNPYivhyedswiDNDNNACIFTAYYEGGNMANAIKKAR 122
Cdd:cd05631   26 KMYACKKL-EKKRIKKRKGEAMALNEKRILEKVNSRFVVSLAYAY---------ETKDALCLVLTIMNGGDLKFHIYNMG 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 123 GKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNSMCPEVLED 202
Cdd:cd05631   96 NPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQIPEGETVRGRVGTVGYMAPEVINN 175
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334185276 203 QPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSL---MSPLPIVYSSTLKQMIKLMLRKKPEYR 271
Cdd:cd05631  176 EKYTFSPDWWGLGCLIYEMIQGQSPFRKRKERVKREEVDRRVkedQEEYSEKFSEDAKSICRMLLTKNPKER 247
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
17-280 6.77e-15

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: 75.43  E-value: 6.77e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  17 DNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAKHTDklkqtalQEISravINYDLMKLLSSLKNP---YIVHYED 93
Cdd:cd06638   18 DTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDPIHDID-------EEIE---AEYNILKALSDHPNVvkfYGMYYKK 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  94 SwIDNDNNACIFTAYYEGGNMANAIKK--ARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLG 171
Cdd:cd06638   88 D-VKNGDQLWLVLELCNGGSVTDLVKGflKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLV 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 172 NYGL-AKLINPEKPVSMVSGISNSMCPEVLE-----DQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLM 245
Cdd:cd06638  167 DFGVsAQLTSTRLRRNTSVGTPFWMAPEVIAceqqlDSTYDARCDVWSLGITAIELGDGDPPLADLHPMRALFKIPRNPP 246
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 334185276 246 SPL--PIVYSSTLKQMIKLMLRKKPEYRPTACELLRN 280
Cdd:cd06638  247 PTLhqPELWSNEFNDFIRKCLTKDYEKRPTVSDLLQH 283
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
78-278 7.74e-15

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


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 75.07  E-value: 7.74e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  78 KLLSSLKNPYIVHYEDSWIDnDNNACIFTAYYEGGNMANAIKKA-------RGKLFPEERIFKWLAQLLLAVNYLHSNRV 150
Cdd:cd14146   45 KLFSMLRHPNIIKLEGVCLE-EPNLCLVMEFARGGTLNRALAAAnaapgprRARRIPPHILVNWAVQIARGMLYLHEEAV 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 151 V---HMDLTCSNIFL-PKDDHVQLGN-------YGLAKLINPEKPVSmVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMY 219
Cdd:cd14146  124 VpilHRDLKSSNILLlEKIEHDDICNktlkitdFGLAREWHRTTKMS-AAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLW 202
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334185276 220 EITAHQPAFKAPDmaGL-------INKinrsLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELL 278
Cdd:cd14146  203 ELLTGEVPYRGID--GLavaygvaVNK----LTLPIPSTCPEPFAKLMKECWEQDPHIRPSFALIL 262
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
108-271 7.81e-15

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: 75.89  E-value: 7.81e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 108 YYEGGNMANAIKKArGKlFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKL-INPEKPVS 186
Cdd:cd05587   78 YVNGGDLMYHIQQV-GK-FKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKEgIFGGKTTR 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 187 MVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSpLPIVYSSTLKQMIKLMLRK 266
Cdd:cd05587  156 TFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVS-YPKSLSKEAVSICKGLLTK 234

                 ....*
gi 334185276 267 KPEYR 271
Cdd:cd05587  235 HPAKR 239
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
50-242 8.02e-15

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: 74.99  E-value: 8.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  50 ICLAKHTDKLKQTALQEISravinyDLMKLLSSLKNPYIVHYEDswIDNDNNACIFTAYYEGGNMANAIKKARGKLFPEe 129
Cdd:cd05111   39 VAIKVIQDRSGRQSFQAVT------DHMLAIGSLDHAYIVRLLG--ICPGASLQLVTQLLPLGSLLDHVRQHRGSLGPQ- 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 130 RIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNS---MCPEVLEDQPYG 206
Cdd:cd05111  110 LLLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLKSPSQVQVADFGVADLLYPDDKKYFYSEAKTPikwMALESIHFGKYT 189
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 334185276 207 YKSDIWSLGCCMYEITAH--QP--AFKAPDMAGLINKINR 242
Cdd:cd05111  190 HQSDVWSYGVTVWEMMTFgaEPyaGMRLAEVPDLLEKGER 229
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
108-271 1.25e-14

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: 75.33  E-value: 1.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 108 YYEGGNMANAIKKARgkLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKL-INPEKPVS 186
Cdd:cd05590   77 FVNGGDLMFHIQKSR--RFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEgIFNGKTTS 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 187 MVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSlmsplPIVYSSTLKQ----MIKL 262
Cdd:cd05590  155 TFCGTPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILND-----EVVYPTWLSQdavdILKA 229

                 ....*....
gi 334185276 263 MLRKKPEYR 271
Cdd:cd05590  230 FMTKNPTMR 238
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
108-235 1.29e-14

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


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 75.15  E-value: 1.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 108 YYEGGNMANAIKKARgKLfPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKL-INPEKPVS 186
Cdd:cd05588   77 FVNGGDLMFHMQRQR-RL-PEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEgLRPGDTTS 154
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 334185276 187 MVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFkapDMAG 235
Cdd:cd05588  155 TFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPF---DIVG 200
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
16-280 1.36e-14

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: 74.53  E-value: 1.36e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  16 LDNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAKHtDKLKQTALQEIsravinydlmKLLSSLKNPYIVHYEDSW 95
Cdd:cd14048    5 LTDFEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRIRLPNN-ELAREKVLREV----------RALAKLDHPGIVRYFNAW 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  96 IDNDNNACI--FTAYYEGGNMANAIKKA-----RGKLFPEERIF----KWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPK 164
Cdd:cd14048   74 LERPPEGWQekMDEVYLYIQMQLCRKENlkdwmNRRCTMESRELfvclNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 165 DDHVQLGNYGLAKLINPEKPVSMVSGISNS-------------MCPEVLEDQPYGYKSDIWSLGCCMYEI-----TAHQP 226
Cdd:cd14048  154 DDVVKVGDFGLVTAMDQGEPEQTVLTPMPAyakhtgqvgtrlyMSPEQIHGNQYSEKVDIFALGLILFELiysfsTQMER 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 334185276 227 AFKAPDMAGLinkinrslmsPLPIVYSSTLKQ---MIKLMLRKKPEYRPTACELLRN 280
Cdd:cd14048  234 IRTLTDVRKL----------KFPALFTNKYPEerdMVQQMLSPSPSERPEAHEVIEH 280
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
42-307 1.41e-14

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: 74.87  E-value: 1.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  42 DKKYAMKKICLAKHTDKLKQTALQEIsravinydlmKLLSSLKNPYIVHYED----SWIDNDNNACIFTAYYEGgNMANA 117
Cdd:cd07834   25 GRKVAIKKISNVFDDLIDAKRILREI----------KILRHLKHENIIGLLDilrpPSPEEFNDVYIVTELMET-DLHKV 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 118 IKkARGKLfPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMvsgisnsM-- 195
Cdd:cd07834   94 IK-SPQPL-TDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGLARGVDPDEDKGF-------Lte 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 196 --------CPEV-LEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSP------------------- 247
Cdd:cd07834  165 yvvtrwyrAPELlLSSKKYTKAIDIWSVGCIFAELLTRKPLFPGRDYIDQLNLIVEVLGTPseedlkfissekarnylks 244
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334185276 248 LPIVYSSTLKQMIKL-----------MLRKKPEYRPTACELLRNPSLQPYllQCQNLSPIYLPVFPIKPVN 307
Cdd:cd07834  245 LPKKPKKPLSEVFPGaspeaidllekMLVFNPKKRITADEALAHPYLAQL--HDPEDEPVAKPPFDFPFFD 313
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
126-281 1.55e-14

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


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 73.84  E-value: 1.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 126 FPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAkLINPEKPVSMVSGISNSMCPEVLEDQPY 205
Cdd:cd14116  102 FDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWS-VHAPSSRRTTLCGTLDYLPPEMIEGRMH 180
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334185276 206 GYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSpLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd14116  181 DEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFT-FPDFVTEGARDLISRLLKHNPSQRPMLREVLEHP 255
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
77-271 1.68e-14

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: 73.56  E-value: 1.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  77 MKLLSSLKNPYIVHYEDSwidNDNNACIFTA--YYEGGNMANAIKkARGKLfPEERIFKWLAQLLLAVNYLHSNRVVHMD 154
Cdd:cd14120   43 IKILKELSHENVVALLDC---QETSSSVYLVmeYCNGGDLADYLQ-AKGTL-SEDTIRVFLQQIAAAMKALHSKGIVHRD 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 155 LTCSNIFL---------PKDDHVQLGNYGLAKLINPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQ 225
Cdd:cd14120  118 LKPQNILLshnsgrkpsPNDIRLKIADFGFARFLQDGMMAATLCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGK 197
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 334185276 226 PAFKA--PDMAGLINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYR 271
Cdd:cd14120  198 APFQAqtPQELKAFYEKNANLRPNIPSGTSPALKDLLLGLLKRNPKDR 245
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
138-294 2.23e-14

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 75.03  E-value: 2.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 138 LLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKL---INPEKPVSMVSGISNSmCPEVLEDQPYGYKSDIWSL 214
Cdd:PHA03212 191 VLRAIQYLHENRIIHRDIKAENIFINHPGDVCLGDFGAACFpvdINANKYYGWAGTIATN-APELLARDPYGPAVDIWSA 269
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 215 GCCMYEI-TAHQPAFKAPDMAG---------LInkINRSLMSP--LPIVYSSTL-KQMIKLMLR--KKPEYRPTACELLR 279
Cdd:PHA03212 270 GIVLFEMaTCHDSLFEKDGLDGdcdsdrqikLI--IRRSGTHPneFPIDAQANLdEIYIGLAKKssRKPGSRPLWTNLYE 347
                        170
                 ....*....|....*
gi 334185276 280 NPSLQPYLLqCQNLS 294
Cdd:PHA03212 348 LPIDLEYLI-CKMLA 361
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
55-278 2.42e-14

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: 73.11  E-value: 2.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  55 HTDKLKQTALQEISRAVinydlmKLLSSLKNPYIVHYEDSWIDN-DNNACIF--TAYYEGGNMANAIKKARG-KLFPEER 130
Cdd:cd14033   35 QTRKLSKGERQRFSEEV------EMLKGLQHPNIVRFYDSWKSTvRGHKCIIlvTELMTSGTLKTYLKRFREmKLKLLQR 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 131 ifkWLAQLLLAVNYLHSNR--VVHMDLTCSNIFLP-KDDHVQLGNYGLAKLINPEKPVSMVsGISNSMCPEVLEDQpYGY 207
Cdd:cd14033  109 ---WSRQILKGLHFLHSRCppILHRDLKCDNIFITgPTGSVKIGDLGLATLKRASFAKSVI-GTPEFMAPEMYEEK-YDE 183
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334185276 208 KSDIWSLGCCMYEI-TAHQPAFKAPDMAGLINKINRSLM-SPLPIVYSSTLKQMIKLMLRKKPEYRPTACELL 278
Cdd:cd14033  184 AVDVYAFGMCILEMaTSEYPYSECQNAAQIYRKVTSGIKpDSFYKVKVPELKEIIEGCIRTDKDERFTIQDLL 256
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
19-281 2.89e-14

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: 73.13  E-value: 2.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  19 YHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAKHTDKLKQTALQEIsraVINydlmkllSSLKNPYIVHYEDSwiDN 98
Cdd:cd14069    3 WDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPGDCPENIKKEV---CIQ-------KMLSHKNVVRFYGH--RR 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  99 DNNAC-IFTAYYEGGNMANAIKKARGklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAK 177
Cdd:cd14069   71 EGEFQyLFLEYASGGELFDKIEPDVG--MPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLAT 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 178 L-INPEKpvsmvSGISNSMC-------PEVLEDQPY-GYKSDIWSLGCCMYEITA-----HQPAFKAPDMAGLINKiNRS 243
Cdd:cd14069  149 VfRYKGK-----ERLLNKMCgtlpyvaPELLAKKKYrAEPVDVWSCGIVLFAMLAgelpwDQPSDSCQEYSDWKEN-KKT 222
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 334185276 244 LMSPLPIVySSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd14069  223 YLTPWKKI-DTAALSLLRKILTENPNKRITIEDIKKHP 259
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
49-240 3.14e-14

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: 73.62  E-value: 3.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  49 KICLAKHTDKLKQTALQEIS-RAVIN-------YDLMKLLSSLKNPYIVHYEDSWIDnDNNACIFTAYYEGGNMANAIKk 120
Cdd:cd05612   16 RVHLVRDRISEHYYALKVMAiPEVIRlkqeqhvHNEKRVLKEVSHPFIIRLFWTEHD-QRFLYMLMEYVPGGELFSYLR- 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 121 ARGKLFPEERIFkWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINpEKPVSMVsGISNSMCPEVL 200
Cdd:cd05612   94 NSGRFSNSTGLF-YASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKKLR-DRTWTLC-GTPEYLAPEVI 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 334185276 201 EDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKI 240
Cdd:cd05612  171 QSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKI 210
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
77-277 3.28e-14

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: 73.39  E-value: 3.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  77 MKLLSSLKNPYIVHYED-SWIDNDNNACIFTAYYEGGNMANAIKKARGKLFPEeRIFKWLAQLLLAVNYLHSNRVVHMDL 155
Cdd:cd05081   56 IQILKALHSDFIVKYRGvSYGPGRRSLRLVMEYLPSGCLRDFLQRHRARLDAS-RLLLYSSQICKGMEYLGSRRCVHRDL 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 156 TCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNS----MCPEVLEDQPYGYKSDIWSLGCCMYEITAHQ------ 225
Cdd:cd05081  135 AARNILVESEAHVKIADFGLAKLLPLDKDYYVVREPGQSpifwYAPESLSDNIFSRQSDVWSFGVVLYELFTYCdkscsp 214
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334185276 226 ---------PAFKAPDMAGLINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACEL 277
Cdd:cd05081  215 saeflrmmgCERDVPALCRLLELLEEGQRLPAPPACPAEVHELMKLCWAPSPQDRPSFSAL 275
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
77-281 3.45e-14

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: 72.54  E-value: 3.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  77 MKLLSSLKNPYIVHYEDSWIDNDNNACIFTAYYEGGNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLT 156
Cdd:cd14109   47 VDIHNSLDHPNIVQMHDAYDDEKLAVTVIDNLASTIELVRDNLLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLR 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 157 CSNIFLpKDDHVQLGNYGLAKLINPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYE-ITAHQPAFKAPDMAG 235
Cdd:cd14109  127 PEDILL-QDDKLKLADFGQSRRLLRGKLTTLIYGSPEFVSPEIVNSYPVTLATDMWSVGVLTYVlLGGISPFLGDNDRET 205
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 334185276 236 LIN------KINRSLMSPLpivySSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd14109  206 LTNvrsgkwSFDSSPLGNI----SDDARDFIKKLLVYIPESRLTVDEALNHP 253
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
46-240 3.99e-14

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: 73.14  E-value: 3.99e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  46 AMKKICLAKHTDKLKQTALQEISravinydLMKLLSSLKNPYIVHYED-SWIDNDNNACIFTAYYE--GGNMANAIKKAR 122
Cdd:cd07862   31 ALKRVRVQTGEEGMPLSTIREVA-------VLRHLETFEHPNVVRLFDvCTVSRTDRETKLTLVFEhvDQDLTTYLDKVP 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 123 GKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNSMCPEVLED 202
Cdd:cd07862  104 EPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLARIYSFQMALTSVVVTLWYRAPEVLLQ 183
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 334185276 203 QPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKI 240
Cdd:cd07862  184 SSYATPVDLWSVGCIFAEMFRRKPLFRGSSDVDQLGKI 221
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
17-302 4.81e-14

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: 74.27  E-value: 4.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  17 DNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMK---KICLAKHTDklkqTALQEISRavinyDLMKLLSSlknPYIVHYED 93
Cdd:cd05622   73 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKllsKFEMIKRSD----SAFFWEER-----DIMAFANS---PWVVQLFY 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  94 SWIDnDNNACIFTAYYEGGNMANAIKKARgklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNY 173
Cdd:cd05622  141 AFQD-DRYLYMVMEYMPGGDLVNLMSNYD---VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADF 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 174 GLAKLINPEKPV--SMVSGISNSMCPEVLEDQP----YGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKI---NRSL 244
Cdd:cd05622  217 GTCMKMNKEGMVrcDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKImnhKNSL 296
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 245 MSPLPIVYSSTLKQMIKLML--RKKPEYRPTACELLRNPSLQPYLLQCQNLSPIYLPVFP 302
Cdd:cd05622  297 TFPDDNDISKEAKNLICAFLtdREVRLGRNGVEEIKRHLFFKNDQWAWETLRDTVAPVVP 356
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
121-283 5.02e-14

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: 72.26  E-value: 5.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 121 ARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSM--VSGISNSMCPE 198
Cdd:cd14110   91 AERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLGNAQPFNQGKVLMTdkKGDYVETMAPE 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 199 VLEDQPYGYKSDIWSLGCCMYEITAHQPAFKApDMAGLINKINRSLMSPLPIVYSSTLKQMIKLM---LRKKPEYRPTAC 275
Cdd:cd14110  171 LLEGQGAGPQTDIWAIGVTAFIMLSADYPVSS-DLNWERDRNIRKGKVQLSRCYAGLSGGAVNFLkstLCAKPWGRPTAS 249

                 ....*...
gi 334185276 276 ELLRNPSL 283
Cdd:cd14110  250 ECLQNPWL 257
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
43-293 5.26e-14

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: 73.16  E-value: 5.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  43 KKYAMKkiCLAKHTDKLKQTALQeisravinyDLMKLLSSLKNPYIVHYEDSWiDNDNNACIFTAYYEGGNMANAIkkAR 122
Cdd:cd14168   36 KLFAVK--CIPKKALKGKESSIE---------NEIAVLRKIKHENIVALEDIY-ESPNHLYLVMQLVSGGELFDRI--VE 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 123 GKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNI--FLPKDD-HVQLGNYGLAKLINPEKPVSMVSGISNSMCPEV 199
Cdd:cd14168  102 KGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLlyFSQDEEsKIMISDFGLSKMEGKGDVMSTACGTPGYVAPEV 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 200 LEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRS---LMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACE 276
Cdd:cd14168  182 LAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAdyeFDSPYWDDISDSAKDFIRNLMEKDPNKRYTCEQ 261
                        250
                 ....*....|....*..
gi 334185276 277 LLRNPSLQPYLLQCQNL 293
Cdd:cd14168  262 ALRHPWIAGDTALCKNI 278
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
77-301 5.47e-14

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: 72.74  E-value: 5.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  77 MKLLSSLKNPYIVHYED-SWIDNDNNACIFTAYYEGGNMANAIKKARGKlFPEERIFKWLAQLLLAVNYLHSNRVVHMDL 155
Cdd:cd14205   56 IEILKSLQHDNIVKYKGvCYSAGRRNLRLIMEYLPYGSLRDYLQKHKER-IDHIKLLQYTSQICKGMEYLGTKRYIHRDL 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 156 TCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNS----MCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAP 231
Cdd:cd14205  135 ATRNILVENENRVKIGDFGLTKVLPQDKEYYKVKEPGESpifwYAPESLTESKFSVASDVWSFGVVLYELFTYIEKSKSP 214
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 232 DmAGLINKINRSLMSPLpIVYsstlkQMIKLMLRKKPEYRPTACEllrnPSLQPYLLQCQNLSPIYLPVF 301
Cdd:cd14205  215 P-AEFMRMIGNDKQGQM-IVF-----HLIELLKNNGRLPRPDGCP----DEIYMIMTECWNNNVNQRPSF 273
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
78-275 5.92e-14

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


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 72.41  E-value: 5.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  78 KLLSSLKNPYIVHYED-SWIDNDNNACIFTAYYEGGNMANAIKKARGKLfPEERIFKWLAQLLLAVNYLHSNRVVHMDLT 156
Cdd:cd05038   58 EILRTLDHEYIVKYKGvCESPGRRSLRLIMEYLPSGSLRDYLQRHRDQI-DLKRLLLFASQICKGMEYLGSQRYIHRDLA 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 157 CSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNS----MCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPd 232
Cdd:cd05038  137 ARNILVESEDLVKISDFGLAKVLPEDKEYYYVKEPGESpifwYAPECLRESRFSSASDVWSFGVTLYELFTYGDPSQSP- 215
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 334185276 233 maglinkINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTAC 275
Cdd:cd05038  216 -------PALFLRMIGIAQGQMIVTRLLELLKSGERLPRPPSC 251
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
101-278 6.16e-14

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: 72.36  E-value: 6.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 101 NACIFTAYYEGGNMANAIKKARGKlFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKL-- 178
Cdd:cd14150   69 NFAIITQWCEGSSLYRHLHVTETR-FDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLATVkt 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 179 -INPEKPVSMVSGISNSMCPEVL---EDQPYGYKSDIWSLGCCMYEI-TAHQPAFKAPDMAGLINKINRSLMSP-LPIVY 252
Cdd:cd14150  148 rWSGSQQVEQPSGSILWMAPEVIrmqDTNPYSFQSDVYAYGVVLYELmSGTLPYSNINNRDQIIFMVGRGYLSPdLSKLS 227
                        170       180
                 ....*....|....*....|....*....
gi 334185276 253 SSTLKQMIKLM---LRKKPEYRPTACELL 278
Cdd:cd14150  228 SNCPKAMKRLLidcLKFKREERPLFPQIL 256
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
46-240 8.03e-14

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: 72.30  E-value: 8.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  46 AMKKICLAKHTDKLKQTALQEISravinydLMKLLSSLKNPYIVHYED----SWIDNDNNACIFTAYYEGgNMANAIKKA 121
Cdd:cd07863   29 ALKSVRVQTNEDGLPLSTVREVA-------LLKRLEAFDHPNIVRLMDvcatSRTDRETKVTLVFEHVDQ-DLRTYLDKV 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 122 RGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNSMCPEVLE 201
Cdd:cd07863  101 PPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLARIYSCQMALTPVVVTLWYRAPEVLL 180
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 334185276 202 DQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKI 240
Cdd:cd07863  181 QSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKI 219
PK_NRBP1_like cd13984
Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The ...
80-283 1.01e-13

Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. This subfamily is composed of NRBP1, also called MLF1-adaptor molecule (MADM), and MADML. NRBP1 was originally named based on the presence of nuclear binding and localization motifs prior to functional analyses. It is expressed ubiquitously and is found to localize in the cytoplasm, not the nucleus. NRBP1 is an adaptor protein that interacts with myeloid leukemia factor 1 (MLF1), an oncogene that enhances myeloid development of hematopoietic cells. It also interacts with the small GTPase Rac3. NRBP1 may also be involved in Golgi to ER trafficking. MADML (for MADM-Like) has been shown to be expressed throughout development in Xenopus laevis with highest expression found in the developing lens and retina. The NRBP1-like 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: 270886 [Multi-domain]  Cd Length: 256  Bit Score: 71.41  E-value: 1.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  80 LSSLKNPYIVHYEDSWIDNDNNA--CIF-TAYYEGGNMANAIKKAR--GKLFPEERIFKWLAQLLLAVNYLHSNR--VVH 152
Cdd:cd13984   49 LIQLDHPNIVKFHRYWTDVQEEKarVIFiTEYMSSGSLKQFLKKTKknHKTMNEKSWKRWCTQILSALSYLHSCDppIIH 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 153 MDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITA---HQPAFK 229
Cdd:cd13984  129 GNLTCDTIFIQHNGLIKIGSVAPDAIHNHVKTCREEHRNLHFFAPEYGYLEDVTTAVDIYSFGMCALEMAAleiQSNGEK 208
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 334185276 230 APDMAGLINKINRSLMSPLpivysstLKQMIKLMLRKKPEYRPTACELLRNPSL 283
Cdd:cd13984  209 VSANEEAIIRAIFSLEDPL-------QKDFIRKCLSVAPQDRPSARDLLFHPVL 255
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
34-226 1.12e-13

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: 72.02  E-value: 1.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  34 FVVLHDIEDKKYAMKKICLAKHTDKLKQTALQEIsravinydlmKLLSSLKNPYIVH-----YEDSWIDNDNNACI---- 104
Cdd:cd07865   29 FKARHRKTGQIVALKKVLMENEKEGFPITALREI----------KILQLLKHENVVNlieicRTKATPYNRYKGSIylvf 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 105 -FTAYYEGGNMANAIKKargklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEK 183
Cdd:cd07865   99 eFCEHDLAGLLSNKNVK-----FTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVLKLADFGLARAFSLAK 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 334185276 184 pvsmvSGISNSMC----------PEV-LEDQPYGYKSDIWSLGCCMYEITAHQP 226
Cdd:cd07865  174 -----NSQPNRYTnrvvtlwyrpPELlLGERDYGPPIDMWGAGCIMAEMWTRSP 222
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
14-271 1.30e-13

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: 72.40  E-value: 1.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  14 FTLDNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKkiCLAKHTDKLKQTALQEISRAVinydLMKLLSSLKNPYIVHYED 93
Cdd:cd05633    2 LTMNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMK--CLDKKRIKMKQGETLALNERI----MLSLVSTGDCPFIVCMTY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  94 SWIDNDNnACIFTAYYEGGNMANAIkkARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNY 173
Cdd:cd05633   76 AFHTPDK-LCFILDLMNGGDLHYHL--SQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 174 GLAKLINPEKPVSMVsGISNSMCPEVLED-QPYGYKSDIWSLGCCMYE-ITAHQP--AFKAPDMAGlINKINRSLMSPLP 249
Cdd:cd05633  153 GLACDFSKKKPHASV-GTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKlLRGHSPfrQHKTKDKHE-IDRMTLTVNVELP 230
                        250       260
                 ....*....|....*....|..
gi 334185276 250 IVYSSTLKQMIKLMLRKKPEYR 271
Cdd:cd05633  231 DSFSPELKSLLEGLLQRDVSKR 252
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
79-276 1.81e-13

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: 70.64  E-value: 1.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  79 LLSSLKNPYIVHYEDSWIDNDNNACIFTAYYEGGNMANaikkargKLFPEERIFKWLAQLLLAVN------YLH--SNRV 150
Cdd:cd14064   44 ILCRLNHPCVIQFVGACLDDPSQFAIVTQYVSGGSLFS-------LLHEQKRVIDLQSKLIIAVDvakgmeYLHnlTQPI 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 151 VHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNS--MCPEVL-EDQPYGYKSDIWSLGCCMYEIT----- 222
Cdd:cd14064  117 IHRDLNSHNILLYEDGHAVVADFGESRFLQSLDEDNMTKQPGNLrwMAPEVFtQCTRYSIKADVFSYALCLWELLtgeip 196
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 334185276 223 -AH-QPAFKAPDMAglinkiNRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACE 276
Cdd:cd14064  197 fAHlKPAAAAADMA------YHHIRPPIGYSIPKPISSLLMRGWNAEPESRPSFVE 246
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
42-281 1.86e-13

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: 71.10  E-value: 1.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  42 DKKYAMKKICLAKHTDKLKQTALQEISravinydlmkLLSSLKNPYIVHYEDSWI-DNDNNACIFTAYYEGgNMANAIKK 120
Cdd:cd07843   30 GEIVALKKLKMEKEKEGFPITSLREIN----------ILLKLQHPNIVTVKEVVVgSNLDKIYMVMEYVEH-DLKSLMET 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 121 ARGKLFPEERifKWLA-QLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLI-NPEKPVSMVSGISNSMCPE 198
Cdd:cd07843   99 MKQPFLQSEV--KCLMlQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLAREYgSPLKPYTQLVVTLWYRAPE 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 199 VLEDQP-YGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSP----------LPIVYSSTLKQMIKLMLRKK 267
Cdd:cd07843  177 LLLGAKeYSTAIDMWSVGCIFAELLTKKPLFPGKSEIDQLNKIFKLLGTPtekiwpgfseLPGAKKKTFTKYPYNQLRKK 256
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 334185276 268 ---------------------PEYRPTACELLRNP 281
Cdd:cd07843  257 fpalslsdngfdllnrlltydPAKRISAEDALKHP 291
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
17-264 1.87e-13

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


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 72.02  E-value: 1.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  17 DNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKkiCLAKhTDKLKQ--TALQEISRavinyDLMKLLSSlknPYIVHYEDS 94
Cdd:cd05596   26 EDFDVIKVIGRGAFGEVQLVRHKSTKKVYAMK--LLSK-FEMIKRsdSAFFWEER-----DIMAHANS---EWIVQLHYA 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  95 WIDnDNNACIFTAYYEGGNMANAIKKARgklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYG 174
Cdd:cd05596   95 FQD-DKYLYMVMDYMPGGDLVNLMSNYD---VPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFG 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 175 LAKLINPEKPV--SMVSGISNSMCPEVLEDQP----YGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKI---NRSLM 245
Cdd:cd05596  171 TCMKMDKDGLVrsDTAVGTPDYISPEVLKSQGgdgvYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYGKImnhKNSLQ 250
                        250
                 ....*....|....*....
gi 334185276 246 SPLPIVYSSTLKQMIKLML 264
Cdd:cd05596  251 FPDDVEISKDAKSLICAFL 269
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
38-280 1.88e-13

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: 71.87  E-value: 1.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  38 HDiEDKKYAMKKICLAKHTDKLKQTALQEISRAVINYdlmkllsSLKNPYIV--HYEdswIDNDNNACIFTAYYEGGNMA 115
Cdd:cd05614   25 HD-ANKLYAMKVLRKAALVQKAKTVEHTRTERNVLEH-------VRQSPFLVtlHYA---FQTDAKLHLILDYVSGGELF 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 116 NAIKKARGklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVS--GISN 193
Cdd:cd05614   94 THLYQRDH--FSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSKEFLTEEKERTYSfcGTIE 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 194 SMCPEVLEDQP-YGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMS---PLPIVYSSTLKQMIKLMLRKKPE 269
Cdd:cd05614  172 YMAPEIIRGKSgHGKAVDWWSLGILMFELLTGASPFTLEGEKNTQSEVSRRILKcdpPFPSFIGPVARDLLQKLLCKDPK 251
                        250
                 ....*....|....*
gi 334185276 270 YR----PTACELLRN 280
Cdd:cd05614  252 KRlgagPQGAQEIKE 266
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
15-229 1.89e-13

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: 71.58  E-value: 1.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  15 TLDNYHVVEQVRRGKsssdFVVLHDIEDKK----YAMKKICLAKHTDKLKQTALQEIsravinydlmKLLSSLKNPYIVH 90
Cdd:cd07866    6 KLRDYEILGKLGEGT----FGEVYKARQIKtgrvVALKKILMHNEKDGFPITALREI----------KILKKLKHPNVVP 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  91 -----YEDSWIDNDNNACIFTAY-YEGGNMANAIKKARGKLfPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPK 164
Cdd:cd07866   72 lidmaVERPDKSKRKRGSVYMVTpYMDHDLSGLLENPSVKL-TESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDN 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334185276 165 DDHVQLGNYGLAKLINPEKPVSMVSGISN-----SMC-------PE-VLEDQPYGYKSDIWSLGCCMYEITAHQPAFK 229
Cdd:cd07866  151 QGILKIADFGLARPYDGPPPNPKGGGGGGtrkytNLVvtrwyrpPElLLGERRYTTAVDIWGIGCVFAEMFTRRPILQ 228
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
17-285 2.04e-13

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: 71.20  E-value: 2.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  17 DNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKIclakhtDKLKQTALQEISravinydlmKLLSSLKNPYIVHYEDSWi 96
Cdd:cd14177    4 DVYELKEDIGVGSYSVCKRCIHRATNMEFAVKII------DKSKRDPSEEIE---------ILMRYGQHPNIITLKDVY- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  97 DNDNNACIFTAYYEGGNMANAIkkARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKD----DHVQLGN 172
Cdd:cd14177   68 DDGRYVYLVTELMKGGELLDRI--LRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDsanaDSIRICD 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 173 YGLAKLINPEKPVSMVSG-ISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITA-HQPAFKAP-----DMAGLINKINRSLM 245
Cdd:cd14177  146 FGFAKQLRGENGLLLTPCyTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAgYTPFANGPndtpeEILLRIGSGKFSLS 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 334185276 246 SPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLR---------NPSLQP 285
Cdd:cd14177  226 GGNWDTVSDAAKDLLSHMLHVDPHQRYTAEQVLKhswiacrdqLPHYQL 274
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
49-281 2.22e-13

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: 70.49  E-value: 2.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  49 KICLAKHTDKLKQTALQEISRAVINYDL------MKLLSSLKNPYIVH-YEdsWIDNDNNACIFTAYYEGGNMANAIKkA 121
Cdd:cd14078   18 KVKLATHILTGEKVAIKIMDKKALGDDLprvkteIEALKNLSHQHICRlYH--VIETDNKIFMVLEYCPGGELFDYIV-A 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 122 RGKLFPEE-RIFkwLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKlinpeKPVSMVSGISNSMC---- 196
Cdd:cd14078   95 KDRLSEDEaRVF--FRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCA-----KPKGGMDHHLETCCgspa 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 197 ---PEVLEDQPY-GYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSpLPIVYSSTLKQMIKLMLRKKPEYRP 272
Cdd:cd14078  168 yaaPELIQGKPYiGSEADVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSGKYE-EPEWLSPSSKLLLDQMLQVDPKKRI 246

                 ....*....
gi 334185276 273 TACELLRNP 281
Cdd:cd14078  247 TVKELLNHP 255
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
17-281 2.27e-13

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: 70.42  E-value: 2.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  17 DNYHVVEQVRRGKsssdFVVLHDIEDK----KYAMKKICLAKHTDKLKQTALQEISRAVinydlmKLLSSLKNPYIVHYE 92
Cdd:cd14195    5 DHYEMGEELGSGQ----FAIVRKCREKgtgkEYAAKFIKKRRLSSSRRGVSREEIEREV------NILREIQHPNIITLH 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  93 DSWiDNDNNACIFTAYYEGGNMANAIkkARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDD----HV 168
Cdd:cd14195   75 DIF-ENKTDVVLILELVSGGELFDFL--AEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNvpnpRI 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 169 QLGNYGLAKLINPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAF---KAPDMAGLINKINRSLM 245
Cdd:cd14195  152 KLIDFGIAHKIEAGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFlgeTKQETLTNISAVNYDFD 231
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 334185276 246 SPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd14195  232 EEYFSNTSELAKDFIRRLLVKDPKKRMTIAQSLEHS 267
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
78-278 2.48e-13

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: 70.08  E-value: 2.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  78 KLLSSLK---NPYIVHYEDSWID--NDNNA---CIFTAYYEGGNMANAIKKArGKLfPEERIFKWLAQLLLAVNYLHSNR 149
Cdd:cd14012   47 KELESLKklrHPNLVSYLAFSIErrGRSDGwkvYLLTEYAPGGSLSELLDSV-GSV-PLDTARRWTLQLLEALEYLHRNG 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 150 VVHMDLTCSNIFLPKDDH---VQLGNYGLAKLINPE--KPVSMVSGISNSMCPEV-LEDQPYGYKSDIWSLGCCMYEIta 223
Cdd:cd14012  125 VVHKSLHAGNVLLDRDAGtgiVKLTDYSLGKTLLDMcsRGSLDEFKQTYWLPPELaQGSKSPTRKTDVWDLGLLFLQM-- 202
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 334185276 224 hqpafkapdMAGLINKINRSLMSPL--PIVYSSTLKQMIKLMLRKKPEYRPTACELL 278
Cdd:cd14012  203 ---------LFGLDVLEKYTSPNPVlvSLDLSASLQDFLSKCLSLDPKKRPTALELL 250
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
43-271 2.67e-13

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: 71.23  E-value: 2.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  43 KKYAMKkiCLAKHTDKLKQTALQEISRAVinydLMKLLSSLKNPYIVHYEDSWIDNDNNACIFTaYYEGGNMANAIkkAR 122
Cdd:cd14223   26 KMYAMK--CLDKKRIKMKQGETLALNERI----MLSLVSTGDCPFIVCMSYAFHTPDKLSFILD-LMNGGDLHYHL--SQ 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 123 GKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVsGISNSMCPEVLED 202
Cdd:cd14223   97 HGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLACDFSKKKPHASV-GTHGYMAPEVLQK 175
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334185276 203 Q-PYGYKSDIWSLGCCMYE-ITAHQP--AFKAPDMAGlINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYR 271
Cdd:cd14223  176 GvAYDSSADWFSLGCMLFKlLRGHSPfrQHKTKDKHE-IDRMTLTMAVELPDSFSPELRSLLEGLLQRDVNRR 247
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
49-282 2.85e-13

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


Pssm-ID: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 69.86  E-value: 2.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  49 KICLAKHTDKLKQTALQEISRAVIN-------YDLMKLLSSLKNPYIVH-YEdsWIDNDNNACIFTAYYEGGNMANAIKk 120
Cdd:cd14072   15 KVKLARHVLTGREVAIKIIDKTQLNpsslqklFREVRIMKILNHPNIVKlFE--VIETEKTLYLVMEYASGGEVFDYLV- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 121 ARGKLFPEERIFKWlAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNSMCPEVL 200
Cdd:cd14072   92 AHGRMKEKEARAKF-RQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFTPGNKLDTFCGSPPYAAPELF 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 201 EDQPY-GYKSDIWSLGCCMYEITAHQPAFKApdmaglinkinrslmsplpivysSTLKQMIKLMLRKK---PEYRPTACE 276
Cdd:cd14072  171 QGKKYdGPEVDVWSLGVILYTLVSGSLPFDG-----------------------QNLKELRERVLRGKyriPFYMSTDCE 227
                        250
                 ....*....|..
gi 334185276 277 ------LLRNPS 282
Cdd:cd14072  228 nllkkfLVLNPS 239
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
78-279 2.85e-13

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: 70.11  E-value: 2.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  78 KLLSSLKNPYIVHYEDSWIdNDNNACIFTAYYEGGNMANAIKkarGKLFPEERIFKWLAQLLLAVNYLHSNR---VVHMD 154
Cdd:cd14061   45 RLFWMLRHPNIIALRGVCL-QPPNLCLVMEYARGGALNRVLA---GRKIPPHVLVDWAIQIARGMNYLHNEApvpIIHRD 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 155 LTCSNIFL---PKDDHVQ-----LGNYGLAKLINPEKPVSmVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQP 226
Cdd:cd14061  121 LKSSNILIleaIENEDLEnktlkITDFGLAREWHKTTRMS-AAGTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEV 199
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 334185276 227 AFKAPDMAGL-----INKinrsLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLR 279
Cdd:cd14061  200 PYKGIDGLAVaygvaVNK----LTLPIPSTCPEPFAQLMKDCWQPDPHDRPSFADILK 253
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
17-281 3.31e-13

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: 70.21  E-value: 3.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  17 DNYHVVEQVrrgkSSSDFVVLHDIEDK----KYAMKKICLAKHTDKLKQTALQEISRAVinydlmKLLSSLKNPYIVHYE 92
Cdd:cd14105    5 DFYDIGEEL----GSGQFAVVKKCREKstglEYAAKFIKKRRSKASRRGVSREDIEREV------SILRQVLHPNIITLH 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  93 DSWiDNDNNACIFTAYYEGGNMANAIkkARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDD----HV 168
Cdd:cd14105   75 DVF-ENKTDVVLILELVAGGELFDFL--AEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNvpipRI 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 169 QLGNYGLAKLINPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPL 248
Cdd:cd14105  152 KLIDFGLAHKIEDGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVNYDFD 231
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 334185276 249 PIVYSST---LKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd14105  232 DEYFSNTselAKDFIRQLLVKDPRKRMTIQESLRHP 267
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
44-271 3.62e-13

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: 70.68  E-value: 3.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  44 KYAMKKICLAKHTDKLKQTALQEI------SRAVINYDLMK--LLSSLKNPYIVHYEDSWiDNDNNACIFTAYYEGGNMA 115
Cdd:cd05585    4 KGSFGKVMQVRKKDTSRIYALKTIrkahivSRSEVTHTLAErtVLAQVDCPFIVPLKFSF-QSPEKLYLVLAFINGGELF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 116 NAIKKaRGKlFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKL-INPEKPVSMVSGISNS 194
Cdd:cd05585   83 HHLQR-EGR-FDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKLnMKDDDKTNTFCGTPEY 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185276 195 MCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKInrsLMSPL--PIVYSSTLKQMIKLMLRKKPEYR 271
Cdd:cd05585  161 LAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKI---LQEPLrfPDGFDRDAKDLLIGLLNRDPTKR 236
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
27-219 3.77e-13

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: 69.56  E-value: 3.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  27 RGKsssdFVVLHDIEDKKyaMKKICLAK----HTDKLKQTALQEISravinydlmkLLSSLKNPYIVHYEDSWiDNDNNA 102
Cdd:cd14103    3 RGK----FGTVYRCVEKA--TGKELAAKfikcRKAKDREDVRNEIE----------IMNQLRHPRLLQLYDAF-ETPREM 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 103 CIFTAYYEGGnmanaikkargKLFpeERIF------------KWLAQLLLAVNYLHSNRVVHMDLTCSNIFL--PKDDHV 168
Cdd:cd14103   66 VLVMEYVAGG-----------ELF--ERVVdddfelterdciLFMRQICEGVQYMHKQGILHLDLKPENILCvsRTGNQI 132
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 334185276 169 QLGNYGLAKLINPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMY 219
Cdd:cd14103  133 KIIDFGLARKYDPDKKLKVLFGTPEFVAPEVVNYEPISYATDMWSVGVICY 183
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
108-271 3.89e-13

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: 70.72  E-value: 3.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 108 YYEGGNMANAIKKARGklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKL-INPEKPVS 186
Cdd:cd05619   87 YLNGGDLMFHIQSCHK--FDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKEnMLGDAKTS 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 187 MVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSlmSPL-PIVYSSTLKQMIKLMLR 265
Cdd:cd05619  165 TFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSIRMD--NPFyPRWLEKEAKDILVKLFV 242

                 ....*.
gi 334185276 266 KKPEYR 271
Cdd:cd05619  243 REPERR 248
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
43-295 5.02e-13

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: 70.01  E-value: 5.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  43 KKYAMKKICLAK-HTDKLKQTALQEISravinydlmkLLSSLKNPYIVHYEDSWIDNdNNACIFTAY-YEGGNMANAIK- 119
Cdd:cd07842   28 KEYAIKKFKGDKeQYTGISQSACREIA----------LLRELKHENVVSLVEVFLEH-ADKSVYLLFdYAEHDLWQIIKf 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 120 --KARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFL----PKDDHVQLGNYGLAKLIN-PEKPVSMVSGIS 192
Cdd:cd07842   97 hrQAKRVSIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVmgegPERGVVKIGDLGLARLFNaPLKPLADLDPVV 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 193 NSM---CPEVLedqpYGYKS-----DIWSLGCCMYEITAHQPAFKApdmaglinkINRSLMSPLPIvYSSTLKQMIKLM- 263
Cdd:cd07842  177 VTIwyrAPELL----LGARHytkaiDIWAIGCIFAELLTLEPIFKG---------REAKIKKSNPF-QRDQLERIFEVLg 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 334185276 264 ---------LRKKPEY----RPTACELLRNPSLQPYLLQCQNLSP 295
Cdd:cd07842  243 tptekdwpdIKKMPEYdtlkSDTKASTYPNSLLAKWMHKHKKPDS 287
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
86-281 5.19e-13

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: 69.24  E-value: 5.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  86 PYIVH----YEDSwidNDNNAC--IFTAYYEGGNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSN 159
Cdd:cd14089   54 PHIVRiidvYENT---YQGRKCllVVMECMEGGELFSRIQERADSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPEN 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 160 I-FLPKDDH--VQLGNYGLAKLINPEKPVsmvsgisNSMC-------PEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFK 229
Cdd:cd14089  131 LlYSSKGPNaiLKLTDFGFAKETTTKKSL-------QTPCytpyyvaPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFY 203
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 334185276 230 A-------PDMAGLINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd14089  204 SnhglaisPGMKKRIRNGQYEFPNPEWSNVSEEAKDLIRGLLKTDPSERLTIEEVMNHP 262
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
42-284 5.49e-13

Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This subfamily is composed of the catalytically inactive kinases with similarity to yeast Scy1. It includes four mammalian proteins called SCY1-like protein 1 (SCYL1), SCYL2, SCYL3, as well as Testis-EXpressed protein 14 (TEX14). SCYL1 binds to and co-localizes with the membrane trafficking coatomer I (COPI) complex, and regulates COPI-mediated vesicle trafficking. Null mutations in the SCYL1 gene are responsible for the pathology in mdf (muscle-deficient) mice which display progressive motor neuropathy. SCYL2, also called coated vesicle-associated kinase of 104 kDa (CVAK104), is involved in the trafficking of clathrin-coated vesicles. It also binds the HIV-1 accessory protein Vpu and acts as a regulatory factor that promotes the dephosphorylation of Vpu, facilitating the restriction of HIV-1 release. SCYL3, also called ezrin-binding protein PACE-1, may be involved in regulating cell adhesion and migration. TEX14 is required for spermatogenesis and male fertility. It localizes to kinetochores (KT) during mitosis and is a target of the mitotic kinase PLK1. It regulates the maturation of the outer KT and the KT-microtubule attachment. The SCY1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 69.66  E-value: 5.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  42 DKKYamkkicLAKHTDKLKQTALQEISRAVinydlmKLLSSLKNPYIVHYEDSWIDNDNN---------ACIFTAYYEGG 112
Cdd:cd14011   30 EKKQ------LEEYSKRDREQILELLKRGV------KQLTRLRHPRILTVQHPLEESRESlafatepvfASLANVLGERD 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 113 NMANAIKKARG-KLFPEERifKW-LAQLLLAVNYLHSN-RVVHMDLTCSNIFLPKDDHVQLGNYGLA-KLINPEKPVSMV 188
Cdd:cd14011   98 NMPSPPPELQDyKLYDVEI--KYgLLQISEALSFLHNDvKLVHGNICPESVVINSNGEWKLAGFDFCiSSEQATDQFPYF 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 189 SGIS-----------NSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKIN----RSLMSPLPIVYS 253
Cdd:cd14011  176 REYDpnlpplaqpnlNYLAPEYILSKTCDPASDMFSLGVLIYAIYNKGKPLFDCVNNLLSYKKNsnqlRQLSLSLLEKVP 255
                        250       260       270
                 ....*....|....*....|....*....|.
gi 334185276 254 STLKQMIKLMLRKKPEYRPTACELLRNPSLQ 284
Cdd:cd14011  256 EELRDHVKTLLNVTPEVRPDAEQLSKIPFFD 286
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
129-285 6.02e-13

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


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 70.14  E-value: 6.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 129 ERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKlinpekpvsmVSGISNSM----------CPE 198
Cdd:cd07850  102 ERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLAR----------TAGTSFMMtpyvvtryyrAPE 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 199 VLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPLPIvYSSTLKQMIKLMLRKKPEYRPTACELL 278
Cdd:cd07850  172 VILGMGYKENVDIWSVGCIMGEMIRGTVLFPGTDHIDQWNKIIEQLGTPSDE-FMSRLQPTVRNYVENRPKYAGYSFEEL 250

                 ....*..
gi 334185276 279 RNPSLQP 285
Cdd:cd07850  251 FPDVLFP 257
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
78-280 7.29e-13

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: 68.98  E-value: 7.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  78 KLLSSLKNPYIVHYEDSW---IDNDNNACIFTAYYEGGNMANAIKkaRGKLFPEERIFKWLAQLLLAVNYLHSNR--VVH 152
Cdd:cd14031   61 EMLKGLQHPNIVRFYDSWesvLKGKKCIVLVTELMTSGTLKTYLK--RFKVMKPKVLRSWCRQILKGLQFLHTRTppIIH 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 153 MDLTCSNIFLP-KDDHVQLGNYGLAKLINPEKPVSMVsGISNSMCPEVLEDQpYGYKSDIWSLGCCMYEI-TAHQPAFKA 230
Cdd:cd14031  139 RDLKCDNIFITgPTGSVKIGDLGLATLMRTSFAKSVI-GTPEFMAPEMYEEH-YDESVDVYAFGMCMLEMaTSEYPYSEC 216
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 334185276 231 PDMAGLINKINRSLM-SPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRN 280
Cdd:cd14031  217 QNAAQIYRKVTSGIKpASFNKVTDPEVKEIIEGCIRQNKSERLSIKDLLNH 267
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
1-302 7.52e-13

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: 70.41  E-value: 7.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276   1 MQMEANDcqeehkftldnYHVVEQVRRGKSSSDFVVLHDIEDKKYAMK---KICLAKHTDklkqTALQEISRavinyDLM 77
Cdd:cd05621   47 LQMKAED-----------YDVVKVIGRGAFGEVQLVRHKASQKVYAMKllsKFEMIKRSD----SAFFWEER-----DIM 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  78 KLLSSlknPYIVHYEDSWIDnDNNACIFTAYYEGGNMANAIKKARgklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTC 157
Cdd:cd05621  107 AFANS---PWVVQLFCAFQD-DKYLYMVMEYMPGGDLVNLMSNYD---VPEKWAKFYTAEVVLALDAIHSMGLIHRDVKP 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 158 SNIFLPKDDHVQLGNYGLAKLINPEKPV--SMVSGISNSMCPEVLEDQP----YGYKSDIWSLGCCMYEITAHQPAFKAP 231
Cdd:cd05621  180 DNMLLDKYGHLKLADFGTCMKMDETGMVhcDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLFEMLVGDTPFYAD 259
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334185276 232 DMAGLINKI---NRSLMSPLPIVYSSTLKQMIKLML--RKKPEYRPTACELLRNPSLQPYLLQCQNLSPIYLPVFP 302
Cdd:cd05621  260 SLVGTYSKImdhKNSLNFPDDVEISKHAKNLICAFLtdREVRLGRNGVEEIKQHPFFRNDQWNWDNIRETAAPVVP 335
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
17-219 8.25e-13

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: 68.88  E-value: 8.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  17 DNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKIclAKHTDKLKQTALQEISravinydlmkLLSSLKNPYIVHYEDSWi 96
Cdd:cd14191    2 DFYDIEERLGSGKFGQVFRLVEKKTKKVWAGKFF--KAYSAKEKENIRQEIS----------IMNCLHHPKLVQCVDAF- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  97 DNDNNACIFTAYYEGGNMANAIKKARGKLfPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFL--PKDDHVQLGNYG 174
Cdd:cd14191   69 EEKANIVMVLEMVSGGELFERIIDEDFEL-TERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCvnKTGTKIKLIDFG 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 334185276 175 LAKLINPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMY 219
Cdd:cd14191  148 LARRLENAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICY 192
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
111-285 8.66e-13

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: 69.25  E-value: 8.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 111 GGNMANAIKKArgKLFPEE---RIFKwlaQLLLAVNYLHSNRVVHMDLTCSNIFL---PKDDHVQLGNYGLAKLINPEKP 184
Cdd:cd14092   83 GGELLERIRKK--KRFTESeasRIMR---QLVSAVSFMHSKGVVHRDLKPENLLFtdeDDDAEIKIVDFGFARLKPENQP 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 185 VSMVSGISNSMCPEVLE--DQPYGYKS--DIWSLGCCMYEITAHQPAFKAPD----MAGLINKINR---SLMSPLPIVYS 253
Cdd:cd14092  158 LKTPCFTLPYAAPEVLKqaLSTQGYDEscDLWSLGVILYTMLSGQVPFQSPSrnesAAEIMKRIKSgdfSFDGEEWKNVS 237
                        170       180       190
                 ....*....|....*....|....*....|..
gi 334185276 254 STLKQMIKLMLRKKPEYRPTACELLRNPSLQP 285
Cdd:cd14092  238 SEAKSLIQGLLTVDPSKRLTMSELRNHPWLQG 269
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
43-271 9.56e-13

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: 69.00  E-value: 9.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  43 KKYAMKkiCLAKHTDKLKQ---TALQEisravinYDLMKLLSSLKN-PYIVHYEDSWIDNDNnACIFTAYYEGGNMANAI 118
Cdd:cd05606   20 KMYAMK--CLDKKRIKMKQgetLALNE-------RIMLSLVSTGGDcPFIVCMTYAFQTPDK-LCFILDLMNGGDLHYHL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 119 kkARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVsGISNSMCPE 198
Cdd:cd05606   90 --SQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLACDFSKKKPHASV-GTHGYMAPE 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 199 VLED-QPYGYKSDIWSLGCCMYE-ITAHQP--AFKAPDMagliNKINRSLMS---PLPIVYSSTLKQMIKLMLRKKPEYR 271
Cdd:cd05606  167 VLQKgVAYDSSADWFSLGCMLYKlLKGHSPfrQHKTKDK----HEIDRMTLTmnvELPDSFSPELKSLLEGLLQRDVSKR 242
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
78-278 9.71e-13

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: 68.52  E-value: 9.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  78 KLLSSLKNPYIVHYEDSWIDnDNNACIFTAYYEGGNMANAIKkarGKLFPEERIFKWLAQLLLAVNYLHSNR---VVHMD 154
Cdd:cd14147   54 RLFAMLAHPNIIALKAVCLE-EPNLCLVMEYAAGGPLSRALA---GRRVPPHVLVNWAVQIARGMHYLHCEAlvpVIHRD 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 155 LTCSNIFLP--------KDDHVQLGNYGLAKLINPEKPVSmVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQP 226
Cdd:cd14147  130 LKSNNILLLqpienddmEHKTLKITDFGLAREWHKTTQMS-AAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEV 208
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 334185276 227 AFKAPDMAGL-----INKinrsLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELL 278
Cdd:cd14147  209 PYRGIDCLAVaygvaVNK----LTLPIPSTCPEPFAQLMADCWAQDPHRRPDFASIL 261
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
112-219 1.01e-12

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: 68.59  E-value: 1.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 112 GNMANAI-KKARGKLFpeERIFKWL-AQLLLAVNYLHSNRVVHMDLTCSNIFLPKDD---HVQLGNYGLAKLINPEKPVS 186
Cdd:cd14082   86 GDMLEMIlSSEKGRLP--ERITKFLvTQILVALRYLHSKNIVHCDLKPENVLLASAEpfpQVKLCDFGFARIIGEKSFRR 163
                         90       100       110
                 ....*....|....*....|....*....|...
gi 334185276 187 MVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMY 219
Cdd:cd14082  164 SVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIY 196
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
78-264 1.10e-12

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 69.62  E-value: 1.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  78 KLLSSLKNPYIVHYEDSWIDnDNNACIFTAYYEGGNMANAIKkaRGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTC 157
Cdd:PTZ00426  83 KILNYINHPFCVNLYGSFKD-ESYLYLVLEFVIGGEFFTFLR--RNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKP 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 158 SNIFLPKDDHVQLGNYGLAKLInpEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLI 237
Cdd:PTZ00426 160 ENLLLDKDGFIKMTDFGFAKVV--DTRTYTLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFYANEPLLIY 237
                        170       180
                 ....*....|....*....|....*..
gi 334185276 238 NKINRSLMSpLPIVYSSTLKQMIKLML 264
Cdd:PTZ00426 238 QKILEGIIY-FPKFLDNNCKHLMKKLL 263
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
108-271 1.16e-12

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: 69.26  E-value: 1.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 108 YYEGGNMANAIKKArGKlFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKlinpEKPVSM 187
Cdd:cd05616   82 YVNGGDLMYHIQQV-GR-FKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCK----ENIWDG 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 188 VS-----GISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSpLPIVYSSTLKQMIKL 262
Cdd:cd05616  156 VTtktfcGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVA-YPKSMSKEAVAICKG 234

                 ....*....
gi 334185276 263 MLRKKPEYR 271
Cdd:cd05616  235 LMTKHPGKR 243
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
129-278 1.18e-12

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: 68.52  E-value: 1.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 129 ERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEK----------PVSMvsgisnsMCPE 198
Cdd:cd05032  119 QKFIQMAAEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVKIGDFGMTRDIYETDyyrkggkgllPVRW-------MAPE 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 199 VLEDQPYGYKSDIWSLGCCMYEIT--AHQPafkapdMAGLINK------INRSLMsPLPIVYSSTLKQMIKLMLRKKPEY 270
Cdd:cd05032  192 SLKDGVFTTKSDVWSFGVVLWEMAtlAEQP------YQGLSNEevlkfvIDGGHL-DLPENCPDKLLELMRMCWQYNPKM 264

                 ....*...
gi 334185276 271 RPTACELL 278
Cdd:cd05032  265 RPTFLEIV 272
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
19-283 1.23e-12

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


Pssm-ID: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 68.06  E-value: 1.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  19 YHVVEQVRRGkSSSDFVVLHDIEDKKYAMKKIcLAKHTDKLKQtALQEISravinydLMKLLSSLKNP---YIVHYEDSW 95
Cdd:cd14133    1 YEVLEVLGKG-TFGQVVKCYDLLTGEEVALKI-IKNNKDYLDQ-SLDEIR-------LLELLNKKDKAdkyHIVRLKDVF 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  96 IdNDNNACIFTayyE--GGNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFL--PKDDHVQLG 171
Cdd:cd14133   71 Y-FKNHLCIVF---EllSQNLYEFLKQNKFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLasYSRCQIKII 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 172 NYGLAKLINPEKPVSMVSGISNSmcPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINrSLMSPLP-- 249
Cdd:cd14133  147 DFGSSCFLTQRLYSYIQSRYYRA--PEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARII-GTIGIPPah 223
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 334185276 250 -IVYSST----LKQMIKLMLRKKPEYRPTACELLRNPSL 283
Cdd:cd14133  224 mLDQGKAddelFVDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
78-278 1.25e-12

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: 68.53  E-value: 1.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  78 KLLSSLKNPYIVHYEDSWIdNDNNACIFTAYYEGGNMANAIKkarGKLFPEERIFKWLAQLLLAVNYLHSNRVV---HMD 154
Cdd:cd14145   57 KLFAMLKHPNIIALRGVCL-KEPNLCLVMEFARGGPLNRVLS---GKRIPPDILVNWAVQIARGMNYLHCEAIVpviHRD 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 155 LTCSNIF-LPKDDHVQLGN-------YGLAKLINPEKPVSmVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQP 226
Cdd:cd14145  133 LKSSNILiLEKVENGDLSNkilkitdFGLAREWHRTTKMS-AAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEV 211
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 334185276 227 AFKAPDMAGLINKINRSLMS-PLPIVYSSTLKQMIKLMLRKKPEYRPTACELL 278
Cdd:cd14145  212 PFRGIDGLAVAYGVAMNKLSlPIPSTCPEPFARLMEDCWNPDPHSRPPFTNIL 264
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
18-247 1.33e-12

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: 68.30  E-value: 1.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  18 NYHVVEQVRRGKsssdFVVLHDIEDKK----YAMKKICLAKHTDKLKQTALQEISravinydlmkLLSSLKNPYIVHYED 93
Cdd:cd07860    1 NFQKVEKIGEGT----YGVVYKARNKLtgevVALKKIRLDTETEGVPSTAIREIS----------LLKELNHPNIVKLLD 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  94 SwIDNDNNACIFTAYyeggnMANAIKK----ARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQ 169
Cdd:cd07860   67 V-IHTENKLYLVFEF-----LHQDLKKfmdaSALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIK 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 170 LGNYGLAKLINpeKPVSMVSGISNSM---CPEV-LEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLM 245
Cdd:cd07860  141 LADFGLARAFG--VPVRTYTHEVVTLwyrAPEIlLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLG 218

                 ..
gi 334185276 246 SP 247
Cdd:cd07860  219 TP 220
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
72-283 1.38e-12

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: 68.08  E-value: 1.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  72 INYDLMK---------LLSSLKNPYIVHYEDSWIDNDNNACIFTAYYEGGNMANAIKkaRGKLfPEERIFKWLAQLLLAV 142
Cdd:cd14113   40 VNKKLMKrdqvthelgVLQSLQHPQLVGLLDTFETPTSYILVLEMADQGRLLDYVVR--WGNL-TEEKIRFYLREILEAL 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 143 NYLHSNRVVHMDLTCSNIFL---PKDDHVQLGNYGLAKLINPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMY 219
Cdd:cd14113  117 QYLHNCRIAHLDLKPENILVdqsLSKPTIKLADFGDAVQLNTTYYIHQLLGSPEFAAPEIILGNPVSLTSDLWSIGVLTY 196
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334185276 220 EITAHQPAFKAPDMAGLINKINRsLMSPLPIVY----SSTLKQMIKLMLRKKPEYRPTACELLRNPSL 283
Cdd:cd14113  197 VLLSGVSPFLDESVEETCLNICR-LDFSFPDDYfkgvSQKAKDFVCFLLQMDPAKRPSAALCLQEQWL 263
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
108-271 1.39e-12

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: 69.26  E-value: 1.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 108 YYEGGNMANAIKKArGKlFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKlinpEKPVSM 187
Cdd:cd05615   92 YVNGGDLMYHIQQV-GK-FKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCK----EHMVEG 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 188 VS-----GISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSpLPIVYSSTLKQMIKL 262
Cdd:cd05615  166 VTtrtfcGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVS-YPKSLSKEAVSICKG 244

                 ....*....
gi 334185276 263 MLRKKPEYR 271
Cdd:cd05615  245 LMTKHPAKR 253
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
36-277 1.48e-12

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: 68.22  E-value: 1.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  36 VLHDIEDKKYAMK-KICLAKHTDKLKQTALQEISravinydLMKllsSLKNPYIVHYEDswIDNDNNACIFTAYYEGGNM 114
Cdd:cd05056   26 VYMSPENEKIAVAvKTCKNCTSPSVREKFLQEAY-------IMR---QFDHPHIVKLIG--VITENPVWIVMELAPLGEL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 115 ANAIKKARGKLfPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEK--PVSMVSGIS 192
Cdd:cd05056   94 RSYLQVNKYSL-DLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSRYMEDESyyKASKGKLPI 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 193 NSMCPEVLEDQPYGYKSDIWSLGCCMYEITAH--QPaFKAPDMAGLINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEY 270
Cdd:cd05056  173 KWMAPESINFRRFTSASDVWMFGVCMWEILMLgvKP-FQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSK 251

                 ....*..
gi 334185276 271 RPTACEL 277
Cdd:cd05056  252 RPRFTEL 258
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
135-286 1.50e-12

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: 68.39  E-value: 1.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 135 LAQLLL-------AVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNS----MCPEVLEDQ 203
Cdd:cd05080  106 LAQLLLfaqqiceGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAKAVPEGHEYYRVREDGDSpvfwYAPECLKEY 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 204 PYGYKSDIWSLGCCMYEITAHQPAFKAP-----DMAG----------LINKINRSLMSPLPIVYSSTLKQMIKLMLRKKP 268
Cdd:cd05080  186 KFYYASDVWSFGVTLYELLTHCDSSQSPptkflEMIGiaqgqmtvvrLIELLERGERLPCPDKCPQEVYHLMKNCWETEA 265
                        170
                 ....*....|....*...
gi 334185276 269 EYRPTACELLrnPSLQPY 286
Cdd:cd05080  266 SFRPTFENLI--PILKTV 281
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
86-281 1.62e-12

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: 68.09  E-value: 1.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  86 PYIVHYEDSWID-NDNNAC--IFTAYYEGGNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFL 162
Cdd:cd14172   57 PHIVHILDVYENmHHGKRCllIIMECMEGGELFSRIQERGDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLY 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 163 P---KDDHVQLGNYGLAKLINPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFK-------APD 232
Cdd:cd14172  137 TskeKDAVLKLTDFGFAKETTVQNALQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYsntgqaiSPG 216
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 334185276 233 MAGLINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd14172  217 MKRRIRMGQYGFPNPEWAEVSEEAKQLIRHLLKTDPTERMTITQFMNHP 265
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
137-300 1.86e-12

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: 68.74  E-value: 1.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 137 QLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINpekpvSMVSGISNSM-----------CPEVLEDQPY 205
Cdd:cd07852  115 QLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGLARSLS-----QLEEDDENPVltdyvatrwyrAPEILLGSTR 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 206 GYKS-DIWSLGCCMYEITAHQPAF-------------------KAPDMAG--------LINKINRSLMSPLPIVYSSTLK 257
Cdd:cd07852  190 YTKGvDMWSVGCILGEMLLGKPLFpgtstlnqlekiievigrpSAEDIESiqspfaatMLESLPPSRPKSLDELFPKASP 269
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 334185276 258 QMIKLM---LRKKPEYRPTACELLRNpslqPYLLQCQNLS-------PIYLPV 300
Cdd:cd07852  270 DALDLLkklLVFNPNKRLTAEEALRH----PYVAQFHNPAdepslpgPIVIPL 318
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
34-294 1.88e-12

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: 68.48  E-value: 1.88e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  34 FVVLHDIEDKKYAMKKICL-AKHTDKLKQTaLQEIsravinydlmKLLSSLKNPYIVHYEDSWIDNdNNACIFTAYYEGG 112
Cdd:cd08216   17 HLAKHKPTNTLVAVKKINLeSDSKEDLKFL-QQEI----------LTSRQLQHPNILPYVTSFVVD-NDLYVVTPLMAYG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 113 NMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAklinpekpVSMVS--- 189
Cdd:cd08216   85 SCRDLLKTHFPEGLPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYA--------YSMVKhgk 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 190 ----------GISNSMC---PEVLEDQPYGY--KSDIWSLGccmyeITA------HQPAFKAPDMAGLINKINRSLMSPL 248
Cdd:cd08216  157 rqrvvhdfpkSSEKNLPwlsPEVLQQNLLGYneKSDIYSVG-----ITAcelangVVPFSDMPATQMLLEKVRGTTPQLL 231
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185276 249 -----------------------------PIVYSSTL----KQMIKLMLRKKPEYRPTACELLRNPSLQpyllQCQNLS 294
Cdd:cd08216  232 dcstypleedsmsqsedsstehpnnrdtrDIPYQRTFseafHQFVELCLQRDPELRPSASQLLAHSFFK----QCRRSN 306
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
104-280 2.17e-12

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: 67.60  E-value: 2.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 104 IFTAYYEGGNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEK 183
Cdd:cd05067   78 IITEYMENGSLVDFLKTPSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLIEDNE 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 184 ---------PVSMVSgisnsmcPEVLEDQPYGYKSDIWSLGCCMYEITAH----QPAFKAPDmagLINKINRSLMSPLPI 250
Cdd:cd05067  158 ytaregakfPIKWTA-------PEAINYGTFTIKSDVWSFGILLTEIVTHgripYPGMTNPE---VIQNLERGYRMPRPD 227
                        170       180       190
                 ....*....|....*....|....*....|
gi 334185276 251 VYSSTLKQMIKLMLRKKPEYRPTAcELLRN 280
Cdd:cd05067  228 NCPEELYQLMRLCWKERPEDRPTF-EYLRS 256
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
36-279 2.98e-12

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: 66.96  E-value: 2.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  36 VLHDIEDKKYAMKKIclakHTDKLKQTA-LQEISravINYDLmkllSSlkNPYIVH-YEDSWIDNDnnACIFTA-YYEGG 112
Cdd:cd13987   12 AVHKGSGTKMALKFV----PKPSTKLKDfLREYN---ISLEL----SV--HPHIIKtYDVAFETED--YYVFAQeYAPYG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 113 NMANAIKKARGklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDD--HVQLGNYGLAKLINpeKPVSMVSG 190
Cdd:cd13987   77 DLFSIIPPQVG--LPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDcrRVKLCDFGLTRRVG--STVKRVSG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 191 ISNSMCPEVLEDQPYG-----YKSDIWSLG----CCM-----YEITAHQPAFKAPDMAGLinkinRSLMSPLPIVY---S 253
Cdd:cd13987  153 TIPYTAPEVCEAKKNEgfvvdPSIDVWAFGvllfCCLtgnfpWEKADSDDQFYEEFVRWQ-----KRKNTAVPSQWrrfT 227
                        250       260
                 ....*....|....*....|....*.
gi 334185276 254 STLKQMIKLMLRKKPEYRPTACELLR 279
Cdd:cd13987  228 PKALRMFKKLLAPEPERRCSIKEVFK 253
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
77-280 3.97e-12

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: 67.38  E-value: 3.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  77 MKLLSSLKNPYIVHYEDSWIdNDNNACIFTAYYEGGnmANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLT 156
Cdd:cd06635   76 VKFLQRIKHPNSIEYKGCYL-REHTAWLVMEYCLGS--ASDLLEVHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIK 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 157 CSNIFLPKDDHVQLGNYGLAKLINPEKpvSMVsGISNSMCPEV---LEDQPYGYKSDIWSLGCCMYEITAHQPA-FKAPD 232
Cdd:cd06635  153 AGNILLTEPGQVKLADFGSASIASPAN--SFV-GTPYWMAPEVilaMDEGQYDGKVDVWSLGITCIELAERKPPlFNMNA 229
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 334185276 233 MAGLINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRN 280
Cdd:cd06635  230 MSALYHIAQNESPTLQSNEWSDYFRNFVDSCLQKIPQDRPTSEELLKH 277
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
80-278 4.96e-12

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: 66.64  E-value: 4.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  80 LSSLKNPYIVHY--EDSWIDNDNNACIFTAYYEGGNMANAIKKARGKLFPEERIfKWLAQLLLAVNYLHSNRVVHMDLTC 157
Cdd:cd13979   53 AARLRHENIVRVlaAETGTDFASLGLIIMEYCGNGTLQQLIYEGSEPLPLAHRI-LISLDIARALRFCHSHGIVHLDVKP 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 158 SNIFLPKDDHVQLGNYGLAKLINP----EKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDM 233
Cdd:cd13979  132 ANILISEQGVCKLCDFGCSVKLGEgnevGTPRSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYAGLRQ 211
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 334185276 234 AGLINKINRSLMSPLPIVYSSTLKQ----MIKLMLRKKPEYRPTACELL 278
Cdd:cd13979  212 HVLYAVVAKDLRPDLSGLEDSEFGQrlrsLISRCWSAQPAERPNADESL 260
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
129-270 4.99e-12

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: 67.42  E-value: 4.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 129 ERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNSMCPEVLEDQPYGYK 208
Cdd:cd07874  119 ERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKEN 198
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334185276 209 SDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPLPiVYSSTLKQMIKLMLRKKPEY 270
Cdd:cd07874  199 VDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVIEQLGTPCP-EFMKKLQPTVRNYVENRPKY 259
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
42-286 5.11e-12

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: 67.50  E-value: 5.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  42 DKKYAMKKICLaKHTDKLKQtALQEIsravinydlmKLLSSLKNPYIVH-YE---DSWIDND---------NNACIFTAY 108
Cdd:cd07854   30 DKRVAVKKIVL-TDPQSVKH-ALREI----------KIIRRLDHDNIVKvYEvlgPSGSDLTedvgsltelNSVYIVQEY 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 109 YEGgNMANAIKKARgklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHV-QLGNYGLAKLINPEKPVS- 186
Cdd:cd07854   98 MET-DLANVLEQGP---LSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTEDLVlKIGDFGLARIVDPHYSHKg 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 187 -----MVSGISNSmcPE-VLEDQPYGYKSDIWSLGCCMYEITAHQPAF-------------------KAPDMAGLINKI- 240
Cdd:cd07854  174 ylsegLVTKWYRS--PRlLLSPNNYTKAIDMWAAGCIFAEMLTGKPLFagaheleqmqlilesvpvvREEDRNELLNVIp 251
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 334185276 241 ----------NRSLMSPLPIVYSSTLKQMIKlMLRKKPEYRPTACELLRNPSLQPY 286
Cdd:cd07854  252 sfvrndggepRRPLRDLLPGVNPEALDFLEQ-ILTFNPMDRLTAEEALMHPYMSCY 306
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
17-281 5.18e-12

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: 66.77  E-value: 5.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  17 DNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKiclakhtdkLKQTALQEISRAVINydlmkLLSSLKNPYIVHYEDSWi 96
Cdd:cd14085    3 DFFEIESELGRGATSVVYRCRQKGTQKPYAVKK---------LKKTVDKKIVRTEIG-----VLLRLSHPNIIKLKEIF- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  97 DNDNNACIFTAYYEGGNMANAIKKaRGkLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFL--PKDDH-VQLGNY 173
Cdd:cd14085   68 ETPTEISLVLELVTGGELFDRIVE-KG-YYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYatPAPDApLKIADF 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 174 GLAKLINPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMY-EITAHQPAFKAPDMAGLINKINR---SLMSPLP 249
Cdd:cd14085  146 GLSKIVDQQVTMKTVCGTPGYCAPEILRGCAYGPEVDMWSVGVITYiLLCGFEPFYDERGDQYMFKRILNcdyDFVSPWW 225
                        250       260       270
                 ....*....|....*....|....*....|..
gi 334185276 250 IVYSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd14085  226 DDVSLNAKDLVKKLIVLDPKKRLTTQQALQHP 257
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
45-228 5.45e-12

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: 67.25  E-value: 5.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  45 YAMKKIclaKHTDKLKQTALQEIsRAVINydlmkLLSSLKNPYIVHYEDSWIDNDNNACIFTaYYEGGNMANA-IKKarg 123
Cdd:cd05599   29 YAMKKL---RKSEMLEKEQVAHV-RAERD-----ILAEADNPWVVKLYYSFQDEENLYLIME-FLPGGDMMTLlMKK--- 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 124 KLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAK-LINPEKPVSMVsGISNSMCPEVLED 202
Cdd:cd05599   96 DTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGLCTgLKKSHLAYSTV-GTPDYIAPEVFLQ 174
                        170       180
                 ....*....|....*....|....*.
gi 334185276 203 QPYGYKSDIWSLGCCMYEITAHQPAF 228
Cdd:cd05599  175 KGYGKECDWWSLGVIMYEMLIGYPPF 200
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
17-281 5.89e-12

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: 66.08  E-value: 5.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  17 DNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAKhtdKLKQTALQEisravinydlMKLLSSLKNPYIVHYEDSWi 96
Cdd:cd14108    2 DYYDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPVRA---KKKTSARRE----------LALLAELDHKSIVRFHDAF- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  97 DNDNNACIFTayyEGGNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFL--PKDDHVQLGNYG 174
Cdd:cd14108   68 EKRRVVIIVT---ELCHEELLERITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMadQKTDQVRICDFG 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 175 LAKLINPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYE-ITAHQPAFKAPDMAGLINKINRSLMSPLPIVYS 253
Cdd:cd14108  145 NAQELTPNEPQYCKYGTPEFVAPEIVNQSPVSKVTDIWPVGVIAYLcLTGISPFVGENDRTTLMNIRNYNVAFEESMFKD 224
                        250       260       270
                 ....*....|....*....|....*....|.
gi 334185276 254 STLKQ---MIKLMLRKKpeYRPTACELLRNP 281
Cdd:cd14108  225 LCREAkgfIIKVLVSDR--LRPDAEETLEHP 253
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
104-273 6.03e-12

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: 66.32  E-value: 6.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 104 IFTAYYEGGNMANAIKKARGKLFPEERiFKWLAQLLLAVNYLH--SNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINP 181
Cdd:cd13978   69 LVMEYMENGSLKSLLEREIQDVPWSLR-FRIIHEIALGMNFLHnmDPPLLHHDLKPENILLDNHFHVKISDFGLSKLGMK 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 182 EKPVSMVSGISNS------MCPEVLEDQPY--GYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKI----NRSLMSPLP 249
Cdd:cd13978  148 SISANRRRGTENLggtpiyMAPEAFDDFNKkpTSKSDVYSFAIVIWAVLTRKEPFENAINPLLIMQIvskgDRPSLDDIG 227
                        170       180
                 ....*....|....*....|....*...
gi 334185276 250 IVY-SSTLKQMIKLMLR---KKPEYRPT 273
Cdd:cd13978  228 RLKqIENVQELISLMIRcwdGNPDARPT 255
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
46-247 6.89e-12

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: 66.29  E-value: 6.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  46 AMKKICLAKHTDKLKQTALQEISravinydlmkLLSSLKNPYIVHYEDSWIDNDNNACIFtayyEGGNMAnaIKK----- 120
Cdd:cd07861   29 AMKKIRLESEEEGVPSTAIREIS----------LLKELQHPNIVCLEDVLMQENRLYLVF----EFLSMD--LKKyldsl 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 121 ARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINpeKPVSMVSGISNSM---CP 197
Cdd:cd07861   93 PKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARAFG--IPVRVYTHEVVTLwyrAP 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 334185276 198 EVLEDQP-YGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSP 247
Cdd:cd07861  171 EVLLGSPrYSTPVDIWSIGTIFAEMATKKPLFHGDSEIDQLFRIFRILGTP 221
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
43-230 7.48e-12

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: 67.36  E-value: 7.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  43 KKYAMKKICLAKHTDKLKQTALQEISRAVINYDLmklLSSLKNPYIVHYEDSWIDNDNnacIFTA--YYEGGNMaNAIKK 120
Cdd:cd05600   31 RKKDTGEICALKIMKKKVLFKLNEVNHVLTERDI---LTTTNSPWLVKLLYAFQDPEN---VYLAmeYVPGGDF-RTLLN 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 121 ARGKLFPEERIFkWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAK-LINPEKPVSM------------ 187
Cdd:cd05600  104 NSGILSEEHARF-YIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGLASgTLSPKKIESMkirleevkntaf 182
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334185276 188 ------------------VSGISNS-------MCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKA 230
Cdd:cd05600  183 leltakerrniyramrkeDQNYANSvvgspdyMAPEVLRGEGYDLTVDYWSLGCILFECLVGFPPFSG 250
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
50-286 8.30e-12

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: 66.83  E-value: 8.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  50 ICLAKHTDKLKQTALQEI----SRAVI---NYDLMKLLSSLKNPYIVHYEDSWIDNDNNACIFTAYYegGNMANAIKKAR 122
Cdd:cd07856   26 VCSARDQLTGQNVAVKKImkpfSTPVLakrTYRELKLLKHLRHENIISLSDIFISPLEDIYFVTELL--GTDLHRLLTSR 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 123 gklfPEERIF--KWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEkpvsMVSGISNSM--CPE 198
Cdd:cd07856  104 ----PLEKQFiqYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLARIQDPQ----MTGYVSTRYyrAPE 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 199 V-LEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSP-------------------LP----IVYSS 254
Cdd:cd07856  176 ImLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDHVNQFSIITELLGTPpddvinticsentlrfvqsLPkrerVPFSE 255
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 334185276 255 TLKQ-------MIKLMLRKKPEYRPTACELLRNPSLQPY 286
Cdd:cd07856  256 KFKNadpdaidLLEKMLVFDPKKRISAAEALAHPYLAPY 294
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
100-283 9.15e-12

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: 65.82  E-value: 9.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 100 NNACIFTAYYEGGNMANA--IKKARGKLFPEERIFKWLAQlllAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAK 177
Cdd:cd14149   80 DNLAIVTQWCEGSSLYKHlhVQETKFQMFQLIDIARQTAQ---GMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAT 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 178 L---INPEKPVSMVSGISNSMCPEVL---EDQPYGYKSDIWSLGCCMYEI-TAHQPAFKAPDMAGLINKINRSLMSP-LP 249
Cdd:cd14149  157 VksrWSGSQQVEQPTGSILWMAPEVIrmqDNNPFSFQSDVYSYGIVLYELmTGELPYSHINNRDQIIFMVGRGYASPdLS 236
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 334185276 250 IVYSSTLKQMIKLM---LRKKPEYRPTACELLRNPSL 283
Cdd:cd14149  237 KLYKNCPKAMKRLVadcIKKVKEERPLFPQILSSIEL 273
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
98-281 1.05e-11

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: 65.80  E-value: 1.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  98 NDNNACIFTAYYEGGNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGL-A 176
Cdd:cd06636   90 HDDQLWLVMEFCGAGSVTDLVKNTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVsA 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 177 KLINPEKPVSMVSGISNSMCPEVLE-----DQPYGYKSDIWSLGccmyeITAHQPAFKAP---DMAGLinkinRSLM--- 245
Cdd:cd06636  170 QLDRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLG-----ITAIEMAEGAPplcDMHPM-----RALFlip 239
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 334185276 246 -SPLPIV----YSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd06636  240 rNPPPKLkskkWSKKFIDFIEGCLVKNYLSRPSTEQLLKHP 280
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
79-277 1.05e-11

Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated protein Triple Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLTK, also called zipper sterile-alpha-motif kinase (ZAK), contains a catalytic kinase domain and a leucine zipper. There are two alternatively-spliced variants, MLTK-alpha and MLTK-beta. MLTK-alpha contains a sterile-alpha-motif (SAM) at the C-terminus. MLTK regulates the c-Jun N-terminal kinase, extracellular signal-regulated kinase, p38 MAPK, and NF-kB pathways. ZAK is the MAP3K involved in the signaling cascade that leads to the ribotoxic stress response initiated by cellular damage due to Shiga toxins and ricin. It may also play a role in cell transformation and cancer development. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals.The MLTK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 64.98  E-value: 1.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  79 LLSSLKNPYIVHYEDSWIDNDNNaCIFTAYYEGGNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSN---RVVHMDL 155
Cdd:cd14060   35 ILSVLSHRNIIQFYGAILEAPNY-GIVTEYASYGSLFDYLNSNESEEMDMDQIMTWATDIAKGMHYLHMEapvKVIHRDL 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 156 TCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVsGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPD--- 232
Cdd:cd14060  114 KSRNVVIAADGVLKICDFGASRFHSHTTHMSLV-GTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPFKGLEglq 192
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 334185276 233 MAGLINKINRSLMSP--LPIVYSSTLKQMIKLMLRKKPEYRPTACEL 277
Cdd:cd14060  193 VAWLVVEKNERPTIPssCPRSFAELMRRCWEADVKERPSFKQIIGIL 239
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
99-284 1.42e-11

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: 65.51  E-value: 1.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  99 DNNACIFTAYYEGGNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGL-AK 177
Cdd:cd06637   81 DDQLWLVMEFCGAGSVTDLIKNTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVsAQ 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 178 LINPEKPVSMVSGISNSMCPEVLE-----DQPYGYKSDIWSLGccmyeITAHQPAFKAPDMAGLinKINRSLM----SPL 248
Cdd:cd06637  161 LDRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDFKSDLWSLG-----ITAIEMAEGAPPLCDM--HPMRALFliprNPA 233
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 334185276 249 PIV----YSSTLKQMIKLMLRKKPEYRPTACELLRNPSLQ 284
Cdd:cd06637  234 PRLkskkWSKKFQSFIESCLVKNHSQRPSTEQLMKHPFIR 273
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
46-284 1.48e-11

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: 65.81  E-value: 1.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  46 AMKKICLA-KHTDKLKQTALQEIsravinydlmKLLSSLKNPYIVHYEDSWIdNDNNACIFTAYYEGGnmANAIKKARGK 124
Cdd:cd06634   44 AIKKMSYSgKQSNEKWQDIIKEV----------KFLQKLRHPNTIEYRGCYL-REHTAWLVMEYCLGS--ASDLLEVHKK 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 125 LFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLInpeKPVSMVSGISNSMCPEV---LE 201
Cdd:cd06634  111 PLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGSASIM---APANSFVGTPYWMAPEVilaMD 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 202 DQPYGYKSDIWSLGCCMYEITAHQPA-FKAPDMAGLINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRN 280
Cdd:cd06634  188 EGQYDGKVDVWSLGITCIELAERKPPlFNMNAMSALYHIAQNESPALQSGHWSEYFRNFVDSCLQKIPQDRPTSDVLLKH 267

                 ....
gi 334185276 281 PSLQ 284
Cdd:cd06634  268 RFLL 271
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
78-279 1.61e-11

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: 65.01  E-value: 1.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  78 KLLSSLKNPYIVHYEDSWIdNDNNACIFTAYYEGGNMANAIKkarGKLFPEERIFKWLAQLLLAVNYLHSNRVV---HMD 154
Cdd:cd14148   45 RLFWMLQHPNIIALRGVCL-NPPHLCLVMEYARGGALNRALA---GKKVPPHVLVNWAVQIARGMNYLHNEAIVpiiHRD 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 155 LTCSNIFL--PKDDH------VQLGNYGLAKLINPEKPVSmVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQP 226
Cdd:cd14148  121 LKSSNILIlePIENDdlsgktLKITDFGLAREWHKTTKMS-AAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEV 199
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 334185276 227 AFKAPDMAGL-----INKinrsLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLR 279
Cdd:cd14148  200 PYREIDALAVaygvaMNK----LTLPIPSTCPEPFARLLEECWDPDPHGRPDFGSILK 253
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
66-242 1.69e-11

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: 65.53  E-value: 1.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  66 EISRAVINYDL--MKLLSSLKNPYIVHYEDSWIDnDNNACIFTAYYEGGNMANAIKKArGKLfPEERIFKWLAQLLLAVN 143
Cdd:cd06615   37 EIKPAIRNQIIreLKVLHECNSPYIVGFYGAFYS-DGEISICMEHMDGGSLDQVLKKA-GRI-PENILGKISIAVLRGLT 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 144 YLHSNR-VVHMDLTCSNIFLPKDDHVQLGNYGLA-KLINpekpvSMVS---GISNSMCPEVLEDQPYGYKSDIWSLGCCM 218
Cdd:cd06615  114 YLREKHkIMHRDVKPSNILVNSRGEIKLCDFGVSgQLID-----SMANsfvGTRSYMSPERLQGTHYTVQSDIWSLGLSL 188
                        170       180
                 ....*....|....*....|....
gi 334185276 219 YEITAHQPAFKAPDMAGLINKINR 242
Cdd:cd06615  189 VEMAIGRYPIPPPDAKELEAMFGR 212
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
30-281 1.72e-11

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


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 66.06  E-value: 1.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  30 SSSDFVVLHDIEdkKYAMKKICLAKHTDKLKQTALQEISRA-VINYDLMK-------LLSSLKNPYIVHYEDSwIDNDNN 101
Cdd:cd05610    2 SIEEFVIVKPIS--RGAFGKVYLGRKKNNSKLYAVKVVKKAdMINKNMVHqvqaerdALALSKSPFIVHLYYS-LQSANN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 102 ACIFTAYYEGGNMANAIkkARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKL--- 178
Cdd:cd05610   79 VYLVMEYLIGGDVKSLL--HIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKVtln 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 179 --IN--------------------PEKPVSMVS-----------------------------GISNSMCPEVLEDQPYGY 207
Cdd:cd05610  157 reLNmmdilttpsmakpkndysrtPGQVLSLISslgfntptpyrtpksvrrgaarvegerilGTPDYLAPELLLGKPHGP 236
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185276 208 KSDIWSLGCCMYEITAHQPAF--KAPDMAgLINKINRSLmsPLPI---VYSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd05610  237 AVDWWALGVCLFEFLTGIPPFndETPQQV-FQNILNRDI--PWPEgeeELSVNAQNAIEILLTMDPTKRAGLKELKQHP 312
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
75-221 2.05e-11

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: 64.74  E-value: 2.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  75 DLMKLLSSLKNPYIVHYEDswIDNDNNACIFTAYYEGGNMANAIKKARGKLFPEErIFKWLAQLLLAVNYLHSNRVVHMD 154
Cdd:cd05057   58 DEAYVMASVDHPHLVRLLG--ICLSSQVQLITQLMPLGCLLDYVRNHRDNIGSQL-LLNWCVQIAKGMSYLEEKRLVHRD 134
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 155 LTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNS---MCPEVLEDQPYGYKSDIWSLGCCMYEI 221
Cdd:cd05057  135 LAARNVLVKTPNHVKITDFGLAKLLDVDEKEYHAEGGKVPikwMALESIQYRIYTHKSDVWSYGVTVWEL 204
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
34-240 2.80e-11

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: 64.17  E-value: 2.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  34 FVVLHDIEDKKYAMK---KIcLAKHTDKLKQTALQEisravinydlMKLLSSLKNPYIVHYEDSwIDNDNNACIFTAYYE 110
Cdd:cd14190   17 FGKVHTCTEKRTGLKlaaKV-INKQNSKDKEMVLLE----------IQVMNQLNHRNLIQLYEA-IETPNEIVLFMEYVE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 111 GGNMANAIKKARGKLfPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFL-PKDDH-VQLGNYGLAKLINPEKPVSMV 188
Cdd:cd14190   85 GGELFERIVDEDYHL-TEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCvNRTGHqVKIIDFGLARRYNPREKLKVN 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 334185276 189 SGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKI 240
Cdd:cd14190  164 FGTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLNNV 215
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
104-273 2.90e-11

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: 63.84  E-value: 2.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 104 IFTAYYEGGNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLI---- 179
Cdd:cd05034   67 IVTELMSKGSLLDYLRTGEGRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGLARLIedde 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 180 -NPEK----PVSMVSgisnsmcPEVLEDQPYGYKSDIWSLGCCMYEITAH-QPAFkaPDMAG--LINKINRSLMSPLPIV 251
Cdd:cd05034  147 yTAREgakfPIKWTA-------PEAALYGRFTIKSDVWSFGILLYEIVTYgRVPY--PGMTNreVLEQVERGYRMPKPPG 217
                        170       180
                 ....*....|....*....|..
gi 334185276 252 YSSTLKQMIKLMLRKKPEYRPT 273
Cdd:cd05034  218 CPDELYDIMLQCWKKEPEERPT 239
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
17-232 3.06e-11

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: 64.69  E-value: 3.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  17 DNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLakhtdKLKQTALQEISRAvinydlMKLLSSLKNPYIVHYEDSWI 96
Cdd:cd06650    5 DDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHL-----EIKPAIRNQIIRE------LQVLHECNSPYIVGFYGAFY 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  97 dNDNNACIFTAYYEGGNMANAIKKArGKLfPEERIFKWLAQLLLAVNYL-HSNRVVHMDLTCSNIFLPKDDHVQLGNYGL 175
Cdd:cd06650   74 -SDGEISICMEHMDGGSLDQVLKKA-GRI-PEQILGKVSIAVIKGLTYLrEKHKIMHRDVKPSNILVNSRGEIKLCDFGV 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 334185276 176 AKLINPEKPVSMVsGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPD 232
Cdd:cd06650  151 SGQLIDSMANSFV-GTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIPPPD 206
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
78-282 3.14e-11

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


Pssm-ID: 271039 [Multi-domain]  Cd Length: 293  Bit Score: 64.45  E-value: 3.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  78 KLLSSLKNPYIVHYEDSWIDNDNNA-----CIFTAYYEGgNMANAIKK--ARGKLFPEE--RIFKWlaQLLLAVNYLHSN 148
Cdd:cd14137   49 QIMRRLKHPNIVKLKYFFYSSGEKKdevylNLVMEYMPE-TLYRVIRHysKNKQTIPIIyvKLYSY--QLFRGLAYLHSL 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 149 RVVHMDLTCSNIFL-PKDDHVQLGNYGLAKLINP-EKPVSMVsgisnsmC------PE-VLEDQPYGYKSDIWSLGCCMY 219
Cdd:cd14137  126 GICHRDIKPQNLLVdPETGVLKLCDFGSAKRLVPgEPNVSYI-------CsryyraPElIFGATDYTTAIDIWSAGCVLA 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 220 EITAHQPAFK---APDMAGLINKI------------NRSLMSP-LPIVYSSTLK------------QMIKLMLRKKPEYR 271
Cdd:cd14137  199 ELLLGQPLFPgesSVDQLVEIIKVlgtptreqikamNPNYTEFkFPQIKPHPWEkvfpkrtppdaiDLLSKILVYNPSKR 278
                        250
                 ....*....|.
gi 334185276 272 PTACELLRNPS 282
Cdd:cd14137  279 LTALEALAHPF 289
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
111-281 3.28e-11

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: 64.24  E-value: 3.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 111 GGNMANAIKK--ARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGL-AKLINPEKPVSM 187
Cdd:cd06639  108 GGSVTELVKGllKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVsAQLTSARLRRNT 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 188 VSGISNSMCPEVLE-----DQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPL--PIVYSSTLKQMI 260
Cdd:cd06639  188 SVGTPFWMAPEVIAceqqyDYSYDARCDVWSLGITAIELADGDPPLFDMHPVKALFKIPRNPPPTLlnPEKWCRGFSHFI 267
                        170       180
                 ....*....|....*....|.
gi 334185276 261 KLMLRKKPEYRPTACELLRNP 281
Cdd:cd06639  268 SQCLIKDFEKRPSVTHLLEHP 288
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
77-285 3.58e-11

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: 63.83  E-value: 3.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  77 MKLLSSLKNPYIVHYEDSWIDNDNNACIFTaYYEGGNMAnaikkARGKLFPEERIFKWLAQLLLA------VNYLHS--- 147
Cdd:cd14066   41 LEMLGRLRHPNLVRLLGYCLESDEKLLVYE-YMPNGSLE-----DRLHCHKGSPPLPWPQRLKIAkgiargLEYLHEecp 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 148 NRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPV---SMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEI-TA 223
Cdd:cd14066  115 PPIIHGDIKSSNILLDEDFEPKLTDFGLARLIPPSESVsktSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELlTG 194
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334185276 224 HQPAFKAPDMAGLinkinRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACE-LLR--------NPSLQP 285
Cdd:cd14066  195 KPAVDENRENASR-----KDLVEWVESKGKEELEDILDKRLVDDDGVEEEEVEaLLRlallctrsDPSLRP 260
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
76-287 4.87e-11

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: 63.60  E-value: 4.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  76 LMKLLSSLKN---PYIVHYE-------DSWIDNDNNACIFTAYYEggnmaNAIKKarGKLFPEERIFKWLAQLLLAVNYL 145
Cdd:cd06617   47 LMDLDISMRSvdcPYTVTFYgalfregDVWICMEVMDTSLDKFYK-----KVYDK--GLTIPEDILGKIAVSIVKALEYL 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 146 HSN-RVVHMDLTCSNIFLPKDDHVQLGNYGLA-KLINpekpvSMV----SGISNSMCPE----VLEDQPYGYKSDIWSLG 215
Cdd:cd06617  120 HSKlSVIHRDVKPSNVLINRNGQVKLCDFGISgYLVD-----SVAktidAGCKPYMAPErinpELNQKGYDVKSDVWSLG 194
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185276 216 CCMYEI-TAHQP--AFKAPdmaglINKINRSLMSPLPIV----YSSTLKQMIKLMLRKKPEYRPTACELLRNPSLQPYL 287
Cdd:cd06617  195 ITMIELaTGRFPydSWKTP-----FQQLKQVVEEPSPQLpaekFSPEFQDFVNKCLKKNYKERPNYPELLQHPFFELHL 268
PK_NRBP1 cd14034
Pseudokinase domain of Nuclear Receptor Binding Protein 1; The pseudokinase domain shows ...
80-283 5.10e-11

Pseudokinase domain of Nuclear Receptor Binding Protein 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. NRBP1, also called MLF1-adaptor molecule (MADM), was originally named based on the presence of nuclear binding and localization motifs prior to functional analyses. It is expressed ubiquitously and is found to localize in the cytoplasm, not the nucleus. NRBP1 is an adaptor protein that interacts with myeloid leukemia factor 1 (MLF1), an oncogene that enhances myeloid development of hematopoietic cells. It also interacts with the small GTPase Rac3. NRBP1 may also be involved in Golgi to ER trafficking and actin dynamics. The NRBP1-like 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: 270936 [Multi-domain]  Cd Length: 277  Bit Score: 63.61  E-value: 5.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  80 LSSLKNPYIVHYEDSWID---NDNNACIFTAYYEGGNMANAIKKARG--KLFPEERIFKWLAQLLLAVNYLHS--NRVVH 152
Cdd:cd14034   64 LIQLEHLNIVKFHKYWADvkeNRARVIFITEYMSSGSLKQFLKKTKKnhKTMNEKAWKRWCTQILSALSYLHScdPPIIH 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 153 MDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCC-----MYEITAHQPA 227
Cdd:cd14034  144 GNLTCDTIFIQHNGLIKIGSVAPDTINNHVKTCREEQKNLHFFAPEYGEVANVTTAVDIYSFGMCalemaVLEIQGNGES 223
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 334185276 228 FKAPDMAglINKINRSLMSPLPivysstlKQMIKLMLRKKPEYRPTACELLRNPSL 283
Cdd:cd14034  224 SYVPQEA--INSAIQLLEDPLQ-------REFIQKCLEVDPSKRPTARELLFHQAL 270
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
131-315 6.95e-11

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: 63.50  E-value: 6.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 131 IFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGIS---NSMCPEVLEDQPYGY 207
Cdd:cd05108  111 LLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKvpiKWMALESILHRIYTH 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 208 KSDIWSLGCCMYEIT--AHQP--AFKAPDMAGLINKINRsLMSPlPIVYSSTLKQMIKLML---RKKPEYRPTACE---L 277
Cdd:cd05108  191 QSDVWSYGVTVWELMtfGSKPydGIPASEISSILEKGER-LPQP-PICTIDVYMIMVKCWMidaDSRPKFRELIIEfskM 268
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 334185276 278 LRNPslQPYLLqCQNLSPIYLPvfpiKPVNSPKDKARR 315
Cdd:cd05108  269 ARDP--QRYLV-IQGDERMHLP----SPTDSNFYRALM 299
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
42-220 7.01e-11

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: 63.36  E-value: 7.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  42 DKKYAMKKICL---AKHTDKLKQTALQEIsravinydlmKLLSSLKNPYIVhyedSWID---NDNNACIFTAYYEGGnmA 115
Cdd:cd07841   25 GRIVAIKKIKLgerKEAKDGINFTALREI----------KLLQELKHPNII----GLLDvfgHKSNINLVFEFMETD--L 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 116 NAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLI-NPekPVSMVSGISNS 194
Cdd:cd07841   89 EKVIKDKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLARSFgSP--NRKMTHQVVTR 166
                        170       180       190
                 ....*....|....*....|....*....|...
gi 334185276 195 M--CPEVLedqpYGYKS-----DIWSLGCCMYE 220
Cdd:cd07841  167 WyrAPELL----FGARHygvgvDMWSVGCIFAE 195
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
129-270 7.32e-11

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: 63.91  E-value: 7.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 129 ERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNSMCPEVLEDQPYGYK 208
Cdd:cd07875  126 ERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKEN 205
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334185276 209 SDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPLPiVYSSTLKQMIKLMLRKKPEY 270
Cdd:cd07875  206 VDIWSVGCIMGEMIKGGVLFPGTDHIDQWNKVIEQLGTPCP-EFMKKLQPTVRTYVENRPKY 266
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
99-271 7.39e-11

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: 63.86  E-value: 7.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  99 DNNACIFTAYYEGGNMANAIKKargKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKL 178
Cdd:cd05589   74 PEHVCFVMEYAAGGDLMMHIHE---DVFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKE 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 179 -INPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKI-NRSLmsPLPIVYSSTL 256
Cdd:cd05589  151 gMGFGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIvNDEV--RYPRFLSTEA 228
                        170
                 ....*....|....*
gi 334185276 257 KQMIKLMLRKKPEYR 271
Cdd:cd05589  229 ISIMRRLLRKNPERR 243
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
124-281 8.57e-11

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: 63.06  E-value: 8.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 124 KLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLA-KLINPEKPVSMVSGISNSMCPEVLED 202
Cdd:cd14199  121 KPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLVGEDGHIKIADFGVSnEFEGSDALLTNTVGTPAFMAPETLSE 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 203 QP---YGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKI-NRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELL 278
Cdd:cd14199  201 TRkifSGKALDVWAMGVTLYCFVFGQCPFMDERILSLHSKIkTQPLEFPDQPDISDDLKDLLFRMLDKNPESRISVPEIK 280

                 ...
gi 334185276 279 RNP 281
Cdd:cd14199  281 LHP 283
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
77-227 8.79e-11

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: 62.51  E-value: 8.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  77 MKLLSSLKNPYIVHYEDSWIdNDNNACIFTAYYEGGNMANAIKKARGKLfpeerifKWLAQLLLAVN------YLHSNRV 150
Cdd:cd14065   39 VKLMRRLSHPNILRFIGVCV-KDNKLNFITEYVNGGTLEELLKSMDEQL-------PWSQRVSLAKDiasgmaYLHSKNI 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 151 VHMDLTCSNIFLPKDD---HVQLGNYGLAKLI------NPE--KPVSMVsGISNSMCPEVLEDQPYGYKSDIWSLGCCMY 219
Cdd:cd14065  111 IHRDLNSKNCLVREANrgrNAVVADFGLAREMpdektkKPDrkKRLTVV-GSPYWMAPEMLRGESYDEKVDVFSFGIVLC 189

                 ....*...
gi 334185276 220 EITAHQPA 227
Cdd:cd14065  190 EIIGRVPA 197
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
41-228 1.18e-10

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: 63.16  E-value: 1.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  41 EDKKYAMKKIclakHTDKLKQTALQEISravinydlmkLLSSLKNPYIVHYEDSWIDNDNNACIFTAYYEGGNMANAIKK 120
Cdd:cd07867   28 DEKEYALKQI----EGTGISMSACREIA----------LLRELKHPNVIALQKVFLSHSDRKVWLLFDYAEHDLWHIIKF 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 121 ARGK-------LFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFL----PKDDHVQLGNYGLAKLIN-PEKPVSMV 188
Cdd:cd07867   94 HRASkankkpmQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNsPLKPLADL 173
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 334185276 189 SGISNSM---CPEVLEDQPYGYKS-DIWSLGCCMYEITAHQPAF 228
Cdd:cd07867  174 DPVVVTFwyrAPELLLGARHYTKAiDIWAIGCIFAELLTSEPIF 217
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
36-302 1.24e-10

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: 62.27  E-value: 1.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  36 VLHDIEDKKYAMKKicLAKHTDKLKQTALQEIsravinydlmKLLSSLKNPYI-----VHYEDSWIDndnnacIFTAYYE 110
Cdd:cd14222   12 VTHKATGKVMVMKE--LIRCDEETQKTFLTEV----------KVMRSLDHPNVlkfigVLYKDKRLN------LLTEFIE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 111 GGNMANAIKKArgKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLI-------NPEK 183
Cdd:cd14222   74 GGTLKDFLRAD--DPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveekkkpPPDK 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 184 PVS--------------MVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHqpAFKAPDMaglinkinrslmspLP 249
Cdd:cd14222  152 PTTkkrtlrkndrkkryTVVGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCEIIGQ--VYADPDC--------------LP 215
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 334185276 250 IVYSSTLKqmIKLMLRKkpeYRPTACEllrnPSLQPYLLQCQNLSPIYLPVFP 302
Cdd:cd14222  216 RTLDFGLN--VRLFWEK---FVPKDCP----PAFFPLAAICCRLEPDSRPAFS 259
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
129-278 1.40e-10

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 63.12  E-value: 1.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 129 ERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNSMCPEVLEDQPYGYK 208
Cdd:cd07876  123 ERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTACTNFMMTPYVVTRYYRAPEVILGMGYKEN 202
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 209 SDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPlPIVYSSTLKQMIKLMLRKKPEYRPTACELL 278
Cdd:cd07876  203 VDIWSVGCIMGELVKGSVIFQGTDHIDQWNKVIEQLGTP-SAEFMNRLQPTVRNYVENRPQYPGISFEEL 271
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
16-274 1.57e-10

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: 62.33  E-value: 1.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  16 LDNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLaKHTDKLKQTALQEISravinydlmkLLSSLKNPYIV------ 89
Cdd:cd07873    1 LETYIKLDKLGEGTYATVYKGRSKLTDNLVALKEIRL-EHEEGAPCTAIREVS----------LLKDLKHANIVtlhdii 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  90 HYEDS------WIDNDnnaciFTAYYEggNMANAIKKARGKLFpeerifkwLAQLLLAVNYLHSNRVVHMDLTCSNIFLP 163
Cdd:cd07873   70 HTEKSltlvfeYLDKD-----LKQYLD--DCGNSINMHNVKLF--------LFQLLRGLAYCHRRKVLHRDLKPQNLLIN 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 164 KDDHVQLGNYGLAKLIN-PEKPVSMVSGISNSMCPEV-LEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKIN 241
Cdd:cd07873  135 ERGELKLADFGLARAKSiPTKTYSNEVVTLWYRPPDIlLGSTDYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEQLHFIF 214
                        250       260       270
                 ....*....|....*....|....*....|...
gi 334185276 242 RSLMSPLPIVYSSTLKQMiKLMLRKKPEYRPTA 274
Cdd:cd07873  215 RILGTPTEETWPGILSNE-EFKSYNYPKYRADA 246
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
46-249 1.61e-10

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: 62.76  E-value: 1.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  46 AMKKICLAKHTDKLKQTALQEISR-------AVINYDLMKLLSSLKNPYIVHYEDSW-----IDNDNNACIFTAYYeGGN 113
Cdd:cd07878   27 AYGSVCSAYDTRLRQKVAVKKLSRpfqslihARRTYRELRLLKHMKHENVIGLLDVFtpatsIENFNEVYLVTNLM-GAD 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 114 MANAIKKARgklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEkpvsMVSGISN 193
Cdd:cd07878  106 LNNIVKCQK---LSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLARQADDE----MTGYVAT 178
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 334185276 194 S--MCPEVLED-QPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPLP 249
Cdd:cd07878  179 RwyRAPEIMLNwMHYNQTVDIWSVGCIMAELLKGKALFPGNDYIDQLKRIMEVVGTPSP 237
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
78-278 1.66e-10

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: 62.02  E-value: 1.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  78 KLLSSLKNPYIVHYEDSWIDN-DNNACIF--TAYYEGGNMANAIKkaRGKLFPEERIFKWLAQLLLAVNYLHSNR--VVH 152
Cdd:cd14032   52 EMLKGLQHPNIVRFYDFWESCaKGKRCIVlvTELMTSGTLKTYLK--RFKVMKPKVLRSWCRQILKGLLFLHTRTppIIH 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 153 MDLTCSNIFLP-KDDHVQLGNYGLAKLINPEKPVSMVsGISNSMCPEVLEDQpYGYKSDIWSLGCCMYEI-TAHQPAFKA 230
Cdd:cd14032  130 RDLKCDNIFITgPTGSVKIGDLGLATLKRASFAKSVI-GTPEFMAPEMYEEH-YDESVDVYAFGMCMLEMaTSEYPYSEC 207
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 334185276 231 PDMAGLINKINRSLM-SPLPIVYSSTLKQMIKLMLRKKPEYRPTACELL 278
Cdd:cd14032  208 QNAAQIYRKVTCGIKpASFEKVTDPEIKEIIGECICKNKEERYEIKDLL 256
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
137-247 1.68e-10

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: 62.81  E-value: 1.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 137 QLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINP---EKPVSMVSGISNS--MCPEV-LEDQPYGYKSD 210
Cdd:cd07857  113 QILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLARGFSEnpgENAGFMTEYVATRwyRAPEImLSFQSYTKAID 192
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 334185276 211 IWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSP 247
Cdd:cd07857  193 VWSVGCILAELLGRKPVFKGKDYVDQLNQILQVLGTP 229
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
137-281 1.71e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 62.97  E-value: 1.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 137 QLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGC 216
Cdd:PHA03209 165 QILEGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLGAAQFPVVAPAFLGLAGTVETNAPEVLARDKYNSKADIWSAGI 244
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 217 CMYEITAH-QPAFKAPDMAG----------LINKINRSLMSP--LP-----------IVYSSTLKQ-------------- 258
Cdd:PHA03209 245 VLFEMLAYpSTIFEDPPSTPeeyvkschshLLKIISTLKVHPeeFPrdpgsrlvrgfIEYASLERQpytrypcfqrvnlp 324
                        170       180
                 ....*....|....*....|....*...
gi 334185276 259 -----MIKLMLRKKPEYRPTACELLRNP 281
Cdd:PHA03209 325 idgefLVHKMLTFDAAMRPSAEEILNYP 352
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
79-231 1.83e-10

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: 62.72  E-value: 1.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  79 LLSSLKNPYIVHYEDSWIDNDNNACIFTaYYEGGN-MANAIKKArgkLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTC 157
Cdd:cd05598   54 ILAEADNEWVVKLYYSFQDKENLYFVMD-YIPGGDlMSLLIKKG---IFEEDLARFYIAELVCAIESVHKMGFIHRDIKP 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 158 SNIFLPKDDHVQLGNYGL--------------AKlinpekpvSMVsGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITA 223
Cdd:cd05598  130 DNILIDRDGHIKLTDFGLctgfrwthdskyylAH--------SLV-GTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLV 200

                 ....*...
gi 334185276 224 HQPAFKAP 231
Cdd:cd05598  201 GQPPFLAQ 208
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
41-228 1.94e-10

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: 62.38  E-value: 1.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  41 EDKKYAMKKIclakHTDKLKQTALQEISravinydlmkLLSSLKNPYIVHYEDSWIDNDNNACIFTAYYEGGNMANAIKK 120
Cdd:cd07868   43 DDKDYALKQI----EGTGISMSACREIA----------LLRELKHPNVISLQKVFLSHADRKVWLLFDYAEHDLWHIIKF 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 121 ARGK-------LFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFL----PKDDHVQLGNYGLAKLIN-PEKPVSMV 188
Cdd:cd07868  109 HRASkankkpvQLPRGMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNsPLKPLADL 188
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 334185276 189 SGISNSM---CPEVLEDQPYGYKS-DIWSLGCCMYEITAHQPAF 228
Cdd:cd07868  189 DPVVVTFwyrAPELLLGARHYTKAiDIWAIGCIFAELLTSEPIF 232
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
75-286 1.95e-10

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: 62.01  E-value: 1.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  75 DLMKLLSSLKNPYIVHYEDSWIDNDNnacIFTAYYEGGNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNR-VVHM 153
Cdd:cd06618   63 DLDVVLKSHDCPYIVKCYGYFITDSD---VFICMELMSTCLDKLLKRIQGPIPEDILGKMTVSIVKALHYLKEKHgVIHR 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 154 DLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNSMCPEVLEDQP---YGYKSDIWSLGCCMYEITAHQPAFKA 230
Cdd:cd06618  140 DVKPSNILLDESGNVKLCDFGISGRLVDSKAKTRSAGCAAYMAPERIDPPDnpkYDIRADVWSLGISLVELATGQFPYRN 219
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334185276 231 PDMAglINKINRSLMSPLPIV-----YSSTLKQMIKLMLRKKPEYRPTACELLRNPSLQPY 286
Cdd:cd06618  220 CKTE--FEVLTKILNEEPPSLppnegFSPDFCSFVDLCLTKDHRYRPKYRELLQHPFIRRY 278
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
28-221 2.11e-10

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: 61.54  E-value: 2.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  28 GKSSSDFVVLHDIEDKKYAMKKIclaKHtDKLKQTALQEISravinydlmkLLSSLKNPYIVHYEDSWIDNDNNACIFTA 107
Cdd:cd05082   15 GKGEFGDVMLGDYRGNKVAVKCI---KN-DATAQAFLAEAS----------VMTQLRHSNLVQLLGVIVEEKGGLYIVTE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 108 YYEGGNMANAIKkARGK-LFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEK--- 183
Cdd:cd05082   81 YMAKGSLVDYLR-SRGRsVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEASSTQdtg 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 334185276 184 --PVSMVSgisnsmcPEVLEDQPYGYKSDIWSLGCCMYEI 221
Cdd:cd05082  160 klPVKWTA-------PEALREKKFSTKSDVWSFGILLWEI 192
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
127-221 3.00e-10

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: 61.90  E-value: 3.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 127 PEERI-FKWLA----QLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLA----------KLINPEKPVSMvsgi 191
Cdd:cd05099  127 PEEQLsFKDLVscayQVARGMEYLESRRCIHRDLAARNVLVTEDNVMKIADFGLArgvhdidyykKTSNGRLPVKW---- 202
                         90       100       110
                 ....*....|....*....|....*....|
gi 334185276 192 snsMCPEVLEDQPYGYKSDIWSLGCCMYEI 221
Cdd:cd05099  203 ---MAPEALFDRVYTHQSDVWSFGILMWEI 229
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
126-286 3.01e-10

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: 61.61  E-value: 3.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 126 FPEERIFKWLAQLLLAVNYLHSN-RVVHMDLTCSNIFLPKDDHVQLGNYGLA-KLINPEKPvSMVSGISNSMCPEVLE-- 201
Cdd:cd06616  106 IPEEILGKIAVATVKALNYLKEElKIIHRDVKPSNILLDRNGNIKLCDFGISgQLVDSIAK-TRDAGCRPYMAPERIDps 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 202 --DQPYGYKSDIWSLGCCMYEITAHQpaFKAPDMAGLINKINRSLMSPLPI-------VYSSTLKQMIKLMLRKKPEYRP 272
Cdd:cd06616  185 asRDGYDVRSDVWSLGITLYEVATGK--FPYPKWNSVFDQLTQVVKGDPPIlsnseerEFSPSFVNFVNLCLIKDESKRP 262
                        170
                 ....*....|....
gi 334185276 273 TACELLRNPSLQPY 286
Cdd:cd06616  263 KYKELLKHPFIKMY 276
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
104-273 3.06e-10

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: 60.91  E-value: 3.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 104 IFTAYYEGGNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEK 183
Cdd:cd05148   79 IITELMEKGSLLAFLRSPEGQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLARLIKEDV 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 184 PVSMVSGISNS-MCPEVLEDQPYGYKSDIWSLGCCMYEITAH-QPAFKAPDMAGLINKINRSLMSPLPIVYSSTLKQMIK 261
Cdd:cd05148  159 YLSSDKKIPYKwTAPEAASHGTFSTKSDVWSFGILLYEMFTYgQVPYPGMNNHEVYDQITAGYRMPCPAKCPQEIYKIML 238
                        170
                 ....*....|..
gi 334185276 262 LMLRKKPEYRPT 273
Cdd:cd05148  239 ECWAAEPEDRPS 250
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
127-226 3.32e-10

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: 61.23  E-value: 3.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 127 PEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPekPVSMVSGISNSM---CPEVL-ED 202
Cdd:cd07847   98 PEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARILTG--PGDDYTDYVATRwyrAPELLvGD 175
                         90       100
                 ....*....|....*....|....
gi 334185276 203 QPYGYKSDIWSLGCCMYEITAHQP 226
Cdd:cd07847  176 TQYGPPVDVWAIGCVFAELLTGQP 199
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
93-283 4.45e-10

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: 60.28  E-value: 4.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  93 DSWIDNDNNACIFTAYYegGNMANAIKkaRGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGN 172
Cdd:cd14024   52 EVVIGQDRAYAFFSRHY--GDMHSHVR--RRRRLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDELRTKLVL 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 173 YGLAK---LINPEKPVSMVSGISNSMCPEVLEDQP--YGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSp 247
Cdd:cd14024  128 VNLEDscpLNGDDDSLTDKHGCPAYVGPEILSSRRsySGKAADVWSLGVCLYTMLLGRYPFQDTEPAALFAKIRRGAFS- 206
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 334185276 248 LPIVYSSTLKQMIKLMLRKKPEYRPTACELLRNPSL 283
Cdd:cd14024  207 LPAWLSPGARCLVSCMLRRSPAERLKASEILLHPWL 242
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
19-281 4.91e-10

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: 60.24  E-value: 4.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  19 YHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKIclakHTDKLkqtalqeiSRAVINYDLmKLLSSLKNPYIVHYEDSWiDN 98
Cdd:cd14087    3 YDIKALIGRGSFSRVVRVEHRVTRQPYAIKMI----ETKCR--------GREVCESEL-NVLRRVRHTNIIQLIEVF-ET 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  99 DNNACIFTAYYEGGNMANAIKkARGKlFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFL--PK-DDHVQLGNYGL 175
Cdd:cd14087   69 KERVYMVMELATGGELFDRII-AKGS-FTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYyhPGpDSKIMITDFGL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 176 A--KLINPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMS----PLP 249
Cdd:cd14087  147 AstRKKGPNCLMKTTCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSysgePWP 226
                        250       260       270
                 ....*....|....*....|....*....|..
gi 334185276 250 IVySSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd14087  227 SV-SNLAKDFIDRLLTVNPGERLSATQALKHP 257
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
126-286 5.25e-10

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: 61.23  E-value: 5.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 126 FPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLI--NPEKPVS-MVSGISNS--MCPEVL 200
Cdd:cd07855  106 LTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMARGLctSPEEHKYfMTEYVATRwyRAPELM 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 201 EDQP-YGYKSDIWSLGCCMYEITAHQPAFKAPDMAG---------------LINKIN----RSLMSPLP--------IVY 252
Cdd:cd07855  186 LSLPeYTQAIDMWSVGCIFAEMLGRRQLFPGKNYVHqlqliltvlgtpsqaVINAIGadrvRRYIQNLPnkqpvpweTLY 265
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 334185276 253 SSTLKQMIKL---MLRKKPEYRPTACELLRNPSLQPY 286
Cdd:cd07855  266 PKADQQALDLlsqMLRFDPSERITVAEALQHPFLAKY 302
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
120-225 6.02e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 61.63  E-value: 6.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 120 KARGKLFPEERIFKwlaQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLI-NPEKP-----VSMVSgiSN 193
Cdd:PHA03210 261 KDRPLLKQTRAIMK---QLLCAVEYIHDKKLIHRDIKLENIFLNCDGKIVLGDFGTAMPFeKEREAfdygwVGTVA--TN 335
                         90       100       110
                 ....*....|....*....|....*....|..
gi 334185276 194 SmcPEVLEDQPYGYKSDIWSLGCCMYEITAHQ 225
Cdd:PHA03210 336 S--PEILAGDGYCEITDIWSCGLILLDMLSHD 365
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
137-231 7.00e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 61.45  E-value: 7.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 137 QLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNSM---CPEVLEDQPYGYKSDIWS 213
Cdd:PHA03211 268 QLLSAIDYIHGEGIIHRDIKTENVLVNGPEDICLGDFGAACFARGSWSTPFHYGIAGTVdtnAPEVLAGDPYTPSVDIWS 347
                         90
                 ....*....|....*....
gi 334185276 214 LGCCMYEITAHQPA-FKAP 231
Cdd:PHA03211 348 AGLVIFEAAVHTASlFSAS 366
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
104-273 7.03e-10

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: 60.05  E-value: 7.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 104 IFTAYYEGGNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEK 183
Cdd:cd05072   79 IITEYMAKGSLLDFLKSDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIEDNE 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 184 ---------PVSMVSgisnsmcPEVLEDQPYGYKSDIWSLGCCMYEI-TAHQPAFKAPDMAGLINKINRSLMSPLPIVYS 253
Cdd:cd05072  159 ytaregakfPIKWTA-------PEAINFGSFTIKSDVWSFGILLYEIvTYGKIPYPGMSNSDVMSALQRGYRMPRMENCP 231
                        170       180
                 ....*....|....*....|
gi 334185276 254 STLKQMIKLMLRKKPEYRPT 273
Cdd:cd05072  232 DELYDIMKTCWKEKAEERPT 251
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
54-281 7.13e-10

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: 60.43  E-value: 7.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  54 KHTDKLKQTALQEISRAVINYDLMKLLSSLknPYIVHYEDSWID-NDNNAC--IFTAYYEGGNMANAIKKARGKLFPEER 130
Cdd:cd14170   25 RTQEKFALKMLQDCPKARREVELHWRASQC--PHIVRIVDVYENlYAGRKCllIVMECLDGGELFSRIQDRGDQAFTERE 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 131 IFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPK---DDHVQLGNYGLAKLINPEKPVSMVSGISNSMCPEVLEDQPYGY 207
Cdd:cd14170  103 ASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSkrpNAILKLTDFGFAKETTSHNSLTTPCYTPYYVAPEVLGPEKYDK 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 208 KSDIWSLGCCMYEITAHQPAFK-------APDMAGLINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRN 280
Cdd:cd14170  183 SCDMWSLGVIMYILLCGYPPFYsnhglaiSPGMKTRIRMGQYEFPNPEWSEVSEEVKMLIRNLLKTEPTQRMTITEFMNH 262

                 .
gi 334185276 281 P 281
Cdd:cd14170  263 P 263
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
66-232 7.50e-10

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: 60.83  E-value: 7.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  66 EISRAVINYDL--MKLLSSLKNPYIVHYEDSWIdNDNNACIFTAYYEGGNMANAIKKARgkLFPEERIFKWLAQLLLAVN 143
Cdd:cd06649   41 EIKPAIRNQIIreLQVLHECNSPYIVGFYGAFY-SDGEISICMEHMDGGSLDQVLKEAK--RIPEEILGKVSIAVLRGLA 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 144 YL-HSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVsGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEIT 222
Cdd:cd06649  118 YLrEKHQIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMANSFV-GTRSYMSPERLQGTHYSVQSDIWSMGLSLVELA 196
                        170
                 ....*....|
gi 334185276 223 AHQPAFKAPD 232
Cdd:cd06649  197 IGRYPIPPPD 206
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
109-278 7.67e-10

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: 60.04  E-value: 7.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 109 YEGGNMANAIKKARGKLfPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINP--EKPVS 186
Cdd:cd06646   87 YCGGGSLQDIYHVTGPL-SELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAAKITAtiAKRKS 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 187 MVsGISNSMCPEVL---EDQPYGYKSDIWSLGCCMYEITAHQPA-FKAPDMAGLINKINRSLMSPL---PIVYSSTLKQM 259
Cdd:cd06646  166 FI-GTPYWMAPEVAaveKNGGYNQLCDIWAVGITAIELAELQPPmFDLHPMRALFLMSKSNFQPPKlkdKTKWSSTFHNF 244
                        170
                 ....*....|....*....
gi 334185276 260 IKLMLRKKPEYRPTACELL 278
Cdd:cd06646  245 VKISLTKNPKKRPTAERLL 263
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
76-279 7.74e-10

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: 59.96  E-value: 7.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  76 LMKLL-SSLKNPYIVHYEDSWIdndnnaCIFTAYYEGGNMANAIKKARGKlFPEERIFKWLAQLLLAVNYLHSNRVVHMD 154
Cdd:cd05112   53 MMKLShPKLVQLYGVCLEQAPI------CLVFEFMEHGCLSDYLRTQRGL-FSAETLLGMCLDVCEGMAYLEEASVIHRD 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 155 LTCSNIFLPKDDHVQLGNYGLAKLINPEK---------PVSMVSgisnsmcPEVLEDQPYGYKSDIWSLGCCMYEITAH- 224
Cdd:cd05112  126 LAARNCLVGENQVVKVSDFGMTRFVLDDQytsstgtkfPVKWSS-------PEVFSFSRYSSKSDVWSFGVLMWEVFSEg 198
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 334185276 225 QPAFKAPDMAGLINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLR 279
Cdd:cd05112  199 KIPYENRSNSEVVEDINAGFRLYKPRLASTHVYEIMNHCWKERPEDRPSFSLLLR 253
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
103-280 7.86e-10

Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Tec-like subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases form the second largest subfamily of nonreceptor PTKs and are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. Tec kinases play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. Mutations in Btk cause the severe B-cell immunodeficiency, X-linked agammaglobulinaemia (XLA). The Tec-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 59.77  E-value: 7.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 103 CIFTAYYEGGNMANAIKKARGKlFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPE 182
Cdd:cd05059   75 FIVTEYMANGCLLNYLRERRGK-FQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLARYVLDD 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 183 KPVSMVSG---ISNSmCPEVLEDQPYGYKSDIWSLGCCMYEI-TAHQPAFKAPDMAGLINKINRSLMSPLPIVYSSTLKQ 258
Cdd:cd05059  154 EYTSSVGTkfpVKWS-PPEVFMYSKFSSKSDVWSFGVLMWEVfSEGKMPYERFSNSEVVEHISQGYRLYRPHLAPTEVYT 232
                        170       180
                 ....*....|....*....|..
gi 334185276 259 MIKLMLRKKPEYRPTACELLRN 280
Cdd:cd05059  233 IMYSCWHEKPEERPTFKILLSQ 254
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
31-232 9.62e-10

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: 59.61  E-value: 9.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  31 SSDFVVLHDIEDKKyaMKKICLAKHTDKLKQTAlQEISRAVINYdlmkllSSLKNPYIVHYEDSwIDNDNNACIFTAYYE 110
Cdd:cd14665   10 SGNFGVARLMRDKQ--TKELVAVKYIERGEKID-ENVQREIINH------RSLRHPNIVRFKEV-ILTPTHLAIVMEYAA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 111 GGNMANAIKKArGKLFPEERIFkWLAQLLLAVNYLHSNRVVHMDLTCSNIFL-----PKddhVQLGNYGLAK-LINPEKP 184
Cdd:cd14665   80 GGELFERICNA-GRFSEDEARF-FFQQLISGVSYCHSMQICHRDLKLENTLLdgspaPR---LKICDFGYSKsSVLHSQP 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 334185276 185 VSMVsGISNSMCPEVLEDQPY-GYKSDIWSLGCCMYEITAHQPAFKAPD 232
Cdd:cd14665  155 KSTV-GTPAYIAPEVLLKKEYdGKIADVWSCGVTLYVMLVGAYPFEDPE 202
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
37-284 1.01e-09

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: 60.05  E-value: 1.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  37 LHDIEDKKYAMKKIclakhTDKLKQTALQEISRavinydlMKLLSSlkNPYIVHYEDSWIDNDNNACIFTaYYEGGNMAN 116
Cdd:cd14179   27 LHKKTNQEYAVKIV-----SKRMEANTQREIAA-------LKLCEG--HPNIVKLHEVYHDQLHTFLVME-LLKGGELLE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 117 AIKKArgKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSN-IFLPKDDH--VQLGNYGLAKLINPE-KPVSMVSGIS 192
Cdd:cd14179   92 RIKKK--QHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENlLFTDESDNseIKIIDFGFARLKPPDnQPLKTPCFTL 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 193 NSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMA-------GLINKINRSLMSPLPIVY---SSTLKQMIKL 262
Cdd:cd14179  170 HYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQCHDKSltctsaeEIMKKIKQGDFSFEGEAWknvSQEAKDLIQG 249
                        250       260
                 ....*....|....*....|..
gi 334185276 263 MLRKKPEYRPTACELLRNPSLQ 284
Cdd:cd14179  250 LLTVDPNKRIKMSGLRYNEWLQ 271
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
32-229 1.16e-09

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 59.48  E-value: 1.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  32 SDFVVL--HDIEDKKYAmkKICLAKH--TDKL---KQTALQ---EISRAVinYDLMKllsslKNPYIV--HYEdswIDND 99
Cdd:PHA03390  14 KNCEIVkkLKLIDGKFG--KVSVLKHkpTQKLfvqKIIKAKnfnAIEPMV--HQLMK-----DNPNFIklYYS---VTTL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 100 NNACIFTAYYEGGNMANAIKKaRGKLfPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNI-FLPKDDHVQLGNYGLAKL 178
Cdd:PHA03390  82 KGHVLIMDYIKDGDLFDLLKK-EGKL-SEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVlYDRAKDRIYLCDYGLCKI 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 334185276 179 INPEkpvSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEI-TAHQPaFK 229
Cdd:PHA03390 160 IGTP---SCYDGTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELlTGKHP-FK 207
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
79-284 1.33e-09

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


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 59.68  E-value: 1.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  79 LLSSLKNPYIVHYEDSWIDN-DNNACIF--TAYYEGGNMANAIKkaRGKLFPEERIFKWLAQLLLAVNYLHSNR--VVHM 153
Cdd:cd14030   77 MLKGLQHPNIVRFYDSWESTvKGKKCIVlvTELMTSGTLKTYLK--RFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHR 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 154 DLTCSNIFLP-KDDHVQLGNYGLAKLINPEKPVSMVsGISNSMCPEVLEDQpYGYKSDIWSLGCCMYEITAHQPAFKAPD 232
Cdd:cd14030  155 DLKCDNIFITgPTGSVKIGDLGLATLKRASFAKSVI-GTPEFMAPEMYEEK-YDESVDVYAFGMCMLEMATSEYPYSECQ 232
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 334185276 233 MAGLINKINRSLMSPLPI--VYSSTLKQMIKLMLRKKPEYRPTACELLRNPSLQ 284
Cdd:cd14030  233 NAAQIYRRVTSGVKPASFdkVAIPEVKEIIEGCIRQNKDERYAIKDLLNHAFFQ 286
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
35-221 1.40e-09

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: 58.90  E-value: 1.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  35 VVLHDIEDKKYAMKKIclaKHTDKLKQTALQEISravinydlmkLLSSLKNPYIVHYEDSWIDnDNNACIFTAYYEGGNM 114
Cdd:cd05039   22 VMLGDYRGQKVAVKCL---KDDSTAAQAFLAEAS----------VMTTLRHPNLVQLLGVVLE-GNGLYIVTEYMAKGSL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 115 ANAIKkARGKLFPEERifkwlAQLLLAVN------YLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEK----- 183
Cdd:cd05039   88 VDYLR-SRGRAVITRK-----DQLGFALDvcegmeYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAKEASSNQdggkl 161
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 334185276 184 PVSMVSgisnsmcPEVLEDQPYGYKSDIWSLGCCMYEI 221
Cdd:cd05039  162 PIKWTA-------PEALREKKFSTKSDVWSFGILLWEI 192
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
137-286 1.40e-09

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: 60.00  E-value: 1.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 137 QLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEkpvsmVSGISNSM---CPEV-LEDQPYGYKSDIW 212
Cdd:cd07851  126 QILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLARHTDDE-----MTGYVATRwyrAPEImLNWMHYNQTVDIW 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 213 SLGCCMYEITAHQPAFK----------------APDmAGLINKIN----RSLMSPLPI--------VYSSTLKQMIKL-- 262
Cdd:cd07851  201 SVGCIMAELLTGKTLFPgsdhidqlkrimnlvgTPD-EELLKKISsesaRNYIQSLPQmpkkdfkeVFSGANPLAIDLle 279
                        170       180
                 ....*....|....*....|....*
gi 334185276 263 -MLRKKPEYRPTACELLRNPSLQPY 286
Cdd:cd07851  280 kMLVLDPDKRITAAEALAHPYLAEY 304
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
65-280 1.40e-09

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: 59.64  E-value: 1.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  65 QEISRAVINYDLMKLLSSLKNpyivhyedswIDNDNNAC-------IFTAYYEGGNMANAIKKAR----------GKLFP 127
Cdd:cd05101   71 KDLSDLVSEMEMMKMIGKHKN----------IINLLGACtqdgplyVIVEYASKGNLREYLRARRppgmeysydiNRVPE 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 128 EERIFKWLA----QLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPekpVSMVSGISNS------MCP 197
Cdd:cd05101  141 EQMTFKDLVsctyQLARGMEYLASQKCIHRDLAARNVLVTENNVMKIADFGLARDINN---IDYYKKTTNGrlpvkwMAP 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 198 EVLEDQPYGYKSDIWSLGCCMYEI----TAHQPAFKAPDMAGLINKINRslMSPlPIVYSSTLKQMIKLMLRKKPEYRPT 273
Cdd:cd05101  218 EALFDRVYTHQSDVWSFGVLMWEIftlgGSPYPGIPVEELFKLLKEGHR--MDK-PANCTNELYMMMRDCWHAVPSQRPT 294

                 ....*..
gi 334185276 274 ACELLRN 280
Cdd:cd05101  295 FKQLVED 301
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
104-279 1.40e-09

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: 59.10  E-value: 1.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 104 IFTAYYEGGNMANAIKKARGKLFPEeRIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEK 183
Cdd:cd05114   76 IVTEFMENGCLLNYLRQRRGKLSRD-MLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRYVLDDQ 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 184 PVSMvSGISNSM---CPEVLEDQPYGYKSDIWSLGCCMYEI-TAHQPAFKAPDMAGLINKINRSLMSPLPIVYSSTLKQM 259
Cdd:cd05114  155 YTSS-SGAKFPVkwsPPEVFNYSKFSSKSDVWSFGVLMWEVfTEGKMPFESKSNYEVVEMVSRGHRLYRPKLASKSVYEV 233
                        170       180
                 ....*....|....*....|
gi 334185276 260 IKLMLRKKPEYRPTACELLR 279
Cdd:cd05114  234 MYSCWHEKPEGRPTFADLLR 253
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
106-233 1.41e-09

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: 59.03  E-value: 1.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 106 TAYYEGGNMAnaikkargKLFPEERIFKWLAQLLLAVN------YLHSNRVVHMDLTCSNIFLPKDDH---VQLGNYGLA 176
Cdd:cd14155   67 TEYINGGNLE--------QLLDSNEPLSWTVRVKLALDiarglsYLHSKGIFHRDLTSKNCLIKRDENgytAVVGDFGLA 138
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 177 KLI---NPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAfkAPDM 233
Cdd:cd14155  139 EKIpdySDGKEKLAVVGSPYWMAPEVLRGEPYNEKADVFSYGIILCEIIARIQA--DPDY 196
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
43-232 1.67e-09

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: 59.53  E-value: 1.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  43 KKYAMKKICLAKHTDKLKQTALQEisravinydlMKLLSSLKNPYIVhyedSWIDNDNNACIFTAYYE----GGNMANAI 118
Cdd:cd07879   41 EKVAIKKLSRPFQSEIFAKRAYRE----------LTLLKHMQHENVI----GLLDVFTSAVSGDEFQDfylvMPYMQTDL 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 119 KKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNSmcPE 198
Cdd:cd07879  107 QKIMGHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGLARHADAEMTGYVVTRWYRA--PE 184
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 334185276 199 V-LEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPD 232
Cdd:cd07879  185 ViLNWMHYNQTVDIWSVGCIMAEMLTGKTLFKGKD 219
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
44-281 1.70e-09

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: 59.58  E-value: 1.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  44 KYAMKKICLAKHTDKLKQTALQEisravinydlMKLLSSLKNPYIVHYEDSWIDnDNNACIFTAYY-----EGGNMANAI 118
Cdd:cd07880   42 KVAIKKLYRPFQSELFAKRAYRE----------LRLLKHMKHENVIGLLDVFTP-DLSLDRFHDFYlvmpfMGTDLGKLM 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 119 KKARgklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNSmcPE 198
Cdd:cd07880  111 KHEK---LSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARQTDSEMTGYVVTRWYRA--PE 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 199 V-LEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKI-------------------NRSLMSPLPIV----YSS 254
Cdd:cd07880  186 ViLNWMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHLDQLMEImkvtgtpskefvqklqsedAKNYVKKLPRFrkkdFRS 265
                        250       260       270
                 ....*....|....*....|....*....|....
gi 334185276 255 TLK----QMIKL---MLRKKPEYRPTACELLRNP 281
Cdd:cd07880  266 LLPnanpLAVNVlekMLVLDAESRITAAEALAHP 299
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
75-275 1.70e-09

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 59.17  E-value: 1.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  75 DLMKLLSSLKNPY---IVHYEDSWI-DNDNNACIFTAYYEGGNMANAIKKARGKLFPEERIfKWLAQLLLAVNYLHSNRV 150
Cdd:cd05079   52 DLKKEIEILRNLYhenIVKYKGICTeDGGNGIKLIMEFLPSGSLKEYLPRNKNKINLKQQL-KYAVQICKGMDYLGSRQY 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 151 VHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNS----MCPEVLEDQPYGYKSDIWSLGCCMYEITAHQP 226
Cdd:cd05079  131 VHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTVKDDLDSpvfwYAPECLIQSKFYIASDVWSFGVTLYELLTYCD 210
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 334185276 227 AFKAPdMAGLINKINrslmsplPIVYSSTLKQMIKLMLRKKPEYRPTAC 275
Cdd:cd05079  211 SESSP-MTLFLKMIG-------PTHGQMTVTRLVRVLEEGKRLPRPPNC 251
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
142-279 1.72e-09

Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SHIK, also referred to as STK40 or LYK4, is a cytoplasmic and nuclear protein that is involved in the negative regulation of NF-kappaB- and p53-mediated transcription. It was identified as a protein related to SINK, a p65-interacting protein that inhibits p65 phosphorylation by the catalytic subunit of PKA, thereby inhibiting transcriptional competence of NF-kappaB. The SHIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 59.34  E-value: 1.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 142 VNYLHSNRVVHMDLTCSNIFLPKDDH-VQLGNYGLAK-LINPEKPVSMVSGISNSMCPEVLEDQPY-GYKSDIWSLGCCM 218
Cdd:cd13974  145 VEALHKKNIVHRDLKLGNMVLNKRTRkITITNFCLGKhLVSEDDLLKDQRGSPAYISPDVLSGKPYlGKPSDMWALGVVL 224
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334185276 219 YEITAHQPAFKAPDMAGLINKINRSLMS-PLPIVYSSTLKQMIKLMLRKKPEYRPTACELLR 279
Cdd:cd13974  225 FTMLYGQFPFYDSIPQELFRKIKAAEYTiPEDGRVSENTVCLIRKLLVLNPQKRLTASEVLD 286
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
46-286 1.75e-09

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: 59.67  E-value: 1.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  46 AMKKICLAKHTDKLKQTALQEISR---AVIN----YDLMKLLSSLKNPYIVHYEDSWID----NDNNACIFTAYYEGGNM 114
Cdd:cd07877   29 AYGSVCAAFDTKTGLRVAVKKLSRpfqSIIHakrtYRELRLLKHMKHENVIGLLDVFTParslEEFNDVYLVTHLMGADL 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 115 ANAIKKARgklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEkpvsMVSGISNS 194
Cdd:cd07877  109 NNIVKCQK---LTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDDE----MTGYVATR 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 195 --MCPEVLED-QPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPLPIV-----------YSSTLKQMI 260
Cdd:cd07877  182 wyRAPEIMLNwMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVGTPGAELlkkissesarnYIQSLTQMP 261
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 334185276 261 KL-------------------MLRKKPEYRPTACELLRNPSLQPY 286
Cdd:cd07877  262 KMnfanvfiganplavdllekMLVLDSDKRITAAQALAHAYFAQY 306
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
127-280 1.94e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 59.86  E-value: 1.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 127 PEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLA-KL-INPEKPVSM-VSGISNSMCPEVLEDQ 203
Cdd:PHA03207 183 PLEQAITIQRRLLEALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGAAcKLdAHPDTPQCYgWSGTLETNSPELLALD 262
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 204 PYGYKSDIWSLGCCMYEITAHQPAF---KAPDMAGLINKINRSL-MSPL--PIVYSSTL-KQMIKLMLRKKPEYrpTACE 276
Cdd:PHA03207 263 PYCAKTDIWSAGLVLFEMSVKNVTLfgkQVKSSSSQLRSIIRCMqVHPLefPQNGSTNLcKHFKQYAIVLRPPY--TIPP 340

                 ....
gi 334185276 277 LLRN 280
Cdd:PHA03207 341 VIRK 344
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
112-282 2.16e-09

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: 58.88  E-value: 2.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 112 GNMANAIKKARGKLFPEErIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGI 191
Cdd:cd05109   93 GCLLDYVRENKDRIGSQD-LLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGG 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 192 S---NSMCPEVLEDQPYGYKSDIWSLGCCMYEITAH--QP--AFKAPDMAGLINKINRslMSPLPIVYSSTLKQMIKLML 264
Cdd:cd05109  172 KvpiKWMALESILHRRFTHQSDVWSYGVTVWELMTFgaKPydGIPAREIPDLLEKGER--LPQPPICTIDVYMIMVKCWM 249
                        170       180
                 ....*....|....*....|....*
gi 334185276 265 rKKPEYRPTACELL-------RNPS 282
Cdd:cd05109  250 -IDSECRPRFRELVdefsrmaRDPS 273
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
112-281 2.42e-09

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: 58.14  E-value: 2.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 112 GNMANAIKkARGKLFPEE--RIFKwlaQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGL--AKLINPEK-PVS 186
Cdd:cd14023   69 GDMHSYVR-SCKRLREEEaaRLFK---QIVSAVAHCHQSAIVLGDLKLRKFVFSDEERTQLRLESLedTHIMKGEDdALS 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 187 MVSGISNSMCPEVLEDQ-PYGYKS-DIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSpLPIVYSSTLKQMIKLML 264
Cdd:cd14023  145 DKHGCPAYVSPEILNTTgTYSGKSaDVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFC-IPDHVSPKARCLIRSLL 223
                        170
                 ....*....|....*..
gi 334185276 265 RKKPEYRPTACELLRNP 281
Cdd:cd14023  224 RREPSERLTAPEILLHP 240
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
135-274 2.75e-09

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: 58.66  E-value: 2.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 135 LAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDD----HVQLGNYGLA---KLINPEKPVSM--VS--GISNSMCPEVLEDQ 203
Cdd:cd14018  144 ILQLLEGVDHLVRHGIAHRDLKSDNILLELDFdgcpWLVIADFGCCladDSIGLQLPFSSwyVDrgGNACLMAPEVSTAV 223
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185276 204 P-------YGyKSDIWSLGCCMYEI-TAHQPAFKAPDMAGLINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTA 274
Cdd:cd14018  224 PgpgvvinYS-KADAWAVGAIAYEIfGLSNPFYGLGDTMLESRSYQESQLPALPSAVPPDVRQVVKDLLQRDPNKRVSA 301
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
128-281 2.79e-09

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: 58.59  E-value: 2.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 128 EERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLIN-PEKPVSMVSGISNSMCPEVL-EDQPY 205
Cdd:cd07846   99 ESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAaPGEVYTDYVATRWYRAPELLvGDTKY 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 206 GYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKI----------NRSLMSPLPIV--------------------YSST 255
Cdd:cd07846  179 GKAVDVWAVGCLVTEMLTGEPLFPGDSDIDQLYHIikclgnliprHQELFQKNPLFagvrlpevkeveplerrypkLSGV 258
                        170       180
                 ....*....|....*....|....*.
gi 334185276 256 LKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd07846  259 VIDLAKKCLHIDPDKRPSCSELLHHE 284
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
28-281 2.83e-09

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


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 58.71  E-value: 2.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  28 GKSSSDFVVL-HDIEDKK-YAMKKIclaKHTDKLKQTALQEIsravinydlmKLLSSLK------NPYIVHYEDSWIDNd 99
Cdd:cd14210   22 GKGSFGQVVKcLDHKTGQlVAIKII---RNKKRFHQQALVEV----------KILKHLNdndpddKHNIVRYKDSFIFR- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 100 NNACIFTayyE--GGNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFL--PKDDHVQLGNYGL 175
Cdd:cd14210   88 GHLCIVF---EllSINLYELLKSNNFQGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLkqPSKSSIKVIDFGS 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 176 AKLINpEKpvsMVSGISNSM--CPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKA----------------PDMAgLI 237
Cdd:cd14210  165 SCFEG-EK---VYTYIQSRFyrAPEVILGLPYDTAIDMWSLGCILAELYTGYPLFPGeneeeqlacimevlgvPPKS-LI 239
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 238 NKINR------SLMSPLPIVY---------SSTLKQM-----------IKLMLRKKPEYRPTACELLRNP 281
Cdd:cd14210  240 DKASRrkkffdSNGKPRPTTNskgkkrrpgSKSLAQVlkcddpsfldfLKKCLRWDPSERMTPEEALQHP 309
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
66-286 3.23e-09

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: 58.35  E-value: 3.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  66 EISRAVINYdlMKLLSSLKNPYIVHYEDSWIdNDNNACIFTAYYEGGNMaNAIKKargklFPEERIFKWLAQLLLAVNYL 145
Cdd:cd06619   41 ELQKQIMSE--LEILYKCDSPYIIGFYGAFF-VENRISICTEFMDGGSL-DVYRK-----IPEHVLGRIAVAVVKGLTYL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 146 HSNRVVHMDLTCSNIFLPKDDHVQLGNYGLA-KLINpeKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAH 224
Cdd:cd06619  112 WSLKILHRDVKPSNMLVNTRGQVKLCDFGVStQLVN--SIAKTYVGTNAYMAPERISGEQYGIHSDVWSLGISFMELALG 189
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334185276 225 QpaFKAPDMAGlinkiNRSLMSPLPIV---------------YSSTLKQMIKLMLRKKPEYRPTACELLRNPSLQPY 286
Cdd:cd06619  190 R--FPYPQIQK-----NQGSLMPLQLLqcivdedppvlpvgqFSEKFVHFITQCMRKQPKERPAPENLMDHPFIVQY 259
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
104-273 3.37e-09

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: 58.11  E-value: 3.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 104 IFTAYYEGGNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEK 183
Cdd:cd05073   82 IITEFMAKGSLLDFLKSDEGSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVIEDNE 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 184 PVSMvSGISNSM---CPEVLEDQPYGYKSDIWSLGCCMYEITAH----QPAFKAPDmagLINKINRSLMSPLPivySSTL 256
Cdd:cd05073  162 YTAR-EGAKFPIkwtAPEAINFGSFTIKSDVWSFGILLMEIVTYgripYPGMSNPE---VIRALERGYRMPRP---ENCP 234
                        170       180
                 ....*....|....*....|
gi 334185276 257 KQMIKLMLR---KKPEYRPT 273
Cdd:cd05073  235 EELYNIMMRcwkNRPEERPT 254
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
108-273 3.63e-09

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: 58.05  E-value: 3.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 108 YYEGGNMA---NAIKKARGklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHV---QLGNYGLAKLINP 181
Cdd:cd14038   79 YCQGGDLRkylNQFENCCG--LREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGEQRlihKIIDLGYAKELDQ 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 182 EKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYE-ITAHQPAFK---------------------APDMAGLInK 239
Cdd:cd14038  157 GSLCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFEcITGFRPFLPnwqpvqwhgkvrqksnedivvYEDLTGAV-K 235
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 334185276 240 INRSLMSP--LPIVYSSTLKQMIKLMLRKKPEYRPT 273
Cdd:cd14038  236 FSSVLPTPnnLNGILAGKLERWLQCMLMWHPRQRGT 271
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
110-283 3.87e-09

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: 58.24  E-value: 3.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 110 EGGNMANAIKKARGklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPK---DDHVQLGNYGLAK-----LINP 181
Cdd:cd14171   92 EGGELFDRISQHRH--FTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDnseDAPIKLCDFGFAKvdqgdLMTP 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 182 EKPVSMVSgisnsmcPEVLEDQ---------------PYGY-KS-DIWSLGCCMYEITAHQPAF--KAPDMAgLINKINR 242
Cdd:cd14171  170 QFTPYYVA-------PQVLEAQrrhrkersgiptsptPYTYdKScDMWSLGVIIYIMLCGYPPFysEHPSRT-ITKDMKR 241
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 334185276 243 SLMS---PLP----IVYSSTLKQMIKLMLRKKPEYRPTACELLRNPSL 283
Cdd:cd14171  242 KIMTgsyEFPeeewSQISEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
16-247 3.93e-09

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: 58.10  E-value: 3.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  16 LDNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLaKHTDKLKQTALQEISravinydlmkLLSSLKNPYIVHYEDsW 95
Cdd:cd07871    4 LETYVKLDKLGEGTYATVFKGRSKLTENLVALKEIRL-EHEEGAPCTAIREVS----------LLKNLKHANIVTLHD-I 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  96 IDNDNNACIFTAYYEGgNMANAIKKArGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGL 175
Cdd:cd07871   72 IHTERCLTLVFEYLDS-DLKQYLDNC-GNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGL 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334185276 176 AKLIN-PEKPVSMVSGISNSMCPEV-LEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSP 247
Cdd:cd07871  150 ARAKSvPTKTYSNEVVTLWYRPPDVlLGSTEYSTPIDMWGVGCILYEMATGRPMFPGSTVKEELHLIFRLLGTP 223
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
24-278 4.23e-09

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: 57.90  E-value: 4.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  24 QVRRGKSSSDFVVLHDIED----KKYAMKKicLAKHTDKLKQTALQEISravinydLMKLLSSlkNPYIVHY-EDSWIDN 98
Cdd:cd14036    3 RIKRVIAEGGFAFVYEAQDvgtgKEYALKR--LLSNEEEKNKAIIQEIN-------FMKKLSG--HPNIVQFcSAASIGK 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  99 DNNA------CIFTAYYEGGnMANAIKKARGK-LFPEERIFKWLAQLLLAVNYLHSNR--VVHMDLTCSNIFLPKDDHVQ 169
Cdd:cd14036   72 EESDqgqaeyLLLTELCKGQ-LVDFVKKVEAPgPFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQIK 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 170 LGNYGLAKLInPEKPVSMVSGISNSM--------------CPEVLE---DQPYGYKSDIWSLGCCMYEITAHQPAFKapD 232
Cdd:cd14036  151 LCDFGSATTE-AHYPDYSWSAQKRSLvedeitrnttpmyrTPEMIDlysNYPIGEKQDIWALGCILYLLCFRKHPFE--D 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 334185276 233 MAGLiNKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELL 278
Cdd:cd14036  228 GAKL-RIINAKYTIPPNDTQYTVFHDLIRSTLKVNPEERLSITEIV 272
PK_MADML cd14035
Pseudokinase domain of MLF1-ADaptor Molecule-Like; The pseudokinase domain shows similarity to ...
80-278 4.62e-09

Pseudokinase domain of MLF1-ADaptor Molecule-Like; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. MADML has been shown to be expressed throughout development in Xenopus laevis with highest expression found in the developing lens and retina. It may play an important role in embryonic eye development. The MADML 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: 270937 [Multi-domain]  Cd Length: 263  Bit Score: 57.63  E-value: 4.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  80 LSSLKNPYIVHYEDSWID-NDNNA-CIF-TAYYEGGNMANAIKKARG--KLFPEERIFKWLAQLLLAVNYLHSNR--VVH 152
Cdd:cd14035   49 LTLVDHPNIVKFHKYWLDvKDNHArVVFiTEYVSSGSLKQFLKKTKKnhKTMNARAWKRWCTQILSALSYLHSCEppIIH 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 153 MDLTCSNIFLPKDDHVQLGNYgLAKLINPEKPVSMVSGISNS----------MCPEV--LEDqpyGYKSDIWSLGCCMYE 220
Cdd:cd14035  129 GNLTSDTIFIQHNGLIKIGSV-WHRLFVNVLPEGGVRGPLRQereelrnlhfFPPEYgsCED---GTAVDIFSFGMCALE 204
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 221 ITAH--QPAFKAPDMAGLINKINRSLMSPLpivysstLKQMIKLMLRKKPEYRPTACELL 278
Cdd:cd14035  205 MAVLeiQANGDTRVSEEAIARARHSLEDPN-------MREFILSCLRHNPCKRPTAHDLL 257
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
104-279 4.74e-09

Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. The KSR subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 57.74  E-value: 4.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 104 IFTAYYEGGNMANAIKKARGKlFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHV--QLGNYGLAKLINP 181
Cdd:cd14063   73 IVTSLCKGRTLYSLIHERKEK-FDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLENGRVVitDFGLFSLSGLLQP 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 182 EKPvSMVSGISNS----MCPEVL----------EDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSP 247
Cdd:cd14063  152 GRR-EDTLVIPNGwlcyLAPEIIralspdldfeESLPFTKASDVYAFGTVWYELLAGRWPFKEQPAESIIWQVGCGKKQS 230
                        170       180       190
                 ....*....|....*....|....*....|...
gi 334185276 248 LPIVYSS-TLKQMIKLMLRKKPEYRPTACELLR 279
Cdd:cd14063  231 LSQLDIGrEVKDILMQCWAYDPEKRPTFSDLLR 263
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
141-292 5.21e-09

Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity.STRAD-beta is also referred to as ALS2CR2 (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 2 protein), since the human gene encoding it is located within the juvenile ALS2 critical region on chromosome 2q33-q34. It is not linked to the development of ALS2. 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. The STRAD-beta 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: 270864 [Multi-domain]  Cd Length: 328  Bit Score: 57.96  E-value: 5.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 141 AVNYLHSNRVVHMDLTCSNIFLPKDDHVQL-GNYGLAKLIN-----------PEKPVSMVSGISnsmcPEVLEDQPYGY- 207
Cdd:cd08226  113 ALNYLHQNGCIHRSVKASHILISGDGLVSLsGLSHLYSMVTngqrskvvydfPQFSTSVLPWLS----PELLRQDLHGYn 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 208 -KSDIWSLGCCMYEITAHQPAFKapDM----------------------------------AGLINKINRS--------- 243
Cdd:cd08226  189 vKSDIYSVGITACELARGQVPFQ--DMrrtqmllqklkgppyspldifpfpelesrmknsqSGMDSGIGESvatssmtrt 266
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 334185276 244 -----LMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRNPSLQPYLLQCQN 292
Cdd:cd08226  267 mtserLQTPSSKTFSPAFHNLVELCLQQDPEKRPSASSLLSHSFFKQVKEQTQA 320
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
135-281 6.40e-09

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: 57.28  E-value: 6.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 135 LAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDH-----VQLGNYGLAKLINPEK----PVSMVSGISNSMCPEVLEDQPY 205
Cdd:cd13982  105 LRQIASGLAHLHSLNIVHRDLKPQNILISTPNAhgnvrAMISDFGLCKKLDVGRssfsRRSGVAGTSGWIAPEMLSGSTK 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 206 G---YKSDIWSLGCCMYEITAH--QPAFKAPDMAGLINKINRSLMSPLPIV-YSSTLKQMIKLMLRKKPEYRPTACELLR 279
Cdd:cd13982  185 RrqtRAVDIFSLGCVFYYVLSGgsHPFGDKLEREANILKGKYSLDKLLSLGeHGPEAQDLIERMIDFDPEKRPSAEEVLN 264

                 ..
gi 334185276 280 NP 281
Cdd:cd13982  265 HP 266
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
134-283 6.86e-09

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: 56.94  E-value: 6.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 134 WLAQ-LLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVqLGNYGLAKLINPEKPVSM-VSGISNSMCPEVLEDQPYGYKSDI 211
Cdd:cd13995  100 WVTKhVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAV-LVDFGLSVQMTEDVYVPKdLRGTEIYMSPEVILCRGHNTKADI 178
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185276 212 WSLGCCMYEITAHQPAF-------KAPDMAGLINKINRSLmSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRNPSL 283
Cdd:cd13995  179 YSLGATIIHMQTGSPPWvrryprsAYPSYLYIIHKQAPPL-EDIAQDCSPAMRELLEAALERNPNHRSSAAELLKHEAL 256
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
18-302 7.29e-09

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: 57.28  E-value: 7.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  18 NYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLaKHTDKLKQTALQEISravinydlmkLLSSLKNPYIVHYEDswID 97
Cdd:cd07870    1 SYLNLEKLGEGSYATVYKGISRINGQLVALKVISM-KTEEGVPFTAIREAS----------LLKGLKHANIVLLHD--II 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  98 NDNNACIFTAYYEGGNMANAIKKARGKLFPEE-RIFkwLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLA 176
Cdd:cd07870   68 HTKETLTFVFEYMHTDLAQYMIQHPGGLHPYNvRLF--MFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLA 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 177 --KLINPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFkaPDMAGLINKINRsLMSPLPIVYSS 254
Cdd:cd07870  146 raKSIPSQTYSSEVVTLWYRPPDVLLGATDYSSALDIWGAGCIFIEMLQGQPAF--PGVSDVFEQLEK-IWTVLGVPTED 222
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 334185276 255 TLKQMIKLMlRKKPE-YRPTACELLR---NPSLQPYllQCQNLSPIYLPVFP 302
Cdd:cd07870  223 TWPGVSKLP-NYKPEwFLPCKPQQLRvvwKRLSRPP--KAEDLASQMLMMFP 271
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
35-220 7.81e-09

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: 57.57  E-value: 7.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  35 VVL-HDIE-DKKYAMKKIclaKHTDKLKQTALQEIsravinydlmKLLSSLKN------PYIVHYEDsWIDNDNNACIFT 106
Cdd:cd14134   28 VLEcWDRKrKRYVAVKII---RNVEKYREAAKIEI----------DVLETLAEkdpngkSHCVQLRD-WFDYRGHMCIVF 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 107 AYYeGGNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVS 186
Cdd:cd14134   94 ELL-GPSLYDFLKKNNYGPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLVDSDYVKVYNPKKKRQIRVPKSTD 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 334185276 187 MV-----SGISNSM------------CPEVLEDQPYGYKSDIWSLGCCMYE 220
Cdd:cd14134  173 IKlidfgSATFDDEyhssivstrhyrAPEVILGLGWSYPCDVWSIGCILVE 223
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
16-247 8.11e-09

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 57.14  E-value: 8.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  16 LDNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAKHTDKLKQTALQEISravinydlmkLLSSLKNPYIVHYEDSw 95
Cdd:PLN00009   1 MDQYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQEDEGVPSTAIREIS----------LLKEMQHGNIVRLQDV- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  96 IDNDNNACIFTAYYE---GGNMANAIKKARgklfpEERIFK-WLAQLLLAVNYLHSNRVVHMDLTCSNIFLPK-DDHVQL 170
Cdd:PLN00009  70 VHSEKRLYLVFEYLDldlKKHMDSSPDFAK-----NPRLIKtYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRrTNALKL 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 171 GNYGLAKLINpeKPVSMVSGISNSM---CPEV-LEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMS 246
Cdd:PLN00009 145 ADFGLARAFG--IPVRTFTHEVVTLwyrAPEIlLGSRHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEIDELFKIFRILGT 222

                 .
gi 334185276 247 P 247
Cdd:PLN00009 223 P 223
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
77-227 8.16e-09

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: 56.76  E-value: 8.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  77 MKLLSSLKNPYIVHYEDSWIdNDNNACIFTAYYEGGNMANAIKKargklfpEERIFKWLAQLLLAVN------YLHSNRV 150
Cdd:cd14156   39 ISLLQKLSHPNIVRYLGICV-KDEKLHPILEYVSGGCLEELLAR-------EELPLSWREKVELACDisrgmvYLHSKNI 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 151 VHMDLTCSNIFL---PKDDHVQLGNYGLAKLI------NPEKPVSMVsGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEI 221
Cdd:cd14156  111 YHRDLNSKNCLIrvtPRGREAVVTDFGLAREVgempanDPERKLSLV-GSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEI 189

                 ....*.
gi 334185276 222 TAHQPA 227
Cdd:cd14156  190 LARIPA 195
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
13-284 8.30e-09

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: 56.80  E-value: 8.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  13 KFTLDNYHVVEQVRRGKSSSdfVVLHDIEDKKYAMKKICLAKhtDKLKQTALQEISRAVInydlmKLLSSLKNPYIVHYE 92
Cdd:cd14117    2 KFTIDDFDIGRPLGKGKFGN--VYLAREKQSKFIVALKVLFK--SQIEKEGVEHQLRREI-----EIQSHLRHPNILRLY 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  93 DSWIDnDNNACIFTAYYEGGNMANAIKKArgKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGN 172
Cdd:cd14117   73 NYFHD-RKRIYLILEYAPRGELYKELQKH--GRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIAD 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 173 YGLAkLINPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSpLPIVY 252
Cdd:cd14117  150 FGWS-VHAPSLRRRTMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVDLK-FPPFL 227
                        250       260       270
                 ....*....|....*....|....*....|..
gi 334185276 253 SSTLKQMIKLMLRKKPEYRPTACELLRNPSLQ 284
Cdd:cd14117  228 SDGSRDLISKLLRYHPSERLPLKGVMEHPWVK 259
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
34-283 1.03e-08

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: 56.46  E-value: 1.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  34 FVVLHDIEDKKYAMKkicLAKHTDKLKQTALQEISRAVINydlmkLLSSLKNPYIVHYEDSWiDNDNNACIFTAYYEGGN 113
Cdd:cd14193   17 FGQVHKCEEKSSGLK---LAAKIIKARSQKEKEEVKNEIE-----VMNQLNHANLIQLYDAF-ESRNDIVLVMEYVDGGE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 114 MANAIKKARGKLfPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDD--HVQLGNYGLAKLINPEKPVSMVSGI 191
Cdd:cd14193   88 LFDRIIDENYNL-TELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSREanQVKIIDFGLARRYKPREKLRVNFGT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 192 SNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKI---NRSLMSPLPIVYSSTLKQMIKLMLRKKP 268
Cdd:cd14193  167 PEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNIlacQWDFEDEEFADISEEAKDFISKLLIKEK 246
                        250
                 ....*....|....*
gi 334185276 269 EYRPTACELLRNPSL 283
Cdd:cd14193  247 SWRMSASEALKHPWL 261
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
137-280 1.14e-08

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


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 56.94  E-value: 1.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 137 QLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLI----------NPEKPVSMvsgisnsMCPEVLEDQPYG 206
Cdd:cd05098  143 QVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIADFGLARDIhhidyykkttNGRLPVKW-------MAPEALFDRIYT 215
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334185276 207 YKSDIWSLGCCMYEI-TAHQPAFKAPDMAGLINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRN 280
Cdd:cd05098  216 HQSDVWSFGVLLWEIfTLGGSPYPGVPVEELFKLLKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVED 290
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
129-279 1.15e-08

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. 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: 56.93  E-value: 1.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 129 ERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLI--NPEK--------PVSMvsgisnsMCPE 198
Cdd:cd14207  180 EDLISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARDIykNPDYvrkgdarlPLKW-------MAPE 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 199 VLEDQPYGYKSDIWSLGCCMYEI----TAHQPAFKAPDmaGLINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTA 274
Cdd:cd14207  253 SIFDKIYSTKSDVWSYGVLLWEIfslgASPYPGVQIDE--DFCSKLKEGIRMRAPEFATSEIYQIMLDCWQGDPNERPRF 330

                 ....*
gi 334185276 275 CELLR 279
Cdd:cd14207  331 SELVE 335
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
34-226 1.15e-08

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: 56.69  E-value: 1.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  34 FVVL--HDIEDKKYAMKK--ICLAKHtDKLKQTALQEIsravinyDLMKllsSLKNPYIVHYED----SWIDNDNNACIF 105
Cdd:cd13989    8 YVTLwkHQDTGEYVAIKKcrQELSPS-DKNRERWCLEV-------QIMK---KLNHPNVVSARDvppeLEKLSPNDLPLL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 106 TAYY-EGGNMA---NAIKKARGklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFL-PKDDHV--QLGNYGLAKL 178
Cdd:cd13989   77 AMEYcSGGDLRkvlNQPENCCG--LKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLqQGGGRViyKLIDLGYAKE 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 334185276 179 INPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYE-ITAHQP 226
Cdd:cd13989  155 LDQGSLCTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFEcITGYRP 203
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
137-228 1.17e-08

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: 56.19  E-value: 1.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 137 QLLLAVNYLHSNRVVHMDLTCSNIFL---PKDDHVQLGNYGLAKLINP--EKPVsmvsGISNSMCPEVLEDQPYGYKSDI 211
Cdd:cd14088  107 QVLEAVAYLHSLKIVHRNLKLENLVYynrLKNSKIVISDFHLAKLENGliKEPC----GTPEYLAPEVVGRQRYGRPVDC 182
                         90
                 ....*....|....*..
gi 334185276 212 WSLGCCMYEITAHQPAF 228
Cdd:cd14088  183 WAIGVIMYILLSGNPPF 199
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
104-273 1.21e-08

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: 56.62  E-value: 1.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 104 IFTAYYEGGNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINpEK 183
Cdd:cd05069   83 IVTEFMGKGSLLDFLKEGDGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIE-DN 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 184 PVSMVSGISNSM---CPEVLEDQPYGYKSDIWSLGCCMYEITAhQPAFKAPDMAG--LINKINRSLMSPLPIVYSSTLKQ 258
Cdd:cd05069  162 EYTARQGAKFPIkwtAPEAALYGRFTIKSDVWSFGILLTELVT-KGRVPYPGMVNreVLEQVERGYRMPCPQGCPESLHE 240
                        170
                 ....*....|....*
gi 334185276 259 MIKLMLRKKPEYRPT 273
Cdd:cd05069  241 LMKLCWKKDPDERPT 255
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
16-247 1.25e-08

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: 56.54  E-value: 1.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  16 LDNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLaKHTDKLKQTALQEISravinydlmkLLSSLKNPYIVHYEDsw 95
Cdd:cd07872    5 METYIKLEKLGEGTYATVFKGRSKLTENLVALKEIRL-EHEEGAPCTAIREVS----------LLKDLKHANIVTLHD-- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  96 IDNDNNACIFTAYYEGGNMANAIKKArGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGL 175
Cdd:cd07872   72 IVHTDKSLTLVFEYLDKDLKQYMDDC-GNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGL 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334185276 176 AKLIN-PEKPVSMVSGISNSMCPEV-LEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSP 247
Cdd:cd07872  151 ARAKSvPTKTYSNEVVTLWYRPPDVlLGSSEYSTQIDMWGVGCIFFEMASGRPLFPGSTVEDELHLIFRLLGTP 224
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
104-273 1.72e-08

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: 55.85  E-value: 1.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 104 IFTAYYEGGNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINpEK 183
Cdd:cd05071   80 IVTEYMSKGSLLDFLKGEMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIE-DN 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 184 PVSMVSGISNSM---CPEVLEDQPYGYKSDIWSLGCCMYEITAhQPAFKAPDMAG--LINKINRSLMSPLPIVYSSTLKQ 258
Cdd:cd05071  159 EYTARQGAKFPIkwtAPEAALYGRFTIKSDVWSFGILLTELTT-KGRVPYPGMVNreVLDQVERGYRMPCPPECPESLHD 237
                        170
                 ....*....|....*
gi 334185276 259 MIKLMLRKKPEYRPT 273
Cdd:cd05071  238 LMCQCWRKEPEERPT 252
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
137-277 1.74e-08

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: 56.27  E-value: 1.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 137 QLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLI----------NPEKPVSMvsgisnsMCPEVLEDQPYG 206
Cdd:cd05053  141 QVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIADFGLARDIhhidyyrkttNGRLPVKW-------MAPEALFDRVYT 213
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334185276 207 YKSDIWSLGCCMYEIT----AHQPAFKAPDMAGLINKINRslMSPlPIVYSSTLKQMIKLMLRKKPEYRPTACEL 277
Cdd:cd05053  214 HQSDVWSFGVLLWEIFtlggSPYPGIPVEELFKLLKEGHR--MEK-PQNCTQELYMLMRDCWHEVPSQRPTFKQL 285
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
46-230 1.79e-08

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: 56.59  E-value: 1.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  46 AMKKICLAKHTDKLKQTALQEISRAVInydLMK-----------LLSSLKNPYIVHYEDSWIDNDNNACIFTaYYEGGNM 114
Cdd:cd05625   13 AFGEVCLARKVDTKALYATKTLRKKDV---LLRnqvahvkaerdILAEADNEWVVRLYYSFQDKDNLYFVMD-YIPGGDM 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 115 ANAIkkARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLI--------------- 179
Cdd:cd05625   89 MSLL--IRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFrwthdskyyqsgdhl 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 180 ------------NPE--------KPV--------------SMVsGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQ 225
Cdd:cd05625  167 rqdsmdfsnewgDPEncrcgdrlKPLerraarqhqrclahSLV-GTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQ 245

                 ....*
gi 334185276 226 PAFKA 230
Cdd:cd05625  246 PPFLA 250
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
46-281 1.83e-08

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: 55.90  E-value: 1.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  46 AMKKICLAKHTDKLKQTALQEISravinydlmkLLSSLKNPYIVHYEDSWIDNDNNACIFTayYEGGNMANAIKKARGKL 125
Cdd:cd07839   29 ALKRVRLDDDDEGVPSSALREIC----------LLKELKHKNIVRLYDVLHSDKKLTLVFE--YCDQDLKKYFDSCNGDI 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 126 FPEErIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKliNPEKPVSMVSGISNSM---CPEVL-E 201
Cdd:cd07839   97 DPEI-VKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLAR--AFGIPVRCYSAEVVTLwyrPPDVLfG 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 202 DQPYGYKSDIWSLGCCMYEIT-AHQPAFKAPDMAGLINKINRSLMSP----------------LPIVYSSTLKQMI---- 260
Cdd:cd07839  174 AKLYSTSIDMWSAGCIFAELAnAGRPLFPGNDVDDQLKRIFRLLGTPteeswpgvsklpdykpYPMYPATTSLVNVvpkl 253
                        250       260
                 ....*....|....*....|....*....
gi 334185276 261 --------KLMLRKKPEYRPTACELLRNP 281
Cdd:cd07839  254 nstgrdllQNLLVCNPVQRISAEEALQHP 282
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
17-228 1.85e-08

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: 56.00  E-value: 1.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  17 DNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLAKHTDKLKQTALQEISravinydLMKLLSslKNPYIVHYED-SW 95
Cdd:cd07837    1 DAYEKLEKIGEGTYGKVYKARDKNTGKLVALKKTRLEMEEEGVPSTALREVS-------LLQMLS--QSIYIVRLLDvEH 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  96 IDNDNNACIFTAY-YEGGNMANAI---KKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHV-QL 170
Cdd:cd07837   72 VEENGKPLLYLVFeYLDTDLKKFIdsyGRGPHNPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQKGLlKI 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 171 GNYGLAKLIN-PEKPVSMVSGISNSMCPEV-LEDQPYGYKSDIWSLGCCMYEITAHQPAF 228
Cdd:cd07837  152 ADLGLGRAFTiPIKSYTHEIVTLWYRAPEVlLGSTHYSTPVDMWSVGCIFAEMSRKQPLF 211
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
134-247 1.96e-08

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: 56.68  E-value: 1.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 134 WLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNSM--CPEVLEDQP-YGYKSD 210
Cdd:cd07853  108 FLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVEEPDESKHMTQEVVTQYyrAPEILMGSRhYTSAVD 187
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 334185276 211 IWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSP 247
Cdd:cd07853  188 IWSVGCIFAELLGRRILFQAQSPIQQLDLITDLLGTP 224
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
34-221 2.10e-08

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: 55.59  E-value: 2.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  34 FVVLHDIEDKKYAMKKicLAKHTDKLKQTALQEIsravinydlmKLLSSLKNPYIVH-----YEDSWIDndnnacIFTAY 108
Cdd:cd14154   10 IKVTHRETGEVMVMKE--LIRFDEEAQRNFLKEV----------KVMRSLDHPNVLKfigvlYKDKKLN------LITEY 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 109 YEGGNManaikkaRGKLFPEERIFKWLAQLLLA------VNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPE 182
Cdd:cd14154   72 IPGGTL-------KDVLKDMARPLPWAQRVRFAkdiasgMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLARLIVEE 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 183 KPVS---------------------MVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEI 221
Cdd:cd14154  145 RLPSgnmspsetlrhlkspdrkkryTVVGNPYWMAPEMLNGRSYDEKVDIFSFGIVLCEI 204
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
135-286 2.32e-08

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: 56.16  E-value: 2.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 135 LAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVS--MVSGISNS--MCPEV-LEDQPYGYKS 209
Cdd:cd07849  112 LYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLARIADPEHDHTgfLTEYVATRwyRAPEImLNSKGYTKAI 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 210 DIWSLGCCMYEITAHQPAF-------------------KAPDMAGLINKINRSLMSPLPI--------VYSSTLKQMIKL 262
Cdd:cd07849  192 DIWSVGCILAEMLSNRPLFpgkdylhqlnlilgilgtpSQEDLNCIISLKARNYIKSLPFkpkvpwnkLFPNADPKALDL 271
                        170       180
                 ....*....|....*....|....*..
gi 334185276 263 ---MLRKKPEYRPTACELLRNPSLQPY 286
Cdd:cd07849  272 ldkMLTFNPHKRITVEEALAHPYLEQY 298
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
111-230 2.50e-08

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: 55.65  E-value: 2.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 111 GGNMANAIKKARgkLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDH---VQLGNYGLAKLI-NPEKPVS 186
Cdd:cd14180   85 GGELLDRIKKKA--RFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDgavLKVIDFGFARLRpQGSRPLQ 162
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 334185276 187 MVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKA 230
Cdd:cd14180  163 TPCFTLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQS 206
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
40-300 2.65e-08

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 55.92  E-value: 2.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  40 IEDKKYAMKKICLAKHTDKLKQTAlQEISRAVINYDLM---KLLSSLKNPYIVHYEDSWIDNDNnACIFTAYyeggnMAN 116
Cdd:PTZ00024  32 LTGKIVAIKKVKIIEISNDVTKDR-QLVGMCGIHFTTLrelKIMNEIKHENIMGLVDVYVEGDF-INLVMDI-----MAS 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 117 AIKKA--RGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLA-------------KLINP 181
Cdd:PTZ00024 105 DLKKVvdRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLArrygyppysdtlsKDETM 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 182 EKPVSMVSGISN--SMCPEVL-EDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSP----------L 248
Cdd:PTZ00024 185 QRREEMTSKVVTlwYRAPELLmGAEKYHFAVDMWSVGCIFAELLTGKPLFPGENEIDQLGRIFELLGTPnednwpqakkL 264
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185276 249 PIV--YSSTLKQMIKL---------------MLRKKPEYRPTACELLRNPSLQPYLLQCqnlSPIYLPV 300
Cdd:PTZ00024 265 PLYteFTPRKPKDLKTifpnasddaidllqsLLKLNPLERISAKEALKHEYFKSDPLPC---DPSQLPF 330
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
17-286 2.74e-08

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: 55.63  E-value: 2.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  17 DNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLakhtdklkqtalqEISRAVINYDLMKL--LSSLKNPYIVH-YED 93
Cdd:cd06622    1 DEIEVLDELGKGNYGSVYKVLHRPTGVTMAMKEIRL-------------ELDESKFNQIIMELdiLHKAVSPYIVDfYGA 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  94 SWIDNDNNACIftAYYEGGNM----ANAIKKARgklFPEERIFKWLAQLLLAVNYL-HSNRVVHMDLTCSNIFLPKDDHV 168
Cdd:cd06622   68 FFIEGAVYMCM--EYMDAGSLdklyAGGVATEG---IPEDVLRRITYAVVKGLKFLkEEHNIIHRDVKPTNVLVNGNGQV 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 169 QLGNYGLAKliNPEKPVSMVS-GISNSMCPEVLEDQ------PYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKIN 241
Cdd:cd06622  143 KLCDFGVSG--NLVASLAKTNiGCQSYMAPERIKSGgpnqnpTYTVQSDVWSLGLSILEMALGRYPYPPETYANIFAQLS 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 334185276 242 RSLMSP---LPIVYSSTLKQMIKLMLRKKPEYRPTACELLRNPSLQPY 286
Cdd:cd06622  221 AIVDGDpptLPSGYSDDAQDFVAKCLNKIPNRRPTYAQLLEHPWLVKY 268
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
112-283 2.86e-08

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: 54.74  E-value: 2.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 112 GNMANAIKkARGKLFPEE--RIFKWLAQlllAVNYLHSNRVVHMDLTCSNiFLPKDD---HVQLGNYGLAKLINPEK-PV 185
Cdd:cd13976   69 GDLHSYVR-SRKRLREPEaaRLFRQIAS---AVAHCHRNGIVLRDLKLRK-FVFADEertKLRLESLEDAVILEGEDdSL 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 186 SMVSGISNSMCPEVLEDQPY--GYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSpLPIVYSSTLKQMIKLM 263
Cdd:cd13976  144 SDKHGCPAYVSPEILNSGATysGKAADVWSLGVILYTMLVGRYPFHDSEPASLFAKIRRGQFA-IPETLSPRARCLIRSL 222
                        170       180
                 ....*....|....*....|
gi 334185276 264 LRKKPEYRPTACELLRNPSL 283
Cdd:cd13976  223 LRREPSERLTAEDILLHPWL 242
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
65-221 3.06e-08

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: 55.80  E-value: 3.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  65 QEISRAVINYDLMKLLSSLKNpyivhyedswIDNDNNAC-------IFTAYYEGGNMANAIKKARG----------KLFP 127
Cdd:cd05100   59 KDLSDLVSEMEMMKMIGKHKN----------IINLLGACtqdgplyVLVEYASKGNLREYLRARRPpgmdysfdtcKLPE 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 128 EERIFKWLA----QLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLA----------KLINPEKPVSMvsgisn 193
Cdd:cd05100  129 EQLTFKDLVscayQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLArdvhnidyykKTTNGRLPVKW------ 202
                        170       180
                 ....*....|....*....|....*...
gi 334185276 194 sMCPEVLEDQPYGYKSDIWSLGCCMYEI 221
Cdd:cd05100  203 -MAPEALFDRVYTHQSDVWSFGVLLWEI 229
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
110-277 3.67e-08

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: 55.25  E-value: 3.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 110 EGGNMANAIKKARgklfPEERIFK-WLAQLLLAVNYLHSNRVVHMDLTCSNIFLPK---DDHVQLGNYGLAKL-----IN 180
Cdd:cd13977  118 DGGDMNEYLLSRR----PDRQTNTsFMLQLSSALAFLHRNQIVHRDLKPDNILISHkrgEPILKVADFGLSKVcsgsgLN 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 181 PEKPV-------SMVSGISNSMCPEVLEDQpYGYKSDIWSLGCCMY----EIT--------------AHQPAFKAPDMAG 235
Cdd:cd13977  194 PEEPAnvnkhflSSACGSDFYMAPEVWEGH-YTAKADIFALGIIIWamveRITfrdgetkkellgtyIQQGKEIVPLGEA 272
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 334185276 236 LINKINRSLMSPLPIVYS--STLKQMIKLMLRKKPEYRPTACEL 277
Cdd:cd13977  273 LLENPKLELQIPLKKKKSmnDDMKQLLRDMLAANPQERPDAFQL 316
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
31-281 3.98e-08

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: 54.78  E-value: 3.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  31 SSDFVVLHDIEDKK----YAMKKICLAKHTDklkqtalQEISRAVINYdlmkllSSLKNPYIVHYEDSWIDNDNNAcIFT 106
Cdd:cd14662   10 SGNFGVARLMRNKEtkelVAVKYIERGLKID-------ENVQREIINH------RSLRHPNIIRFKEVVLTPTHLA-IVM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 107 AYYEGGNMANAIKKArGKlFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKD--DHVQLGNYGLAK-LINPEK 183
Cdd:cd14662   76 EYAAGGELFERICNA-GR-FSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSpaPRLKICDFGYSKsSVLHSQ 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 184 PVSMVsGISNSMCPEVLEDQPY-GYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMS-----PLPIVYSSTLK 257
Cdd:cd14662  154 PKSTV-GTPAYIAPEVLSRKEYdGKVADVWSCGVTLYVMLVGAYPFEDPDDPKNFRKTIQRIMSvqykiPDYVRVSQDCR 232
                        250       260
                 ....*....|....*....|....
gi 334185276 258 QMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd14662  233 HLLSRIFVANPAKRITIPEIKNHP 256
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
56-226 4.49e-08

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: 54.73  E-value: 4.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  56 TDKLKQTALQEisravinydlMKLLSSLKNPYIVHYEDSWIDNDNNACIFTaYYEGGNMANAIKKARGKLFPEERI-FKW 134
Cdd:cd05044   39 TDQEKAEFLKE----------AHLMSNFKHPNILKLLGVCLDNDPQYIILE-LMEGGDLLSYLRAARPTAFTPPLLtLKD 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 135 LAQLLLAV----NYLHSNRVVHMDLTCSNIFL----PKDDHVQLGNYGLAKLINPEK----------PVSMvsgisnsMC 196
Cdd:cd05044  108 LLSICVDVakgcVYLEDMHFVHRDLAARNCLVsskdYRERVVKIGDFGLARDIYKNDyyrkegegllPVRW-------MA 180
                        170       180       190
                 ....*....|....*....|....*....|..
gi 334185276 197 PEVLEDQPYGYKSDIWSLGCCMYEIT--AHQP 226
Cdd:cd05044  181 PESLVDGVFTTQSDVWAFGVLMWEILtlGQQP 212
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
104-280 4.90e-08

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


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 54.50  E-value: 4.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 104 IFTAYYEGGNMANAIKKARGKLFPEErIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEK 183
Cdd:cd05113   76 IITEYMANGCLLNYLREMRKRFQTQQ-LLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVLDDE 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 184 PVSMVSG---ISNSmCPEVLEDQPYGYKSDIWSLGCCMYEI-TAHQPAFKAPDMAGLINKINRSLMSPLPIVYSSTLKQM 259
Cdd:cd05113  155 YTSSVGSkfpVRWS-PPEVLMYSKFSSKSDVWAFGVLMWEVySLGKMPYERFTNSETVEHVSQGLRLYRPHLASEKVYTI 233
                        170       180
                 ....*....|....*....|.
gi 334185276 260 IKLMLRKKPEYRPTACELLRN 280
Cdd:cd05113  234 MYSCWHEKADERPTFKILLSN 254
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
131-288 7.82e-08

Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER4 (ErbB4) 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. Ligands that bind HER4 fall into two groups, the neuregulins (or heregulins) and some EGFR (HER1) ligands including betacellulin, HBEGF, and epiregulin. All four neuregulins (NRG1-4) interact with HER4. Upon ligand binding, HER4 forms homo- or heterodimers with other HER proteins. HER4 is essential in embryonic development. It is implicated in mammary gland, cardiac, and neural development. As a postsynaptic receptor of NRG1, HER4 plays an important role in synaptic plasticity and maturation. The impairment of NRG1/HER4 signaling may contribute to schizophrenia. The HER4 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: 173655 [Multi-domain]  Cd Length: 303  Bit Score: 54.30  E-value: 7.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 131 IFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGIS---NSMCPEVLEDQPYGY 207
Cdd:cd05110  111 LLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLARLLEGDEKEYNADGGKmpiKWMALECIHYRKFTH 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 208 KSDIWSLGCCMYEITAHQ-------PAFKAPDmagLINKINRsLMSPlPIVYSSTLKQMIKLML---RKKPEYRPTACE- 276
Cdd:cd05110  191 QSDVWSYGVTIWELMTFGgkpydgiPTREIPD---LLEKGER-LPQP-PICTIDVYMVMVKCWMidaDSRPKFKELAAEf 265
                        170
                 ....*....|....
gi 334185276 277 --LLRNPslQPYLL 288
Cdd:cd05110  266 srMARDP--QRYLV 277
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
136-273 8.27e-08

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: 53.95  E-value: 8.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 136 AQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNSM---CPEVLEDQPYGYKSDIW 212
Cdd:cd05068  111 AQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFGLARVIKVEDEYEAREGAKFPIkwtAPEAANYNRFSIKSDVW 190
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334185276 213 SLGCCMYEITAHQpAFKAPDMAG--LINKINRSLMSPLPivySSTLKQMIKLML---RKKPEYRPT 273
Cdd:cd05068  191 SFGILLTEIVTYG-RIPYPGMTNaeVLQQVERGYRMPCP---PNCPPQLYDIMLecwKADPMERPT 252
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
78-273 9.06e-08

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: 53.66  E-value: 9.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  78 KLLSSLKNPYIVHYEDSWIDNDNNACIFTaYYEGGNMANAIKKARGKLFPEERIfkwLAQLLLAVNYLHSNRVVHMDLTC 157
Cdd:cd14027   43 KMMNRLRHSRVVKLLGVILEEGKYSLVME-YMEKGNLMHVLKKVSVPLSVKGRI---ILEIIEGMAYLHGKGVIHKDLKP 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 158 SNIFLPKDDHVQLGNYGLA------KLINPE-KPVSMVSGISNS-------MCPEVLED---QPyGYKSDIWSLGCCMYE 220
Cdd:cd14027  119 ENILVDNDFHIKIADLGLAsfkmwsKLTKEEhNEQREVDGTAKKnagtlyyMAPEHLNDvnaKP-TEKSDVYSFAIVLWA 197
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 334185276 221 ITA----HQPAFKAPDMAGLINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPT 273
Cdd:cd14027  198 IFAnkepYENAINEDQIIMCIKSGNRPDVDDITEYCPREIIDLMKLCWEANPEARPT 254
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
97-240 1.06e-07

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: 53.43  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  97 DNDNNACIFTAYYEGGNMANAIKKARGKLFPEERIFkWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKD--DHVQLGNYG 174
Cdd:cd14192   71 ESKTNLTLIMEYVDGGELFDRITDESYQLTELDAIL-FTRQICEGVHYLHQHYILHLDLKPENILCVNStgNQIKIIDFG 149
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334185276 175 LAKLINPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKI 240
Cdd:cd14192  150 LARRYKPREKLKVNFGTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNNI 215
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
135-278 1.27e-07

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: 53.91  E-value: 1.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 135 LAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKlINPEKPVSMVSGISNS--MCPEVLED-QPYGYKSDI 211
Cdd:cd07858  114 LYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLAR-TTSEKGDFMTEYVVTRwyRAPELLLNcSEYTTAIDV 192
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185276 212 WSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSP----LPIVYSSTLKQMIKLM--------LRKKPEYRPTACELL 278
Cdd:cd07858  193 WSVGCIFAELLGRKPLFPGKDYVHQLKLITELLGSPseedLGFIRNEKARRYIRSLpytprqsfARLFPHANPLAIDLL 271
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
136-278 1.39e-07

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: 53.24  E-value: 1.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 136 AQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAK---------LINPEKPVSMvsgisnsMCPEVLEDQPYG 206
Cdd:cd05046  124 TQIALGMDHLSNARFVHRDLAARNCLVSSQREVKVSLLSLSKdvynseyykLRNALIPLRW-------LAPEAVQEDDFS 196
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334185276 207 YKSDIWSLGCCMYEI--TAHQPAFKAPDMAGLINKINRSLMSPLPivySSTLKQMIKLMLR---KKPEYRPTACELL 278
Cdd:cd05046  197 TKSDVWSFGVLMWEVftQGELPFYGLSDEEVLNRLQAGKLELPVP---EGCPSRLYKLMTRcwaVNPKDRPSFSELV 270
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
36-221 1.39e-07

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: 53.04  E-value: 1.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  36 VLHDIEDKKYAMKKicLAKHTDKLKQTALQEIsravinydlmKLLSSLKNPYI-----VHYEDSWIDndnnacIFTAYYE 110
Cdd:cd14221   12 VTHRETGEVMVMKE--LIRFDEETQRTFLKEV----------KVMRCLEHPNVlkfigVLYKDKRLN------FITEYIK 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 111 GGNMANAIKKARGKlFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLI-----NPEKPV 185
Cdd:cd14221   74 GGTLRGIIKSMDSH-YPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLARLMvdektQPEGLR 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 334185276 186 SM----------VSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEI 221
Cdd:cd14221  153 SLkkpdrkkrytVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEI 198
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
38-267 1.49e-07

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: 53.70  E-value: 1.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  38 HDIEDKKYAMKKIclaKHTDKLKQTALQEIsravinyDLMKLLSSL--KNPYIVHYEDSWIDNDNNACIFtayYE--GGN 113
Cdd:cd14213   34 HKMGGMHVAVKIV---KNVDRYREAARSEI-------QVLEHLNTTdpNSTFRCVQMLEWFDHHGHVCIV---FEllGLS 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 114 MANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAK----LINPEKPV---- 185
Cdd:cd14213  101 TYDFIKENSFLPFPIDHIRNMAYQICKSVNFLHHNKLTHTDLKPENILFVQSDYVVKYNPKMKRdertLKNPDIKVvdfg 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 186 ---------SMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRsLMSPLPivysstl 256
Cdd:cd14213  181 satyddehhSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFQTHDSKEHLAMMER-ILGPLP------- 252
                        250
                 ....*....|.
gi 334185276 257 KQMIKLMLRKK 267
Cdd:cd14213  253 KHMIQKTRKRK 263
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
126-221 1.58e-07

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: 53.09  E-value: 1.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 126 FPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLIN----------PEKPVSMVSgisnsm 195
Cdd:cd05075  110 LPTQMLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADFGLSKKIYngdyyrqgriSKMPVKWIA------ 183
                         90       100
                 ....*....|....*....|....*.
gi 334185276 196 cPEVLEDQPYGYKSDIWSLGCCMYEI 221
Cdd:cd05075  184 -IESLADRVYTTKSDVWSFGVTMWEI 208
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
78-277 1.78e-07

Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Syk-like subfamily is composed of Syk, ZAP-70, Shark, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. They are involved in the signaling downstream of activated receptors (including B-cell, T-cell, and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. Syk is important in B-cell receptor signaling, while Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor signaling. Syk also plays a central role in Fc receptor-mediated phagocytosis in the adaptive immune system. Shark is exclusively expressed in ectodermally derived epithelia, and is localized preferentially to the apical surface of the epithelial cells, it may play a role in a signaling pathway for epithelial cell polarity. The Syk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 52.74  E-value: 1.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  78 KLLSSLKNPYIVHY-----EDSWidndnnaCIFTAYYEGGNMANAIKKARgkLFPEERIFKWLAQLLLAVNYLHSNRVVH 152
Cdd:cd05060   48 SVMAQLDHPCIVRLigvckGEPL-------MLVMELAPLGPLLKYLKKRR--EIPVSDLKELAHQVAMGMAYLESKHFVH 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 153 MDLTCSNIFLPKDDHVQLGNYGLAKLINPEK-----------PVSMVSgisnsmcPEVLEDQPYGYKSDIWSLGCCMYEI 221
Cdd:cd05060  119 RDLAARNVLLVNRHQAKISDFGMSRALGAGSdyyrattagrwPLKWYA-------PECINYGKFSSKSDVWSYGVTLWEA 191
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334185276 222 TAH--QP--AFKAPDMAGLINKINRsLMSP--LPI-VYSstlkqmikLMLR---KKPEYRPTACEL 277
Cdd:cd05060  192 FSYgaKPygEMKGPEVIAMLESGER-LPRPeeCPQeIYS--------IMLScwkYRPEDRPTFSEL 248
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
104-273 1.83e-07

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: 52.76  E-value: 1.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 104 IFTAYYEGGNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINpEK 183
Cdd:cd05070   80 IVTEYMSKGSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIE-DN 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 184 PVSMVSGISNSM---CPEVLEDQPYGYKSDIWSLGCCMYE-ITAHQPAFKAPDMAGLINKINRSLMSPLPIVYSSTLKQM 259
Cdd:cd05070  159 EYTARQGAKFPIkwtAPEAALYGRFTIKSDVWSFGILLTElVTKGRVPYPGMNNREVLEQVERGYRMPCPQDCPISLHEL 238
                        170
                 ....*....|....
gi 334185276 260 IKLMLRKKPEYRPT 273
Cdd:cd05070  239 MIHCWKKDPEERPT 252
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
100-221 1.89e-07

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: 52.57  E-value: 1.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 100 NNACIFTAYYEGGNMANAIKkARGK-LFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAK- 177
Cdd:cd05083   71 NGLYIVMELMSKGNLVNFLR-SRGRaLVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAKv 149
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 334185276 178 ----LINPEKPVSMVSgisnsmcPEVLEDQPYGYKSDIWSLGCCMYEI 221
Cdd:cd05083  150 gsmgVDNSRLPVKWTA-------PEALKNKKFSSKSDVWSYGVLLWEV 190
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
104-273 2.09e-07

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


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 52.23  E-value: 2.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 104 IFTAYYEGGNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEK 183
Cdd:cd14203   66 IVTEFMSKGSLLDFLKDGEGKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNE 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 184 ---------PVSMVSgisnsmcPEVLEDQPYGYKSDIWSLGCCMYEITAhQPAFKAPDMAG--LINKINRSLMSPLPIVY 252
Cdd:cd14203  146 ytarqgakfPIKWTA-------PEAALYGRFTIKSDVWSFGILLTELVT-KGRVPYPGMNNreVLEQVERGYRMPCPPGC 217
                        170       180
                 ....*....|....*....|.
gi 334185276 253 SSTLKQMIKLMLRKKPEYRPT 273
Cdd:cd14203  218 PESLHELMCQCWRKDPEERPT 238
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
137-221 2.33e-07

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


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 53.06  E-value: 2.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 137 QLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEkPVSMVSGISNS----MCPEVLEDQPYGYKSDIW 212
Cdd:cd05103  187 QVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKD-PDYVRKGDARLplkwMAPETIFDRVYTIQSDVW 265

                 ....*....
gi 334185276 213 SLGCCMYEI 221
Cdd:cd05103  266 SFGVLLWEI 274
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
78-280 2.59e-07

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


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 52.27  E-value: 2.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  78 KLLSSLKNPYIVHY-----EDSWIdndnnacIFTAYYEGGNMANAIKKARGklFPEERIFKWLAQLLLAVNYLHSNRVVH 152
Cdd:cd05116   48 NVMQQLDNPYIVRMigiceAESWM-------LVMEMAELGPLNKFLQKNRH--VTEKNITELVHQVSMGMKYLEESNFVH 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 153 MDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGIS----NSMCPEVLEDQPYGYKSDIWSLGCCMYEITAH--QP 226
Cdd:cd05116  119 RDLAARNVLLVTQHYAKISDFGLSKALRADENYYKAQTHGkwpvKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSYgqKP 198
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 334185276 227 --AFKAPDMAGLINKINRslMSPlPIVYSSTLKQMIKLMLRKKPEYRP--TACEL-LRN 280
Cdd:cd05116  199 ykGMKGNEVTQMIEKGER--MEC-PAGCPPEMYDLMKLCWTYDVDERPgfAAVELrLRN 254
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
19-240 2.61e-07

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: 52.56  E-value: 2.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  19 YHVVEQVRRGKSSSDFVVLHDIEDKKYaMKKICLAKHTDKlkQTALQEISravinydlmkLLSSLKNPYIVHYEDSWIDN 98
Cdd:cd14104    2 YMIAEELGRGQFGIVHRCVETSSKKTY-MAKFVKVKGADQ--VLVKKEIS----------ILNIARHRNILRLHESFESH 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  99 DNNACIFTaYYEGGNMANAIKKARGKLfPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNI--FLPKDDHVQLGNYGLA 176
Cdd:cd14104   69 EELVMIFE-FISGVDIFERITTARFEL-NEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIiyCTRRGSYIKIIEFGQS 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334185276 177 KLINPEKPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKI 240
Cdd:cd14104  147 RQLKPGDKFRLQYTSAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENI 210
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
110-273 2.93e-07

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: 51.96  E-value: 2.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 110 EGGNMANAIKKARGKlFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAK---------LIN 180
Cdd:cd05040   80 PLGSLLDRLRKDQGH-FLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGLMRalpqnedhyVMQ 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 181 PEKPVSMvsgisnSMC-PEVLEDQPYGYKSDIWSLGCCMYEI--TAHQP--AFKAPDMAGLINKINRSLmsPLPIVYSST 255
Cdd:cd05040  159 EHRKVPF------AWCaPESLKTRKFSHASDVWMFGVTLWEMftYGEEPwlGLNGSQILEKIDKEGERL--ERPDDCPQD 230
                        170
                 ....*....|....*...
gi 334185276 256 LKQMIKLMLRKKPEYRPT 273
Cdd:cd05040  231 IYNVMLQCWAHKPADRPT 248
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
81-223 3.10e-07

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: 52.38  E-value: 3.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  81 SSLKNPYIVHY---EDSWIDNDNNACIFTAYYEGGNMANAIKKargklfpeeRIFKWLAQLLLA------VNYLHSNR-- 149
Cdd:cd14055   50 ASLKHENILQFltaEERGVGLDRQYWLITAYHENGSLQDYLTR---------HILSWEDLCKMAgslargLAHLHSDRtp 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 150 -------VVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPV-----SMVSGISNSMCPEVLE------DQPYGYKSDI 211
Cdd:cd14055  121 cgrpkipIAHRDLKSSNILVKNDGTCVLADFGLALRLDPSLSVdelanSGQVGTARYMAPEALEsrvnleDLESFKQIDV 200
                        170
                 ....*....|..
gi 334185276 212 WSLGCCMYEITA 223
Cdd:cd14055  201 YSMALVLWEMAS 212
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
44-281 3.23e-07

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: 51.88  E-value: 3.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  44 KYAMKKICLAKHTDKlkQTALQEISRAVINYDLMK----LLSSLKNPYIVHYEDSWiDNDNNACIFTAYYEGGNMANAIK 119
Cdd:cd14115    5 RFSIVKKCLHKATRK--DVAVKFVSKKMKKKEQAAheaaLLQHLQHPQYITLHDTY-ESPTSYILVLELMDDGRLLDYLM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 120 kARGKLFpEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFL------PKddhVQLGNYGLAKLINPEKPVSMVSGISN 193
Cdd:cd14115   82 -NHDELM-EEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIdlripvPR---VKLIDLEDAVQISGHRHVHHLLGNPE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 194 SMCPEVLEDQPYGYKSDIWSLGCCMY-EITAHQPAFKAPDMAGLINkINRSLMSpLPIVY----SSTLKQMIKLMLRKKP 268
Cdd:cd14115  157 FAAPEVIQGTPVSLATDIWSIGVLTYvMLSGVSPFLDESKEETCIN-VCRVDFS-FPDEYfgdvSQAARDFINVILQEDP 234
                        250
                 ....*....|...
gi 334185276 269 EYRPTACELLRNP 281
Cdd:cd14115  235 RRRPTAATCLQHP 247
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
39-221 3.80e-07

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: 51.94  E-value: 3.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  39 DIEDKKYAMKKIclakH------TDKLKQTAlqeISRAVINYDLMKllsSLKNPYIVHYEDSW-IDNDNnACIFTAYYEG 111
Cdd:cd13990   21 DLVEQRYVACKI----HqlnkdwSEEKKQNY---IKHALREYEIHK---SLDHPRIVKLYDVFeIDTDS-FCTVLEYCDG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 112 GNMANAIKkaRGKLFPEERIFKWLAQLLLAVNYL--HSNRVVHMDLTCSNIFLPKDDH---VQLGNYGLAKLINPEkpvs 186
Cdd:cd13990   90 NDLDFYLK--QHKSIPEREARSIIMQVVSALKYLneIKPPIIHYDLKPGNILLHSGNVsgeIKITDFGLSKIMDDE---- 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 334185276 187 mvSGISNSM----------------CPEVLEDQP-YGYKSDIWSLGCCMYEI 221
Cdd:cd13990  164 --SYNSDGMeltsqgagtywylppeCFVVGKTPPkISSKVDVWSVGVIFYQM 213
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
137-274 3.95e-07

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


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 51.85  E-value: 3.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 137 QLLLAVNYLHSNRVVHMDLTCSNIFL-----PKDDHVQLGNYGLAKLINPEKpVSMVSGISNSMCPEVLE-DQPYGYKSD 210
Cdd:cd14000  120 QVADGLRYLHSAMIIYRDLKSHNVLVwtlypNSAIIIKIADYGISRQCCRMG-AKGSEGTPGFRAPEIARgNVIYNEKVD 198
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334185276 211 IWSLGCCMYE-ITAHQPAF---KAPDMAGLINKINRSLMSPlPIVYSSTLKQMIKLMLRKKPEYRPTA 274
Cdd:cd14000  199 VFSFGMLLYEiLSGGAPMVghlKFPNEFDIHGGLRPPLKQY-ECAPWPEVEVLMKKCWKENPQQRPTA 265
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
112-281 4.18e-07

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


Pssm-ID: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 51.58  E-value: 4.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 112 GNMANAIKKArgKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAK---LINPEKPVSMV 188
Cdd:cd14022   69 GDMHSFVRTC--KKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKDEERTRVKLESLEDayiLRGHDDSLSDK 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 189 SGISNSMCPEVLEDQ-PY-GYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSpLPIVYSSTLKQMIKLMLRK 266
Cdd:cd14022  147 HGCPAYVSPEILNTSgSYsGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFN-IPETLSPKAKCLIRSILRR 225
                        170
                 ....*....|....*
gi 334185276 267 KPEYRPTACELLRNP 281
Cdd:cd14022  226 EPSERLTSQEILDHP 240
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
144-279 5.58e-07

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: 51.32  E-value: 5.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 144 YLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINpEKPVSMVSGISNSMCP------EVLEDQPYGYKSDIWSLGCC 217
Cdd:cd05058  113 YLASKKFVHRDLAARNCMLDESFTVKVADFGLARDIY-DKEYYSVHNHTGAKLPvkwmalESLQTQKFTTKSDVWSFGVL 191
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334185276 218 MYEI-TAHQPAFKAPDMAGLINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLR 279
Cdd:cd05058  192 LWELmTRGAPPYPDVDSFDITVYLLQGRRLLQPEYCPDPLYEVMLSCWHPKPEMRPTFSELVS 254
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
127-273 5.99e-07

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: 51.34  E-value: 5.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 127 PEERIFKWLAQLLLAVNYLHSNR--VVHMDLTCSNIFLPKDDHVQLGNYGLAK--------LINPEKPVSMVSGISNSMC 196
Cdd:cd14025   90 PWELRFRIIHETAVGMNFLHCMKppLLHLDLKPANILLDAHYHVKISDFGLAKwnglshshDLSRDGLRGTIAYLPPERF 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 197 PEvlEDQPYGYKSDIWSLGCCMYEI-TAHQPAFKAPDMAGLINKI---NRSLMSPLPIVYSSTLKQMIKLMLR---KKPE 269
Cdd:cd14025  170 KE--KNRCPDTKHDVYSFAIVIWGIlTQKKPFAGENNILHIMVKVvkgHRPSLSPIPRQRPSECQQMICLMKRcwdQDPR 247

                 ....
gi 334185276 270 YRPT 273
Cdd:cd14025  248 KRPT 251
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
103-290 6.00e-07

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: 51.46  E-value: 6.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 103 CIFTAYYEGGNMANAIKkaRGKLFPEERI---FKWLAQLLLAVNYLH--SNRVVHMDLTCSNIFLPKDDHVQLGNYGLAK 177
Cdd:cd14026   73 GIVTEYMTNGSLNELLH--EKDIYPDVAWplrLRILYEIALGVNYLHnmSPPLLHHDLKTQNILLDGEFHVKIADFGLSK 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 178 LinpeKPVSMVSGISNSMCPE---VLEDQPYGY----------KSDIWSLGCCMYEITAHQPAFKapdmaglinkinrSL 244
Cdd:cd14026  151 W----RQLSISQSRSSKSAPEggtIIYMPPEEYepsqkrrasvKHDIYSYAIIMWEVLSRKIPFE-------------EV 213
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 334185276 245 MSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLR--------NPSLQPYLLQC 290
Cdd:cd14026  214 TNPLQIMYSVSQGHRPDTGEDSLPVDIPHRATLINliesgwaqNPDERPSFLKC 267
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
144-230 6.52e-07

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: 50.96  E-value: 6.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 144 YLH---SNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSM--VSGISNSMCPEVLEDQPYGYKSDIWSLGCCM 218
Cdd:cd14664  109 YLHhdcSPLIIHRDVKSNNILLDEEFEAHVADFGLAKLMDDKDSHVMssVAGSYGYIAPEYAYTGKVSEKSDVYSYGVVL 188
                         90
                 ....*....|..
gi 334185276 219 YEITAHQPAFKA 230
Cdd:cd14664  189 LELITGKRPFDE 200
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
137-221 8.05e-07

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


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 51.13  E-value: 8.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 137 QLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEkPVSMVSGISNS----MCPEVLEDQPYGYKSDIW 212
Cdd:cd05102  180 QVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKD-PDYVRKGSARLplkwMAPESIFDKVYTTQSDVW 258

                 ....*....
gi 334185276 213 SLGCCMYEI 221
Cdd:cd05102  259 SFGVLLWEI 267
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
123-284 8.75e-07

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


Pssm-ID: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 50.74  E-value: 8.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 123 GKLFPE-ERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPE-------KPVSMVSGisns 194
Cdd:cd05061  112 GRPPPTlQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKIGDFGMTRDIYETdyyrkggKGLLPVRW---- 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 195 MCPEVLEDQPYGYKSDIWSLGCCMYEIT--AHQPafkapdMAGLIN-KINRSLMS----PLPIVYSSTLKQMIKLMLRKK 267
Cdd:cd05061  188 MAPESLKDGVFTTSSDMWSFGVVLWEITslAEQP------YQGLSNeQVLKFVMDggylDQPDNCPERVTDLMRMCWQFN 261
                        170       180
                 ....*....|....*....|...
gi 334185276 268 PEYRPTACELLR------NPSLQ 284
Cdd:cd05061  262 PKMRPTFLEIVNllkddlHPSFP 284
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
126-219 9.21e-07

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


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 50.61  E-value: 9.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 126 FPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQ--LGNYGLAKLINPEKPVSmVSGISNSMCPEVLEDQ 203
Cdd:cd14112   96 YSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSVRSWQvkLVDFGRAQKVSKLGKVP-VDGDTDWASPEFHNPE 174
                         90
                 ....*....|....*..
gi 334185276 204 PYGY-KSDIWSLGCCMY 219
Cdd:cd14112  175 TPITvQSDIWGLGVLTF 191
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
120-226 9.35e-07

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 51.72  E-value: 9.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 120 KARGKLFPEERIfKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINpekpvsmVSGI--SNSM-- 195
Cdd:NF033483  99 REHGPLSPEEAV-EIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIARALS-------STTMtqTNSVlg 170
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 334185276 196 -----CPEVLEDQPYGYKSDIWSLGCCMYE-ITAHQP 226
Cdd:NF033483 171 tvhylSPEQARGGTVDARSDIYSLGIVLYEmLTGRPP 207
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
108-271 1.02e-06

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: 50.69  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 108 YYEGGNMANAIKKARGKL-FPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLP----KDDHvQLGNYGLAKLINPE 182
Cdd:cd14039   77 YCSGGDLRKLLNKPENCCgLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQeingKIVH-KIIDLGYAKDLDQG 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 183 KPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITA----------------------HQPAFKAPDMAGlinKI 240
Cdd:cd14039  156 SLCTSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAgfrpflhnlqpftwhekikkkdPKHIFAVEEMNG---EV 232
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 334185276 241 NRSLMSPLPIVYSST----LKQMIKLMLRKKPEYR 271
Cdd:cd14039  233 RFSTHLPQPNNLCSLivepMEGWLQLMLNWDPVQR 267
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
17-244 1.26e-06

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: 50.62  E-value: 1.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  17 DNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKiclakhtdkLKQTALQEISRAVinydlmKLLSSLKN-PYIVHYEDSW 95
Cdd:cd14132   18 DDYEIIRKIGRGKYSEVFEGINIGNNEKVVIKV---------LKPVKKKKIKREI------KILQNLRGgPNIVKLLDVV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  96 IDNDNNACIF-TAYYEggnmANAIKKARGKLFPEErIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFL-PKDDHVQLGNY 173
Cdd:cd14132   83 KDPQSKTPSLiFEYVN----NTDFKTLYPTLTDYD-IRYYMYELLKALDYCHSKGIMHRDVKPHNIMIdHEKRKLRLIDW 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334185276 174 GLAKLINPEKPVSMVSGISNSMCPEVLED-QPYGYKSDIWSLGCCMYE-ITAHQPAFKAPDMAGLINKINRSL 244
Cdd:cd14132  158 GLAEFYHPGQEYNVRVASRYYKGPELLVDyQYYDYSLDMWSLGCMLASmIFRKEPFFHGHDNYDQLVKIAKVL 230
STKc_VRK cd14015
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase; STKs ...
118-176 1.28e-06

Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. They play important roles in cell signaling, nuclear envelope dynamics, apoptosis, and stress responses. Vertebrates contain three VRK proteins (VRK1, VRK2, and VRK3) while invertebrates, specifically fruit flies and nematodes, seem to carry only a single ortholog. Mutations of VRK in Drosophila and Caenorhabditis elegans showed varying phenotypes ranging from embryonic lethality to mitotic and meiotic defects resulting in sterility. In vertebrates, VRK1 is implicated in cell cycle progression and proliferation, nuclear envelope assembly, and chromatin condensation. VRK2 is involved in modulating JNK signaling. VRK3 is an inactive pseudokinase that inhibits ERK signaling. The VRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270917 [Multi-domain]  Cd Length: 300  Bit Score: 50.36  E-value: 1.28e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334185276 118 IKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFL---PKDDHVQLGNYGLA 176
Cdd:cd14015  116 IFEKNGKRFPEKTVLQLALRILDVLEYIHENGYVHADIKASNLLLgfgKNKDQVYLVDYGLA 177
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
43-281 1.33e-06

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: 50.55  E-value: 1.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  43 KKYAMKKIclakhtdklkQTALQEISRAVINYDLMKLLSSLKNPYIVHYEDSWIDNDNNAC--IFTAYYEGGNMANAIKK 120
Cdd:cd07859   26 EKVAIKKI----------NDVFEHVSDATRILREIKLLRLLRHPDIVEIKHIMLPPSRREFkdIYVVFELMESDLHQVIK 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 121 ARGKLFPEERIFkWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMV----SGISNSMC 196
Cdd:cd07859   96 ANDDLTPEHHQF-FLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLARVAFNDTPTAIFwtdyVATRWYRA 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 197 PEVLED--QPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPLPIV-----------YSSTLKQ----- 258
Cdd:cd07859  175 PELCGSffSKYTPAIDIWSIGCIFAEVLTGKPLFPGKNVVHQLDLITDLLGTPSPETisrvrnekarrYLSSMRKkqpvp 254
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 334185276 259 --------------MIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd07859  255 fsqkfpnadplalrLLERLLAFDPKDRPTAEEALADP 291
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
104-221 1.48e-06

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: 50.18  E-value: 1.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 104 IFTAYYEGGNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLI---- 179
Cdd:cd05055  116 VITEYCCYGDLLNFLRRKRESFLTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTHGKIVKICDFGLARDImnds 195
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 334185276 180 ------NPEKPVSMvsgisnsMCPEVLEDQPYGYKSDIWSLGCCMYEI 221
Cdd:cd05055  196 nyvvkgNARLPVKW-------MAPESIFNCVYTFESDVWSYGILLWEI 236
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
124-222 1.83e-06

Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Mer (or Mertk) is named after its original reported expression pattern (monocytes, epithelial, and reproductive tissues). It is required for the ingestion of apoptotic cells by phagocytes such as macrophages, retinal pigment epithelial cells, and dendritic cells. Mer is also important in maintaining immune homeostasis. Mer is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Mer subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271106 [Multi-domain]  Cd Length: 284  Bit Score: 49.93  E-value: 1.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 124 KLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLIN----------PEKPVSMVSgisn 193
Cdd:cd14204  115 QHVPLQTLLKFMIDIALGMEYLSSRNFLHRDLAARNCMLRDDMTVCVADFGLSKKIYsgdyyrqgriAKMPVKWIA---- 190
                         90       100
                 ....*....|....*....|....*....
gi 334185276 194 smcPEVLEDQPYGYKSDIWSLGCCMYEIT 222
Cdd:cd14204  191 ---VESLADRVYTVKSDVWAFGVTMWEIA 216
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
137-277 1.88e-06

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: 49.57  E-value: 1.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 137 QLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAK-------LINPEK---PVSMVSgisnsmcPEVLE----- 201
Cdd:cd14206  115 EITLGLLHLHKNNYIHSDLALRNCLLTSDLTVRIGDYGLSHnnykedyYLTPDRlwiPLRWVA-------PELLDelhgn 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 202 ----DQpyGYKSDIWSLGCCMYEI--TAHQPAFKAPD---MAGLINKINRSLMSP-LPIVYSSTLKQMIKLMLRkKPEYR 271
Cdd:cd14206  188 livvDQ--SKESNVWSLGVTIWELfeFGAQPYRHLSDeevLTFVVREQQMKLAKPrLKLPYADYWYEIMQSCWL-PPSQR 264

                 ....*.
gi 334185276 272 PTACEL 277
Cdd:cd14206  265 PSVEEL 270
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
126-221 2.73e-06

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: 49.07  E-value: 2.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 126 FPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEK----------PVSMvsgisnsM 195
Cdd:cd05035  110 LPLQTLLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVCVADFGLSRKIYSGDyyrqgriskmPVKW-------I 182
                         90       100
                 ....*....|....*....|....*.
gi 334185276 196 CPEVLEDQPYGYKSDIWSLGCCMYEI 221
Cdd:cd05035  183 ALESLADNVYTSKSDVWSFGVTMWEI 208
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
17-245 2.95e-06

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: 49.31  E-value: 2.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  17 DNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKKICLaKHTDKLKQTALQEISravinydlmkLLSSLKNPYIVHYEDSWI 96
Cdd:cd07869    5 DSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRL-QEEEGTPFTAIREAS----------LLKGLKHANIVLLHDIIH 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  97 DNDNNACIFTayYEGGNMANAIKKARGKLFPEErIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLA 176
Cdd:cd07869   74 TKETLTLVFE--YVHTDLCQYMDKHPGGLHPEN-VKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLA 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334185276 177 KLIN-PEKPVSMVSGISNSMCPEV-LEDQPYGYKSDIWSLGCCMYEITAHQPAFkaPDMAGLINKINRSLM 245
Cdd:cd07869  151 RAKSvPSHTYSNEVVTLWYRPPDVlLGSTEYSTCLDMWGVGCIFVEMIQGVAAF--PGMKDIQDQLERIFL 219
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
99-228 3.00e-06

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: 49.26  E-value: 3.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  99 DNNACIFTAY--YEGGNMANAIKKArgKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQ------- 169
Cdd:cd14174   70 EDDTRFYLVFekLRGGSILAHIQKR--KHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPDKVSpvkicdf 147
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 170 -LG-----NYGLAKLINPEkpVSMVSGISNSMCPEVLE---DQP--YGYKSDIWSLGCCMYEITAHQPAF 228
Cdd:cd14174  148 dLGsgvklNSACTPITTPE--LTTPCGSAEYMAPEVVEvftDEAtfYDKRCDLWSLGVILYIMLSGYPPF 215
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
137-302 3.26e-06

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 49.65  E-value: 3.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 137 QLLLAVNYLHSNRVVHMDLTCSNIFL-PKDDHVQLGNYGLAK-LINPEKPVSMVSGiSNSMCPEV-LEDQPYGYKSDIWS 213
Cdd:PTZ00036 178 QLCRALAYIHSKFICHRDLKPQNLLIdPNTHTLKLCDFGSAKnLLAGQRSVSYICS-RFYRAPELmLGATNYTTHIDLWS 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 214 LGCCMYEITAHQPAFKAPDMAGLINKINRSLMSP----------------LPIVYSSTLKQ------------MIKLMLR 265
Cdd:PTZ00036 257 LGCIIAEMILGYPIFSGQSSVDQLVRIIQVLGTPtedqlkemnpnyadikFPDVKPKDLKKvfpkgtpddainFISQFLK 336
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 334185276 266 KKPEYRPTACELLRNPSLQPYLLQCQNLsPIYLPVFP 302
Cdd:PTZ00036 337 YEPLKRLNPIEALADPFFDDLRDPCIKL-PKYIDKLP 372
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
131-281 3.43e-06

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: 48.76  E-value: 3.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 131 IFKWLAQLLLAVNYLHSNRVVHMDLTCSNiFL--PKDDHVQLGNYGLAKLINPEKP-VSMVSGISNSMCPEVL---EDQp 204
Cdd:cd14019  103 IRIYLRNLFKALKHVHSFGIIHRDVKPGN-FLynRETGKGVLVDFGLAQREEDRPEqRAPRAGTRGFRAPEVLfkcPHQ- 180
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185276 205 yGYKSDIWSLGCCM-YEITAHQPAFK-APDMAGLInkinrSLMSplpIVYSSTLKQMIKLMLRKKPEYRPTACELLRNP 281
Cdd:cd14019  181 -TTAIDIWSAGVILlSILSGRFPFFFsSDDIDALA-----EIAT---IFGSDEAYDLLDKLLELDPSKRITAEEALKHP 250
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
53-278 3.91e-06

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


Pssm-ID: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 48.71  E-value: 3.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  53 AKHTDKLKQTALQEISravinydlmkLLSSLKNPYIVHYEDSwIDNDNNACIFTAYYEGGNMANAIKKARGKlFPEERIF 132
Cdd:cd05066   42 AGYTEKQRRDFLSEAS----------IMGQFDHPNIIHLEGV-VTRSKPVMIVTEYMENGSLDAFLRKHDGQ-FTVIQLV 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 133 KWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLI--NPEKPVSMVSGI--SNSMCPEVLEDQPYGYK 208
Cdd:cd05066  110 GMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRVLedDPEAAYTTRGGKipIRWTAPEAIAYRKFTSA 189
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334185276 209 SDIWSLGCCMYEITAH--QPAFkapDMAG--LINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELL 278
Cdd:cd05066  190 SDVWSYGIVMWEVMSYgeRPYW---EMSNqdVIKAIEEGYRLPAPMDCPAALHQLMLDCWQKDRNERPKFEQIV 260
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
102-272 4.67e-06

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: 48.43  E-value: 4.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 102 ACIFTAYYEGGNMANAIKKARGKlFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLI-- 179
Cdd:cd05063   81 AMIITEYMENGALDKYLRDHDGE-FSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRVLed 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 180 NPEKPVSMVSGIS--NSMCPEVLEDQPYGYKSDIWSLGCCMYEITAH--QPAFkapDMAG--LINKINRSLMSPLPIVYS 253
Cdd:cd05063  160 DPEGTYTTSGGKIpiRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSFgeRPYW---DMSNheVMKAINDGFRLPAPMDCP 236
                        170
                 ....*....|....*....
gi 334185276 254 STLKQMIKLMLRKKPEYRP 272
Cdd:cd05063  237 SAVYQLMLQCWQQDRARRP 255
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
137-221 4.70e-06

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. 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: 48.64  E-value: 4.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 137 QLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEkPVSMVSGISNS----MCPEVLEDQPYGYKSDIW 212
Cdd:cd05054  146 QVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKD-PDYVRKGDARLplkwMAPESIFDKVYTTQSDVW 224

                 ....*....
gi 334185276 213 SLGCCMYEI 221
Cdd:cd05054  225 SFGVLLWEI 233
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
142-279 5.73e-06

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: 48.35  E-value: 5.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 142 VNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAK-------LINPEKPVSMVSGISNSMCPEV-----LEDQPygYKS 209
Cdd:cd05042  113 LAHLHKLNFVHSDLALRNCLLTSDLTVKIGDYGLAHsrykedyIETDDKLWFPLRWTAPELVTEFhdrllVVDQT--KYS 190
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334185276 210 DIWSLGCCMYEI--TAHQPAFKAPD---MAGLINKINRSLMSP-LPIVYSSTLKQMIKLMLRkKPEYRPTACELLR 279
Cdd:cd05042  191 NIWSLGVTLWELfeNGAQPYSNLSDldvLAQVVREQDTKLPKPqLELPYSDRWYEVLQFCWL-SPEQRPAAEDVHL 265
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
137-222 6.83e-06

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


Pssm-ID: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 48.22  E-value: 6.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 137 QLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLI----------NPEKPVSMvsgisnsMCPEVLEDQPYG 206
Cdd:cd05043  124 QIACGMSYLHRRGVIHKDIAARNCVIDDELQVKITDNALSRDLfpmdyhclgdNENRPIKW-------MSLESLVNKEYS 196
                         90
                 ....*....|....*.
gi 334185276 207 YKSDIWSLGCCMYEIT 222
Cdd:cd05043  197 SASDVWSFGVLLWELM 212
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
25-272 6.88e-06

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


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 48.15  E-value: 6.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  25 VRRGKSSsdfvvlhdIEDKKYAMKKICLaKHTDKLKQTALQEISravinydlmkLLSSLKNPYIV------HYEDS---- 94
Cdd:cd07844   16 VYKGRSK--------LTGQLVALKEIRL-EHEEGAPFTAIREAS----------LLKDLKHANIVtlhdiiHTKKTltlv 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  95 --WIDNDnnaciFTAYYE----GGNMANAikkargKLFpeerifkwLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHV 168
Cdd:cd07844   77 feYLDTD-----LKQYMDdcggGLSMHNV------RLF--------LFQLLRGLAYCHQRRVLHRDLKPQNLLISERGEL 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 169 QLGNYGLA--KLInPEKPVSmvsgisNSMC------PEVL-EDQPYGYKSDIWSLGCCMYEITAHQPAFK-APDMAGLIN 238
Cdd:cd07844  138 KLADFGLAraKSV-PSKTYS------NEVVtlwyrpPDVLlGSTEYSTSLDMWGVGCIFYEMATGRPLFPgSTDVEDQLH 210
                        250       260       270
                 ....*....|....*....|....*....|....
gi 334185276 239 KINRSLMSPLPIVYSStlkqmiklmLRKKPEYRP 272
Cdd:cd07844  211 KIFRVLGTPTEETWPG---------VSSNPEFKP 235
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
104-279 7.41e-06

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: 47.75  E-value: 7.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 104 IFTAYYEGGNMANAIKKARGKLFPEErIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEK 183
Cdd:cd05033   82 IVTEYMENGSLDKFLRENDGKFTVTQ-LVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLSRRLEDSE 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 184 PVSMVSGISNSM---CPEVLEDQPYGYKSDIWSLGCCMYEITAH--QPAFkapDMAG--LINKINRSLMSPLPIVYSSTL 256
Cdd:cd05033  161 ATYTTKGGKIPIrwtAPEAIAYRKFTSASDVWSFGIVMWEVMSYgeRPYW---DMSNqdVIKAVEDGYRLPPPMDCPSAL 237
                        170       180
                 ....*....|....*....|...
gi 334185276 257 KQMIKLMLRKKPEYRPTACELLR 279
Cdd:cd05033  238 YQLMLDCWQKDRNERPTFSQIVS 260
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
53-272 8.30e-06

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: 47.56  E-value: 8.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  53 AKHTDKLKQTALQEISravinydlmkLLSSLKNPYIVHYEDSwIDNDNNACIFTAYYEGGNMANAIKKARGKlFPEERIF 132
Cdd:cd05065   42 SGYTEKQRRDFLSEAS----------IMGQFDHPNIIHLEGV-VTKSRPVMIITEFMENGALDSFLRQNDGQ-FTVIQLV 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 133 KWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLI--NPEKPvSMVSGISNSM-----CPEVLEDQPY 205
Cdd:cd05065  110 GMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLedDTSDP-TYTSSLGGKIpirwtAPEAIAYRKF 188
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334185276 206 GYKSDIWSLGCCMYEITAH--QPAFkapDMAG--LINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRP 272
Cdd:cd05065  189 TSASDVWSYGIVMWEVMSYgeRPYW---DMSNqdVINAIEQDYRLPPPMDCPTALHQLMLDCWQKDRNLRP 256
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
112-277 8.47e-06

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: 47.68  E-value: 8.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 112 GNMANAIKKARG--KLFPEERIFKWLA-QLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEK----- 183
Cdd:cd05087   82 GDLKGYLRSCRAaeSMAPDPLTLQRMAcEVACGLLHLHRNNFVHSDLALRNCLLTADLTVKIGDYGLSHCKYKEDyfvta 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 184 -----PVSMVSgisnsmcPEVLeDQPYG--------YKSDIWSLGCCMYEI--TAHQPAFKAPDMAGLINKI-NRSLMSP 247
Cdd:cd05087  162 dqlwvPLRWIA-------PELV-DEVHGnllvvdqtKQSNVWSLGVTIWELfeLGNQPYRHYSDRQVLTYTVrEQQLKLP 233
                        170       180       190
                 ....*....|....*....|....*....|..
gi 334185276 248 LPIVYSSTLKQMIKLM--LRKKPEYRPTACEL 277
Cdd:cd05087  234 KPQLKLSLAERWYEVMqfCWLQPEQRPTAEEV 265
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
127-278 8.90e-06

Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. IGF-1R is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the ligand (IGF-1 or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, which stimulates downstream kinase activities and biological function. IGF-1R signaling is important in the differentiation, growth, and survival of normal cells. In cancer cells, where it is frequently overexpressed, IGF-1R is implicated in proliferation, the suppression of apoptosis, invasion, and metastasis. IGF-1R is being developed as a therapeutic target in cancer treatment. The IGF-1R subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133193 [Multi-domain]  Cd Length: 277  Bit Score: 47.72  E-value: 8.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 127 PEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINpEKPVSMVSGIS----NSMCPEVLED 202
Cdd:cd05062  117 SLKKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVKIGDFGMTRDIY-ETDYYRKGGKGllpvRWMSPESLKD 195
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334185276 203 QPYGYKSDIWSLGCCMYEIT--AHQPaFKAPDMAGLINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELL 278
Cdd:cd05062  196 GVFTTYSDVWSFGVVLWEIAtlAEQP-YQGMSNEQVLRFVMEGGLLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEII 272
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
127-221 1.24e-05

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: 47.16  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 127 PEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEkpvSMVSGISNSMC-PEVLEDQPY 205
Cdd:cd05576  111 PEECIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDS---CDSDAIENMYCaPEVGGISEE 187
                         90
                 ....*....|....*.
gi 334185276 206 GYKSDIWSLGCCMYEI 221
Cdd:cd05576  188 TEACDWWSLGALLFEL 203
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
142-228 1.32e-05

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: 47.11  E-value: 1.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 142 VNYLHSNRVVHMDLTCSNIFLpkDDHV--QLGNYGLAKlINPEKPVSM----VSGISNSMCPEVLEDQpYGYKSDIWSLG 215
Cdd:cd14158  130 INYLHENNHIHRDIKSANILL--DETFvpKISDFGLAR-ASEKFSQTImterIVGTTAYMAPEALRGE-ITPKSDIFSFG 205
                         90
                 ....*....|...
gi 334185276 216 CCMYEITAHQPAF 228
Cdd:cd14158  206 VVLLEIITGLPPV 218
PK_VRK3 cd14124
Pseudokinase domain of Vaccinia Related Kinase 3; The pseudokinase domain shows similarity to ...
111-218 1.87e-05

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


Pssm-ID: 271026 [Multi-domain]  Cd Length: 298  Bit Score: 46.76  E-value: 1.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 111 GGNMANAIKKARGKLfPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQ--LGNYGLAKLINPE-KPVSM 187
Cdd:cd14124  105 GQSLQSALDEGKGVL-SEKAVLQLACRLLDALEFIHENEYVHGDITAENIFVDPEDQSEvyLAGYGFAFRYCPGgKHVEY 183
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 334185276 188 VSGiSNSMCPEVLE----DQPYG----YKSDIWSLGCCM 218
Cdd:cd14124  184 REG-SRSPHEGDIEfislDSHKGagpsRRSDLQSLGYCM 221
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
137-273 1.93e-05

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: 47.33  E-value: 1.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 137 QLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAK-LINPEKPVSMVSGI--SNSMCPEVLEDQPYGYKSDIWS 213
Cdd:cd05105  245 QVARGMEFLASKNCVHRDLAARNVLLAQGKIVKICDFGLARdIMHDSNYVSKGSTFlpVKWMAPESIFDNLYTTLSDVWS 324
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334185276 214 LGCCMYEITAhQPAFKAPDM---AGLINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPT 273
Cdd:cd05105  325 YGILLWEIFS-LGGTPYPGMivdSTFYNKIKSGYRMAKPDHATQEVYDIMVKCWNSEPEKRPS 386
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
132-221 1.95e-05

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: 46.88  E-value: 1.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 132 FKWlaQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKpvsmvSGISNS--------MCPEVLEDQ 203
Cdd:cd05045  132 FAW--QISRGMQYLAEMKLVHRDLAARNVLVAEGRKMKISDFGLSRDVYEED-----SYVKRSkgripvkwMAIESLFDH 204
                         90
                 ....*....|....*...
gi 334185276 204 PYGYKSDIWSLGCCMYEI 221
Cdd:cd05045  205 IYTTQSDVWSFGVLLWEI 222
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
98-274 2.55e-05

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: 46.23  E-value: 2.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  98 NDNNACIFTAYYEGGNMANAIkkaRGKLFPEERIFK--WLAQLLLAVNYLHSNR-VVHMDLTCSNIFLpkDDH--VQLGN 172
Cdd:cd13992   67 NPPNIAVVTEYCTRGSLQDVL---LNREIKMDWMFKssFIKDIVKGMNYLHSSSiGYHGRLKSSNCLV--DSRwvVKLTD 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 173 YGLAKLINPEKPVSMVSGISNS----MCPEVLEDQPYGY----KSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSL 244
Cdd:cd13992  142 FGLRNLLEEQTNHQLDEDAQHKkllwTAPELLRGSLLEVrgtqKGDVYSFAIILYEILFRSDPFALEREVAIVEKVISGG 221
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 334185276 245 MSP-LPIVYSSTLKQ--MIKLMLR----KKPEYRPTA 274
Cdd:cd13992  222 NKPfRPELAVLLDEFppRLVLLVKqcwaENPEKRPSF 258
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
85-281 2.69e-05

Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. 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. A mutation which results in a truncation of a C-terminal part of the human STRAD-alpha pseudokinase domain and disrupts its association with LKB1, leads to PMSE (polyhydramnios, megalencephaly, symptomatic epilepsy) syndrome. Several splice variants of STRAD-alpha exist which exhibit different effects on the localization and activation of LKB1. 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. The STRAD alpha 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: 173767 [Multi-domain]  Cd Length: 327  Bit Score: 46.47  E-value: 2.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  85 NPYIVHYEDSWIdNDNNACIFTAYYEGGNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPK 164
Cdd:cd08227   58 HPNIVPYRATFI-ADNELWVVTSFMAYGSAKDLICTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISV 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 165 DDHVQL-GNYGLAKLINPEKPVSMVSGISNS-------MCPEVLEDQPYGY--KSDIWSLGCCMYEI-TAHQPAFKAPDM 233
Cdd:cd08227  137 DGKVYLsGLRSNLSMINHGQRLRVVHDFPKYsvkvlpwLSPEVLQQNLQGYdaKSDIYSVGITACELaNGHVPFKDMPAT 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 234 AGLINKIN--------------------------------------------RSLMSPLPIVYSSTLKQMIKLMLRKKPE 269
Cdd:cd08227  217 QMLLEKLNgtvpclldtttipaeeltmkpsrsgansglgesttvstprpsngESSSHPYNRTFSPHFHHFVEQCLQRNPD 296
                        250
                 ....*....|..
gi 334185276 270 YRPTACELLRNP 281
Cdd:cd08227  297 ARPSASTLLNHS 308
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
16-228 3.62e-05

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR2 (also called STK38-like) plays a role in proper centrosome duplication. In addition, it is involved in regulating neuronal growth and differentiation, as well as in facilitating neurite outgrowth. NDR2 is also implicated in fear conditioning as it contributes to the coupling of neuronal morphological changes with fear-memory consolidation. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 46.20  E-value: 3.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  16 LDNYHVVEQVRRGKSSSDFVVLHDIEDKKYAMKkicLAKHTDKLKQTALQEIsRAVINydlmkLLSSLKNPYIVHYEDSW 95
Cdd:cd05627    1 LDDFESLKVIGRGAFGEVRLVQKKDTGHIYAMK---ILRKADMLEKEQVAHI-RAERD-----ILVEADGAWVVKMFYSF 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  96 IDNdNNACIFTAYYEGGNMANAIKKaRGKLFPEERIFkWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGL 175
Cdd:cd05627   72 QDK-RNLYLIMEFLPGGDMMTLLMK-KDTLSEEATQF-YIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 176 AKLI--------------NPEKPVSMVS----------------------GISNSMCPEVLEDQPYGYKSDIWSLGCCMY 219
Cdd:cd05627  149 CTGLkkahrtefyrnlthNPPSDFSFQNmnskrkaetwkknrrqlaystvGTPDYIAPEVFMQTGYNKLCDWWSLGVIMY 228

                 ....*....
gi 334185276 220 EITAHQPAF 228
Cdd:cd05627  229 EMLIGYPPF 237
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
126-271 3.64e-05

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: 46.16  E-value: 3.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 126 FPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDH-------------------VQLGNYGLAKLiNPEKPVS 186
Cdd:cd14215  113 YPIHQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFVNSDYeltynlekkrdersvkstaIRVVDFGSATF-DHEHHST 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 187 MVSgISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRsLMSPLPivysstlKQMIKLMLRK 266
Cdd:cd14215  192 IVS-TRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNREHLAMMER-ILGPIP-------SRMIRKTRKQ 262

                 ....*
gi 334185276 267 KPEYR 271
Cdd:cd14215  263 KYFYH 267
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
130-240 4.08e-05

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: 45.77  E-value: 4.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 130 RIFKWLAQLLLAVNYLHSN--RVVHMDLTCSNIFL--PKDDHVQLGNYGLAKLINPEKPVSMVSGISNSmcPEVLEDQPY 205
Cdd:cd14226  117 LTRKFAQQLCTALLFLSTPelSIIHCDLKPENILLcnPKRSAIKIIDFGSSCQLGQRIYQYIQSRFYRS--PEVLLGLPY 194
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 334185276 206 GYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKI 240
Cdd:cd14226  195 DLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKI 229
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
111-228 4.50e-05

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


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 45.40  E-value: 4.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 111 GGNMANAIKKARGklFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDH---VQLGNYGLA---KLINPEKP 184
Cdd:cd14173   84 GGSILSHIHRRRH--FNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQvspVKICDFDLGsgiKLNSDCSP 161
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 334185276 185 VSMVS-----GISNSMCPEVL-----EDQPYGYKSDIWSLGCCMYEITAHQPAF 228
Cdd:cd14173  162 ISTPElltpcGSAEYMAPEVVeafneEASIYDKRCDLWSLGVILYIMLSGYPPF 215
pknD PRK13184
serine/threonine-protein kinase PknD;
142-221 5.14e-05

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 46.30  E-value: 5.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 142 VNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEK----------PVSMVS---------GISNSMCPEVLED 202
Cdd:PRK13184 126 IEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGAAIFKKLEEedlldidvdeRNICYSsmtipgkivGTPDYMAPERLLG 205
                         90
                 ....*....|....*....
gi 334185276 203 QPYGYKSDIWSLGCCMYEI 221
Cdd:PRK13184 206 VPASESTDIYALGVILYQM 224
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
45-223 5.53e-05

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: 45.47  E-value: 5.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  45 YAMKKI---ClAKHTDKLKQTALQEisRAVInydlmklLSSLKNPYIVHYEDSWIDNDNNACIFTAYYEG--GNMANAIK 119
Cdd:cd14001   31 WAVKKInskC-DKGQRSLYQERLKE--EAKI-------LKSLNHPNIVGFRAFTKSEDGSLCLAMEYGGKslNDLIEERY 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 120 KARGKLFPEERIFKWLAQLLLAVNYLHSN-RVVHMDLTCSNIFLPKD-DHVQLGNYGLA-----KLINPEKPVSMVSGIS 192
Cdd:cd14001  101 EAGLGPFPAATILKVALSIARALEYLHNEkKILHGDIKSGNVLIKGDfESVKLCDFGVSlplteNLEVDSDPKAQYVGTE 180
                        170       180       190
                 ....*....|....*....|....*....|..
gi 334185276 193 NSMCPEVL-EDQPYGYKSDIWSLGCCMYEITA 223
Cdd:cd14001  181 PWKAKEALeEGGVITDKADIFAYGLVLWEMMT 212
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
137-228 6.53e-05

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror kinases are expressed in many tissues during development. Avian Ror1 was found to be involved in late limb development. Studies in mice reveal that Ror1 is important in the regulation of neurite growth in central neurons, as well as in respiratory development. Loss of Ror1 also enhances the heart and skeletal abnormalities found in Ror2-deficient mice. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 45.00  E-value: 6.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 137 QLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPE-----KPVSMVSgiSNSMCPEVLEDQPYGYKSDI 211
Cdd:cd05090  132 QIAAGMEYLSSHFFVHKDLAARNILVGEQLHVKISDLGLSREIYSSdyyrvQNKSLLP--IRWMPPEAIMYGKFSSDSDI 209
                         90
                 ....*....|....*....
gi 334185276 212 WSLGCCMYEITAH--QPAF 228
Cdd:cd05090  210 WSFGVVLWEIFSFglQPYY 228
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
78-220 6.65e-05

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


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 44.94  E-value: 6.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  78 KLLSSLKNPYIVHYEDSWidnDNNACIFTAYYEGGNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTC 157
Cdd:cd05115   56 QIMHQLDNPYIVRMIGVC---EAEALMLVMEMASGGPLNKFLSGKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAA 132
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334185276 158 SNIFLPKDDHVQLGNYGLAKLINPE----KPVSMVSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYE 220
Cdd:cd05115  133 RNVLLVNQHYAKISDFGLSKALGADdsyyKARSAGKWPLKWYAPECINFRKFSSRSDVWSYGVTMWE 199
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
104-301 7.61e-05

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


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 44.72  E-value: 7.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 104 IFTAYYEGGNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEK 183
Cdd:cd05052   79 IITEFMPYGNLLDYLRECNREELNAVVLLYMATQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDT 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 184 ---------PVSMVSgisnsmcPEVLEDQPYGYKSDIWSLGCCMYEITAHQpafkapdmaglinkinrslMSPLPIVYSS 254
Cdd:cd05052  159 ytahagakfPIKWTA-------PESLAYNKFSIKSDVWAFGVLLWEIATYG-------------------MSPYPGIDLS 212
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 334185276 255 TLKQMIKLMLRKKpeyRPTACEllrnPSLQPYLLQCQNLSPIYLPVF 301
Cdd:cd05052  213 QVYELLEKGYRME---RPEGCP----PKVYELMRACWQWNPSDRPSF 252
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
45-229 8.92e-05

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: 44.82  E-value: 8.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  45 YAMKKICLAKHTD--KLKQTALQEISRavinydlmklLSSLKNPYIVHYEDSWIDNDNnACIFTAYYEGGNMANaikkar 122
Cdd:cd14159   19 YAVKRLKEDSELDwsVVKNSFLTEVEK----------LSRFRHPNIVDLAGYSAQQGN-YCLIYVYLPNGSLED------ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 123 gKLFPEERIFK--WLAQLLL------AVNYLHSNR--VVHMDLTCSNIFLpkDDHV--QLGNYGLAKLINPEKPVSMVSG 190
Cdd:cd14159   82 -RLHCQVSCPClsWSQRLHVllgtarAIQYLHSDSpsLIHGDVKSSNILL--DAALnpKLGDFGLARFSRRPKQPGMSST 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 334185276 191 ISNS---------MCPEVLEDQPYGYKSDIWSLGCCMYEITAHQPAFK 229
Cdd:cd14159  159 LARTqtvrgtlayLPEEYVKTGTLSVEIDVYSFGVVLLELLTGRRAME 206
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
104-221 9.44e-05

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: 44.69  E-value: 9.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 104 IFTAYYEGGNMANAIKKARGKLFPEERIF-KWLAQLLLAV----NYLHSNRVVHMDLTCSNIFLPK---DDHVQLGNYGL 175
Cdd:cd05036   86 ILLELMAGGDLKSFLRENRPRPEQPSSLTmLDLLQLAQDVakgcRYLEENHFIHRDIAARNCLLTCkgpGRVAKIGDFGM 165
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 334185276 176 AKLINPEK----------PVSMvsgisnsMCPEVLEDQPYGYKSDIWSLGCCMYEI 221
Cdd:cd05036  166 ARDIYRADyyrkggkamlPVKW-------MPPEAFLDGIFTSKTDVWSFGVLLWEI 214
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
49-272 1.11e-04

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: 43.97  E-value: 1.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  49 KICLAKHTDKLKQTALQEiSRAVINYD---LMKLL--SSLKNP-YIVhyedswidndnnacifTAYYEGGNMANAIKKAR 122
Cdd:cd05041   26 KTCRETLPPDLKRKFLQE-ARILKQYDhpnIVKLIgvCVQKQPiMIV----------------MELVPGGSLLTFLRKKG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 123 GKLFPEErifkwLAQLLL----AVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKliNPEKPVSMVSGISNSM--- 195
Cdd:cd05041   89 ARLTVKQ-----LLQMCLdaaaGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSR--EEEDGEYTVSDGLKQIpik 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 196 --CPEVLEDQPYGYKSDIWSLGCCMYEITahqpAFKAPDMAGLINKINRSLMS-----PLPivySSTLKQMIKLMLR--- 265
Cdd:cd05041  162 wtAPEALNYGRYTSESDVWSFGILLWEIF----SLGATPYPGMSNQQTREQIEsgyrmPAP---ELCPEAVYRLMLQcwa 234

                 ....*..
gi 334185276 266 KKPEYRP 272
Cdd:cd05041  235 YDPENRP 241
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
132-276 1.13e-04

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: 44.19  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 132 FKWLAQLLLAVNYLHSNRVVHMDLTCSNIF---LPKDDHV--QLGNYGLAKLINPEKPVSmVSGISNSMCPEVLEDQPYG 206
Cdd:cd14067  117 FKIAYQIAAGLAYLHKKNIIFCDLKSDNILvwsLDVQEHIniKLSDYGISRQSFHEGALG-VEGTPGYQAPEIRPRIVYD 195
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334185276 207 YKSDIWSLGCCMYE-ITAHQPAFKAPDMAgLINKINRSLMSPLPIVYSSTLKQMIKLMLR---KKPEYRPTACE 276
Cdd:cd14067  196 EKVDMFSYGMVLYElLSGQRPSLGHHQLQ-IAKKLSKGIRPVLGQPEEVQFFRLQALMMEcwdTKPEKRPLACS 268
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
127-221 1.18e-04

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: 44.14  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 127 PEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLI----------NPEKPVSMVSgisnsmc 196
Cdd:cd05074  121 PLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCMLNENMTVCVADFGLSKKIysgdyyrqgcASKLPVKWLA------- 193
                         90       100
                 ....*....|....*....|....*
gi 334185276 197 PEVLEDQPYGYKSDIWSLGCCMYEI 221
Cdd:cd05074  194 LESLADNVYTTHSDVWAFGVTMWEI 218
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
101-228 1.46e-04

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: 44.26  E-value: 1.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 101 NACIFTAYYEGGNMANAIKKaRGKLFPEERIFkWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLA---- 176
Cdd:cd05628   75 NLYLIMEFLPGGDMMTLLMK-KDTLTEEETQF-YIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCtglk 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 177 --------KLINPEKPVSM------------------------VSGISNSMCPEVLEDQPYGYKSDIWSLGCCMYEITAH 224
Cdd:cd05628  153 kahrtefyRNLNHSLPSDFtfqnmnskrkaetwkrnrrqlafsTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIG 232

                 ....
gi 334185276 225 QPAF 228
Cdd:cd05628  233 YPPF 236
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
115-278 1.62e-04

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: 43.88  E-value: 1.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 115 ANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNS 194
Cdd:cd05047   98 AFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRGQEVYVKKTMGRLPVRW 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 195 MCPEVLEDQPYGYKSDIWSLGCCMYEITA-HQPAFKAPDMAGLINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPT 273
Cdd:cd05047  178 MAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPS 257

                 ....*
gi 334185276 274 ACELL 278
Cdd:cd05047  258 FAQIL 262
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
137-221 1.75e-04

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: 43.75  E-value: 1.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 137 QLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHV-QLGNYGLAKLINPEKPVS-MVSGISNSmcPEVLEDQPYGYKSDIWSL 214
Cdd:cd14135  113 QLFLALKHLKKCNILHADIKPDNILVNEKKNTlKLCDFGSASDIGENEITPyLVSRFYRA--PEIILGLPYDYPIDMWSV 190

                 ....*..
gi 334185276 215 GCCMYEI 221
Cdd:cd14135  191 GCTLYEL 197
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
136-228 2.21e-04

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


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 43.52  E-value: 2.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 136 AQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMvsgISNS------MCPEVLEDQPYGYKS 209
Cdd:cd05048  131 IQIAAGMEYLSSHHYVHRDLAARNCLVGDGLTVKISDFGLSRDIYSSDYYRV---QSKSllpvrwMPPEAILYGKFTTES 207
                         90       100
                 ....*....|....*....|.
gi 334185276 210 DIWSLGCCMYEITAH--QPAF 228
Cdd:cd05048  208 DVWSFGVVLWEIFSYglQPYY 228
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
137-278 2.60e-04

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR beta is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR beta forms homodimers or heterodimers with PDGFR alpha, depending on the nature of the PDGF ligand. PDGF-BB and PDGF-DD induce PDGFR beta homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR beta signaling leads to a variety of cellular effects including the stimulation of cell growth and chemotaxis, as well as the inhibition of apoptosis and GAP junctional communication. It is critical in normal angiogenesis as it is involved in the recruitment of pericytes and smooth muscle cells essential for vessel stability. Aberrant PDGFR beta expression is associated with some human cancers. The continuously-active fusion proteins of PDGFR beta with COL1A1 and TEL are associated with dermatofibrosarcoma protuberans (DFSP) and a subset of chronic myelomonocytic leukemia (CMML), respectively. The PDGFR beta subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133238 [Multi-domain]  Cd Length: 401  Bit Score: 43.46  E-value: 2.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 137 QLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKpvSMVSGISNS-----MCPEVLEDQPYGYKSDI 211
Cdd:cd05107  247 QVANGMEFLASKNCVHRDLAARNVLICEGKLVKICDFGLARDIMRDS--NYISKGSTFlplkwMAPESIFNNLYTTLSDV 324
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185276 212 WSLGCCMYEI--TAHQPAFKAPDMAGLINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELL 278
Cdd:cd05107  325 WSFGILLWEIftLGGTPYPELPMNEQFYNAIKRGYRMAKPAHASDEIYEIMQKCWEEKFEIRPDFSQLV 393
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
119-226 2.92e-04

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: 43.08  E-value: 2.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 119 KKARGKLFPEErIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMvsgISNS---- 194
Cdd:cd05091  116 KTVKSTLEPAD-FLHIVTQIAAGMEYLSSHHVVHKDLATRNVLVFDKLNVKISDLGLFREVYAADYYKL---MGNSllpi 191
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 334185276 195 --MCPEVLEDQPYGYKSDIWSLGCCMYEITAH--QP 226
Cdd:cd05091  192 rwMSPEAIMYGKFSIDSDIWSYGVVLWEVFSYglQP 227
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
122-281 3.67e-04

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: 42.65  E-value: 3.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 122 RGKLfPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLP-KDDHVQLGNYGLAKLINpEKPVSMVSGISNSMCPEVL 200
Cdd:cd14100  100 RGAL-PEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDlNTGELKLIDFGSGALLK-DTVYTDFDGTRVYSPPEWI 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 201 EDQPY-GYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPlpivyssTLKQMIKLMLRKKPEYRPTACELLR 279
Cdd:cd14100  178 RFHRYhGRSAAVWSLGILLYDMVCGDIPFEHDEEIIRGQVFFRQRVSS-------ECQHLIKWCLALRPSDRPSFEDIQN 250

                 ..
gi 334185276 280 NP 281
Cdd:cd14100  251 HP 252
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
136-279 5.37e-04

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: 42.13  E-value: 5.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 136 AQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLI----------NPEKPVSMvsgisnsMCPEVLEDQPY 205
Cdd:cd05050  137 KQVAAGMAYLSERKFVHRDLATRNCLVGENMVVKIADFGLSRNIysadyykaseNDAIPIRW-------MPPESIFYNRY 209
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334185276 206 GYKSDIWSLGCCMYEITAH--QPAFkapDMAG--LINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLR 279
Cdd:cd05050  210 TTESDVWAYGVVLWEIFSYgmQPYY---GMAHeeVIYYVRDGNVLSCPDNCPLELYNLMRLCWSKLPSDRPSFASINR 284
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
95-220 6.33e-04

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: 42.30  E-value: 6.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  95 WIDNDNNACIftaYYE--GGNMANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLP--------- 163
Cdd:cd14214   84 WFNFHGHMCI---AFEllGKNTFEFLKENNFQPYPLPHIRHMAYQLCHALKFLHENQLTHTDLKPENILFVnsefdtlyn 160
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334185276 164 ----------KDDHVQLGNYGLAKLiNPEKPVSMVSgISNSMCPEVLEDQPYGYKSDIWSLGCCMYE 220
Cdd:cd14214  161 esksceeksvKNTSIRVADFGSATF-DHEHHTTIVA-TRHYRPPEVILELGWAQPCDVWSLGCILFE 225
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
137-278 6.52e-04

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: 41.92  E-value: 6.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 137 QLLLAVNYLHSNRVVHMDLTCSNIFLpKDDHVQLGNYGLAKLI------NPEKPVSMVSG--------ISNSMCPEVLED 202
Cdd:cd14153  105 EIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGLFTISgvlqagRREDKLRIQSGwlchlapeIIRQLSPETEED 183
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334185276 203 Q-PYGYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPLP-IVYSSTLKQMIKLMLRKKPEYRPTACELL 278
Cdd:cd14153  184 KlPFSKHSDVFAFGTIWYELHAREWPFKTQPAEAIIWQVGSGMKPNLSqIGMGKEISDILLFCWAYEQEERPTFSKLM 261
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
137-221 6.57e-04

Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. Kit signaling is involved in major cellular functions including cell survival, proliferation, differentiation, adhesion, and chemotaxis. Mutations in Kit, which result in constitutive ligand-independent activation, are found in human cancers such as gastrointestinal stromal tumor (GIST) and testicular germ cell tumor (TGCT). The aberrant expression of Kit and/or SCF is associated with other tumor types such as systemic mastocytosis and cancers of the breast, neurons, lung, prostate, colon, and rectum. Although the structure of the human Kit catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. Kit is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of Kit to its ligand, the stem-cell factor (SCF), leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. The Kit subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270682 [Multi-domain]  Cd Length: 375  Bit Score: 42.20  E-value: 6.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 137 QLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVsMVSGISNS----MCPEVLEDQPYGYKSDIW 212
Cdd:cd05104  222 QVAKGMEFLASKNCIHRDLAARNILLTHGRITKICDFGLARDIRNDSNY-VVKGNARLpvkwMAPESIFECVYTFESDVW 300

                 ....*....
gi 334185276 213 SLGCCMYEI 221
Cdd:cd05104  301 SYGILLWEI 309
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
104-231 8.43e-04

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


Pssm-ID: 271042 [Multi-domain]  Cd Length: 291  Bit Score: 41.55  E-value: 8.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 104 IFTAYYEGGNMANAIKkarGKLFPEERIFKWLAQLLLAVNYLHSN-----------RVVHMDLTCSNIFLPKDDHVQLGN 172
Cdd:cd14140   70 LITAFHDKGSLTDYLK---GNIVSWNELCHIAETMARGLSYLHEDvprckgeghkpAIAHRDFKSKNVLLKNDLTAVLAD 146
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334185276 173 YGLAKLINPEKPVSMVSGISNS---MCPEVLE-----DQPYGYKSDIWSLGCCMYEITAHQPAFKAP 231
Cdd:cd14140  147 FGLAVRFEPGKPPGDTHGQVGTrryMAPEVLEgainfQRDSFLRIDMYAMGLVLWELVSRCKAADGP 213
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
78-229 1.09e-03

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: 41.18  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  78 KLLSSLKNPYIVHYEDSWIDNDNNACIFTaYYEGGNM--------ANAIKKARGKLFPE---ERIFKWLAQLLLAVNYLH 146
Cdd:cd05093   59 ELLTNLQHEHIVKFYGVCVEGDPLIMVFE-YMKHGDLnkflrahgPDAVLMAEGNRPAEltqSQMLHIAQQIAAGMVYLA 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 147 SNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINpEKPVSMVSGIS----NSMCPEVLEDQPYGYKSDIWSLGCCMYEIT 222
Cdd:cd05093  138 SQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVY-STDYYRVGGHTmlpiRWMPPESIMYRKFTTESDVWSLGVVLWEIF 216

                 ....*....
gi 334185276 223 AH--QPAFK 229
Cdd:cd05093  217 TYgkQPWYQ 225
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
115-278 1.14e-03

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: 41.14  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 115 ANAIKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKPVSMVSGISNS 194
Cdd:cd05088  110 AFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRGQEVYVKKTMGRLPVRW 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 195 MCPEVLEDQPYGYKSDIWSLGCCMYEITA-HQPAFKAPDMAGLINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEYRPT 273
Cdd:cd05088  190 MAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPS 269

                 ....*
gi 334185276 274 ACELL 278
Cdd:cd05088  270 FAQIL 274
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
28-220 1.39e-03

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: 40.76  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  28 GKSSSDFVVLHDIEDKKYAMKKICLAKHTDKLKQTALQEiSRAVINYD---LMKLLS--SLKNP-YIVhyedswidndnn 101
Cdd:cd05085    5 GKGNFGEVYKGTLKDKTPVAVKTCKEDLPQELKIKFLSE-ARILKQYDhpnIVKLIGvcTQRQPiYIV------------ 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 102 acifTAYYEGGNMANAIKKARGKLfPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKliNP 181
Cdd:cd05085   72 ----MELVPGGDFLSFLRKKKDEL-KTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSR--QE 144
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 334185276 182 EKPVSMVSGISNS----MCPEVLEDQPYGYKSDIWSLGCCMYE 220
Cdd:cd05085  145 DDGVYSSSGLKQIpikwTAPEALNYGRYSSESDVWSFGILLWE 187
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
134-223 1.78e-03

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


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 40.55  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 134 WLAQLLLAVN------YLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAklinpeKPVSMVSG-ISNS---MCPEVLeDQ 203
Cdd:cd13975  101 LEERLQIALDvvegirFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFC------KPEAMMSGsIVGTpihMAPELF-SG 173
                         90       100
                 ....*....|....*....|
gi 334185276 204 PYGYKSDIWSLGCCMYEITA 223
Cdd:cd13975  174 KYDNSVDVYAFGILFWYLCA 193
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
106-222 1.83e-03

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: 40.50  E-value: 1.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 106 TAYYEGGNMANAIKKargklfpeeRIFKWLAQLLLA------VNYLHSNRV---------VHMDLTCSNIFLPKDDHVQL 170
Cdd:cd13998   72 TAFHPNGSL*DYLSL---------HTIDWVSLCRLAlsvargLAHLHSEIPgctqgkpaiAHRDLKSKNILVKNDGTCCI 142
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334185276 171 GNYGLAKLINP---EKPVSMVS--GISNSMCPEVLE-----DQPYGYKS-DIWSLGCCMYEIT 222
Cdd:cd13998  143 ADFGLAVRLSPstgEEDNANNGqvGTKRYMAPEVLEgainlRDFESFKRvDIYAMGLVLWEMA 205
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
122-281 2.05e-03

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: 40.32  E-value: 2.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 122 RGKLfPEERIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLP-KDDHVQLGNYGLAKLINpEKPVSMVSGISNSMCPEVL 200
Cdd:cd14102   99 KGAL-DEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDlRTGELKLIDFGSGALLK-DTVYTDFDGTRVYSPPEWI 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 201 EDQPY-GYKSDIWSLGCCMYEITAHQPAFKAPDMAGLINKINRSLMSPlpivyssTLKQMIKLMLRKKPEYRPTACELLR 279
Cdd:cd14102  177 RYHRYhGRSATVWSLGVLLYDMVCGDIPFEQDEEILRGRLYFRRRVSP-------ECQQLIKWCLSLRPSDRPTLEQIFD 249

                 ..
gi 334185276 280 NP 281
Cdd:cd14102  250 HP 251
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
96-272 2.44e-03

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphA10, which contains an inactive tyr kinase domain, may function to attenuate signals of co-clustered active receptors. EphA10 is mainly expressed in the testis. Ephrin/EphR interaction 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. EphRs comprise the largest subfamily of receptor tyr kinases (RTKs). In general, 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). The EphA10 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: 133195 [Multi-domain]  Cd Length: 266  Bit Score: 39.91  E-value: 2.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  96 IDNDNNACIFTAYYEGGNMANAIKKARGKLFPEErIFKWLAQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGL 175
Cdd:cd05064   75 ITRGNTMMIVTEYMSNGALDSFLRKHEGQLVAGQ-LMGMLPGLASGMKYLSEMGYVHKGLAAHKVLVNSDLVCKISGFRR 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 176 AKLINPEKPVSMVSGISNSM--CPEVLEDQPYGYKSDIWSLGCCMYEITAH--QPAFkapDMAG--LINKINRSLMSPLP 249
Cdd:cd05064  154 LQEDKSEAIYTTMSGKSPVLwaAPEAIQYHHFSSASDVWSFGIVMWEVMSYgeRPYW---DMSGqdVIKAVEDGFRLPAP 230
                        170       180
                 ....*....|....*....|...
gi 334185276 250 IVYSSTLKQMIKLMLRKKPEYRP 272
Cdd:cd05064  231 RNCPNLLHQLMLDCWQKERGERP 253
PTK_Jak2_rpt1 cd05078
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely ...
137-238 2.62e-03

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely expressed in many tissues. It 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 cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Despite this, the presumed pseudokinase (repeat 1) domain of Jak2 exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Inactivation of the repeat 1 domain increased Jak2 basal activity, suggesting that it modulates the kinase activity of the C-terminal catalytic (repeat 2) domain. The Jak2 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: 270663 [Multi-domain]  Cd Length: 262  Bit Score: 39.93  E-value: 2.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 137 QLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPekpvsmvsGISNSMCPE--VLEDQPY--------- 205
Cdd:cd05078  112 QLAWAMHFLEEKTLVHGNVCAKNILLIREEDRKTGNPPFIKLSDP--------GISITVLPKdiLLERIPWvppecienp 183
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 334185276 206 ---GYKSDIWSLGCCMYEITA---------------------HQ-PAFKAPDMAGLIN 238
Cdd:cd05078  184 knlSLATDKWSFGTTLWEICSggdkplsaldsqrklqfyedrHQlPAPKWTELANLIN 241
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
137-301 2.96e-03

Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. CSF-1R, also called c-Fms, is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of CSF-1R to its ligand, CSF-1, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. It leads to increases in gene transcription and protein translation, and induces cytoskeletal remodeling. CSF-1R signaling leads to a variety of cellular responses including survival, proliferation, and differentiation of target cells. It plays an important role in innate immunity, tissue development and function, and the pathogenesis of some diseases including atherosclerosis and cancer. CSF-1R signaling is also implicated in mammary gland development during pregnancy and lactation. Aberrant CSF-1/CSF-1R expression correlates with tumor cell invasiveness, poor clinical prognosis, and bone metastasis in breast cancer. Although the structure of the human CSF-1R catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. The CSF-1R subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133237 [Multi-domain]  Cd Length: 374  Bit Score: 40.21  E-value: 2.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 137 QLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLI----------NPEKPVSMvsgisnsMCPEVLEDQPYG 206
Cdd:cd05106  220 QVAQGMDFLASKNCIHRDVAARNVLLTDGRVAKICDFGLARDImndsnyvvkgNARLPVKW-------MAPESIFDCVYT 292
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 207 YKSDIWSLGCCMYEITahqpafkapdmaglinkinrSL-MSPLP-IVYSSTLKQMIKLMLR-KKPEYRPtacellrnPSL 283
Cdd:cd05106  293 VQSDVWSYGILLWEIF--------------------SLgKSPYPgILVNSKFYKMVKRGYQmSRPDFAP--------PEI 344
                        170
                 ....*....|....*...
gi 334185276 284 QPYLLQCQNLSPIYLPVF 301
Cdd:cd05106  345 YSIMKMCWNLEPTERPTF 362
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
118-283 3.22e-03

kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to the C-terminal protein kinase catalytic fold (C lobe). Its presence at the N terminus of signalling proteins and the absence of the active-site residues in the catalytic and activation loops suggest that it folds independently and is likely to be non-catalytic. The occurrence of KIND only in metazoa implies that it has evolved from the catalytic protein kinase domain into an interaction domain possibly by keeping the substrate-binding features


Pssm-ID: 214801  Cd Length: 176  Bit Score: 38.92  E-value: 3.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276   118 IKKARGKLFPEERIFKWLAQLLLAVNYLHSNRVVHmdltcsNIFLPKDDHVQLgnYGLAKLINPE--KPVSMVsgisnsM 195
Cdd:smart00750   6 ILEVRGRPLNEEEIWAVCLQCLGALRELHRQAKSG------NILLTWDGLLKL--DGSVAFKTPEqsRPDPYF------M 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276   196 CPEVLEDQPYGYKSDIWSLGCCMYEITahqpAFKAPDMagLINKINRSLMSPL-----------PIVYS----STLKQMI 260
Cdd:smart00750  72 APEVIQGQSYTEKADIYSLGITLYEAL----DYELPYN--EERELSAILEILLngmpaddprdrSNLEGvsaaRSFEDFM 145
                          170       180
                   ....*....|....*....|...
gi 334185276   261 KLMLRKKPEYRPTACELLRNPSL 283
Cdd:smart00750 146 RLCASRLPQRREAANHYLAHCRA 168
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
136-229 3.38e-03

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: 39.56  E-value: 3.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 136 AQLLLAVNYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINpEKPVSMVSGIS----NSMCPEVLEDQPYGYKSDI 211
Cdd:cd05092  129 SQIASGMVYLASLHFVHRDLATRNCLVGQGLVVKIGDFGMSRDIY-STDYYRVGGRTmlpiRWMPPESILYRKFTTESDI 207
                         90       100
                 ....*....|....*....|
gi 334185276 212 WSLGCCMYEITAH--QPAFK 229
Cdd:cd05092  208 WSFGVVLWEIFTYgkQPWYQ 227
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
78-229 3.51e-03

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


Pssm-ID: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 39.61  E-value: 3.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276  78 KLLSSLKNPYIVHYEDSWIDNDNNACIFTaYYEGGNMANAIK---------------KARGKLfPEERIFKWLAQLLLAV 142
Cdd:cd05094   59 ELLTNLQHDHIVKFYGVCGDGDPLIMVFE-YMKHGDLNKFLRahgpdamilvdgqprQAKGEL-GLSQMLHIATQIASGM 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 143 NYLHSNRVVHMDLTCSNIFLPKDDHVQLGNYGLAKLINPEKpVSMVSGIS----NSMCPEVLEDQPYGYKSDIWSLGCCM 218
Cdd:cd05094  137 VYLASQHFVHRDLATRNCLVGANLLVKIGDFGMSRDVYSTD-YYRVGGHTmlpiRWMPPESIMYRKFTTESDVWSFGVIL 215
                        170
                 ....*....|...
gi 334185276 219 YEITAH--QPAFK 229
Cdd:cd05094  216 WEIFTYgkQPWFQ 228
PHA02988 PHA02988
hypothetical protein; Provisional
152-283 6.22e-03

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 38.96  E-value: 6.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 152 HMDLTCSNIFLPKDDHVQLGNYGLAKLIN--PEKPVSMVSGISNSMCPEVLEdqPYGYKSDIWSLGCCMYEI-TAHQPaF 228
Cdd:PHA02988 146 YKNLTSVSFLVTENYKLKIICHGLEKILSspPFKNVNFMVYFSYKMLNDIFS--EYTIKDDIYSLGVVLWEIfTGKIP-F 222
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 334185276 229 KAPDMAGLINKI---NRSLmsPLPIVYSSTLKQMIKLMLRKKPEYRPTACELLRNPSL 283
Cdd:PHA02988 223 ENLTTKEIYDLIinkNNSL--KLPLDCPLEIKCIVEACTSHDSIKRPNIKEILYNLSL 278
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
134-281 6.54e-03

Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called U2AF homology motif (UHM) kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KIS (or UHMK1) contains an N-terminal kinase domain and a C-terminal domain with a UHM motif, a protein interaction motif initially found in the pre-mRNA splicing factor U2AF. It phosphorylates the splicing factor SF1, which enhances binding to the splice site to promote spliceosome assembly. KIS was first identified as a kinase that interacts with stathmin, a phosphoprotein that plays a role in axon development and microtubule dynamics. It localizes in RNA granules in neurons and is important in neurite outgrowth. The KIS/UHMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 38.76  E-value: 6.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 134 WLAQ-----LLLAVNYLHSNRVVHMDLTCSNIFLPKDDHV-QLGNYGLA--------KLINPEKPVSMVSGISNSMCPEV 199
Cdd:cd14020  110 WMIQhcardVLEALAFLHHEGYVHADLKPRNILWSAEDECfKLIDFGLSfkegnqdvKYIQTDGYRAPEAELQNCLAQAG 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185276 200 LE-DQPYGYKSDIWSLGCCMYEI--------TAHQPAFKApDMAGLINKINRSLMSPLPIVYSSTLKQMIKLMLRKKPEY 270
Cdd:cd14020  190 LQsETECTSAVDLWSLGIVLLEMfsgmklkhTVRSQEWKD-NSSAIIDHIFASNAVVNPAIPAYHLRDLIKSMLHNDPGK 268
                        170
                 ....*....|.
gi 334185276 271 RPTACELLRNP 281
Cdd:cd14020  269 RATAEAALCSP 279
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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