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Conserved domains on  [gi|15222437|ref|NP_172237|]
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Protein kinase superfamily protein [Arabidopsis thaliana]

Protein Classification

serine/threonine-protein kinase family protein( domain architecture ID 10197261)

serine/threonine-protein kinase family protein may catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates

Gene Ontology:  GO:0004672|GO:0005524|GO:0006468
PubMed:  7768349
SCOP:  4003661

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
74-353 6.25e-93

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: 280.70  E-value: 6.25e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWIDeksltasrpgTGLVIAVKKLNQDGWQ-GHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYE 152
Cdd:cd14066   1 IGSGGFGTVYKGVLE----------NGTVVAVKRLNEMNCAaSKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMPRGSLENHLFRRGLYfQPLSWKLRLKVALGAAKGLAFLHSS-ETRVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPIG 231
Cdd:cd14066  71 YMPNGSLEDRLHCHKGS-PPLPWPQRLKIAKGIARGLEYLHEEcPPPIIHGDIKSSNILLDEDFEPKLTDFGLARLIPPS 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 232 DKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVDKNR-PSGERNLVEWAKPylVNKRKIFRVID 310
Cdd:cd14066 150 ESVSKTSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDENReNASRKDLVEWVES--KGKEELEDILD 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 15222437 311 NRLQDQYSMEEAC--KVATLSLRCLTTEIKLRPNMSEVVSHLEHI 353
Cdd:cd14066 228 KRLVDDDGVEEEEveALLRLALLCTRSDPSLRPSMKEVVQMLEKL 272
 
Name Accession Description Interval E-value
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
74-353 6.25e-93

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: 280.70  E-value: 6.25e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWIDeksltasrpgTGLVIAVKKLNQDGWQ-GHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYE 152
Cdd:cd14066   1 IGSGGFGTVYKGVLE----------NGTVVAVKRLNEMNCAaSKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMPRGSLENHLFRRGLYfQPLSWKLRLKVALGAAKGLAFLHSS-ETRVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPIG 231
Cdd:cd14066  71 YMPNGSLEDRLHCHKGS-PPLPWPQRLKIAKGIARGLEYLHEEcPPPIIHGDIKSSNILLDEDFEPKLTDFGLARLIPPS 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 232 DKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVDKNR-PSGERNLVEWAKPylVNKRKIFRVID 310
Cdd:cd14066 150 ESVSKTSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDENReNASRKDLVEWVES--KGKEELEDILD 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 15222437 311 NRLQDQYSMEEAC--KVATLSLRCLTTEIKLRPNMSEVVSHLEHI 353
Cdd:cd14066 228 KRLVDDDGVEEEEveALLRLALLCTRSDPSLRPSMKEVVQMLEKL 272
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
73-350 6.25e-55

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: 182.31  E-value: 6.25e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437    73 VLGEGGFGCVFKGWideksLTASRPGTGLVIAVKKLNQD-GWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVY 151
Cdd:pfam07714   6 KLGEGAFGEVYKGT-----LKGEGENTKIKVAVKTLKEGaDEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437   152 EFMPRGSLENHLFRRGlyfQPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPIG 231
Cdd:pfam07714  81 EYMPGGDLLDFLRKHK---RKLTLKDLLSMALQIAKGMEYLESK--NFVHRDLAARNCLVSENLVVKISDFGLSRDIYDD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437   232 DKSHVST------RVMgthgyaAPEYLATGHLTTKSDVYSFGVVLLELLSGrravdknrpsGErnlvewaKPY--LVNKR 303
Cdd:pfam07714 156 DYYRKRGggklpiKWM------APESLKDGKFTSKSDVWSFGVLLWEIFTL----------GE-------QPYpgMSNEE 212
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 15222437   304 KIFRVID-NRL-QDQYSMEEackVATLSLRCLTTEIKLRPNMSEVVSHL 350
Cdd:pfam07714 213 VLEFLEDgYRLpQPENCPDE---LYDLMKQCWAYDPEDRPTFSELVEDL 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
71-350 1.09e-52

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 176.57  E-value: 1.09e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437     71 DSVLGEGGFGCVFKGWIDEKSltasrPGTGLVIAVKKLNQD-GWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLL 149
Cdd:smart00219   4 GKKLGEGAFGEVYKGKLKGKG-----GKKKVEVAVKTLKEDaSEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437    150 VYEFMPRGSLENHLFRRGlyfQPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAKDGP 229
Cdd:smart00219  79 VMEYMEGGDLLSYLRKNR---PKLSLSDLLSFALQIARGMEYLESK--NFIHRDLAARNCLVGENLVVKISDFGLSRDLY 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437    230 igdkSHVSTRVMGTHG---YAAPEYLATGHLTTKSDVYSFGVVLLELLSGrravdknrpsGErnlvewaKPY--LVNKRK 304
Cdd:smart00219 154 ----DDDYYRKRGGKLpirWMAPESLKEGKFTSKSDVWSFGVLLWEIFTL----------GE-------QPYpgMSNEEV 212
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 15222437    305 IFRVID-NRLqdqySMEEAC--KVATLSLRCLTTEIKLRPNMSEVVSHL 350
Cdd:smart00219 213 LEYLKNgYRL----PQPPNCppELYDLMLQCWAEDPEDRPTFSELVEIL 257
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
67-359 2.25e-45

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 163.26  E-value: 2.25e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGCVFKGWideksltasRPGTGLVIAVKKLNQDgWQGHQEWLA----EVNYLGQFSHRHLVKLIGYCL 142
Cdd:COG0515   8 RYRILRLLGRGGMGVVYLAR---------DLRLGRPVALKVLRPE-LAADPEARErfrrEARALARLNHPNIVRVYDVGE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 143 EDEHRLLVYEFMPRGSLENHLFRRGlyfqPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDF 222
Cdd:COG0515  78 EDGRPYLVMEYVEGESLADLLRRRG----PLPPAEALRILAQLAEALAAAHAA--GIVHRDIKPANILLTPDGRVKLIDF 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 223 GLAKdgPIGDKSHVST-RVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRravdknRPSGERNLVEWAKPYLVN 301
Cdd:COG0515 152 GIAR--ALGGATLTQTgTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGR------PPFDGDSPAELLRAHLRE 223
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15222437 302 KRKIFRVIDNRLQDQysmeeackVATLSLRCLTTEIKLRP-NMSEVVSHLEHIQSLNAA 359
Cdd:COG0515 224 PPPPPSELRPDLPPA--------LDAIVLRALAKDPEERYqSAAELAAALRAVLRSLAA 274
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
44-351 1.58e-22

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 100.31  E-value: 1.58e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437   44 EGEILQSPNLKSFSFAELKSATRNfrpDSVLGEGGFGCVFKGwideKSLTasrpgTGLVIAVKKLNQDgwqgHQEWLAEV 123
Cdd:PLN00113 671 ELQFFDSKVSKSITINDILSSLKE---ENVISRGKKGASYKG----KSIK-----NGMQFVVKEINDV----NSIPSSEI 734
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  124 NYLGQFSHRHLVKLIGYCLEDEHRLLVYEFMPRGSLENHLfrRGLyfqplSWKLRLKVALGAAKGLAFLHSS-ETRVIYR 202
Cdd:PLN00113 735 ADMGKLQHPNIVKLIGLCRSEKGAYLIHEYIEGKNLSEVL--RNL-----SWERRRKIAIGIAKALRFLHCRcSPAVVVG 807
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  203 DFKTSNILLDSEYNAKLSdfgLAKDGPIGdkshVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVDK 282
Cdd:PLN00113 808 NLSPEKIIIDGKDEPHLR---LSLPGLLC----TDTKCFISSAYVAPETRETKDITEKSDIYGFGLILIELLTGKSPADA 880
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15222437  283 NRpSGERNLVEWAKpYLVNKRKIFRVIDNRLQDQYSM--EEACKVATLSLRCLTTEIKLRPNMSEVVSHLE 351
Cdd:PLN00113 881 EF-GVHGSIVEWAR-YCYSDCHLDMWIDPSIRGDVSVnqNEIVEVMNLALHCTATDPTARPCANDVLKTLE 949
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
172-277 2.08e-12

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 68.67  E-value: 2.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  172 PLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAKdgpigdksHVST-------RVMGTH 244
Cdd:NF033483 103 PLSPEEAVEIMIQILSALEHAHRN--GIVHRDIKPQNILITKDGRVKVTDFGIAR--------ALSSttmtqtnSVLGTV 172
                         90       100       110
                 ....*....|....*....|....*....|...
gi 15222437  245 GYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:NF033483 173 HYLSPEQARGGTVDARSDIYSLGIVLYEMLTGR 205
 
Name Accession Description Interval E-value
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
74-353 6.25e-93

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: 280.70  E-value: 6.25e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWIDeksltasrpgTGLVIAVKKLNQDGWQ-GHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYE 152
Cdd:cd14066   1 IGSGGFGTVYKGVLE----------NGTVVAVKRLNEMNCAaSKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMPRGSLENHLFRRGLYfQPLSWKLRLKVALGAAKGLAFLHSS-ETRVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPIG 231
Cdd:cd14066  71 YMPNGSLEDRLHCHKGS-PPLPWPQRLKIAKGIARGLEYLHEEcPPPIIHGDIKSSNILLDEDFEPKLTDFGLARLIPPS 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 232 DKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVDKNR-PSGERNLVEWAKPylVNKRKIFRVID 310
Cdd:cd14066 150 ESVSKTSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDENReNASRKDLVEWVES--KGKEELEDILD 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 15222437 311 NRLQDQYSMEEAC--KVATLSLRCLTTEIKLRPNMSEVVSHLEHI 353
Cdd:cd14066 228 KRLVDDDGVEEEEveALLRLALLCTRSDPSLRPSMKEVVQMLEKL 272
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
74-353 3.97e-78

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: 242.79  E-value: 3.97e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWIDEksltasrpgtGLVIAVKKLNQDGWQGHQ-EWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYE 152
Cdd:cd14664   1 IGRGGAGTVYKGVMPN----------GTLVAVKRLKGEGTQGGDhGFQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMPRGSLENHLFRRGLYFQPLSWKLRLKVALGAAKGLAFLHSS-ETRVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPIG 231
Cdd:cd14664  71 YMPNGSLGELLHSRPESQPPLDWETRQRIALGSARGLAYLHHDcSPLIIHRDVKSNNILLDEEFEAHVADFGLAKLMDDK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 232 DkSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVDKNRPSGERNLVEWAKPyLVNKRKIFRVIDN 311
Cdd:cd14664 151 D-SHVMSSVAGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRPFDEAFLDDGVDIVDWVRG-LLEEKKVEALVDP 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 15222437 312 RLQDQYSMEEACKVATLSLRCLTTEIKLRPNMSEVVSHLEHI 353
Cdd:cd14664 229 DLQGVYKLEEVEQVFQVALLCTQSSPMERPTMREVVRMLEGD 270
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
74-350 8.04e-65

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: 207.39  E-value: 8.04e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKG-WIdeksltasrpgtGLVIAVKKLNQDGWQGH--QEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLV 150
Cdd:cd13999   1 IGSGSFGEVYKGkWR------------GTDVAIKKLKVEDDNDEllKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIV 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 151 YEFMPRGSLENHLFRRGlyfQPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAKDgpI 230
Cdd:cd13999  69 TEYMPGGSLYDLLHKKK---IPLSWSLRLKIALDIARGMNYLHSP--PIIHRDLKSLNILLDENFTVKIADFGLSRI--K 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 231 GDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRavdknrpsgernlvewakPY--LVNKRKIFRV 308
Cdd:cd13999 142 NSTTEKMTGVVGTPRWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEV------------------PFkeLSPIQIAAAV 203
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 15222437 309 IDNRLQdQYSMEEACK-VATLSLRCLTTEIKLRPNMSEVVSHL 350
Cdd:cd13999 204 VQKGLR-PPIPPDCPPeLSKLIKRCWNEDPEKRPSFSEIVKRL 245
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
58-353 9.06e-64

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: 206.20  E-value: 9.06e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  58 FAELKSATRNF--RPDSV----LGEGGFGCVFKGWIDEKSltasrpgtglvIAVKKLNQDGWQGHQE----WLAEVNYLG 127
Cdd:cd14158   1 FHELKNMTNNFdeRPISVggnkLGEGGFGVVFKGYINDKN-----------VAVKKLAAMVDISTEDltkqFEQEIQVMA 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 128 QFSHRHLVKLIGYCLEDEHRLLVYEFMPRGSLENHLFRRGlYFQPLSWKLRLKVALGAAKGLAFLHssETRVIYRDFKTS 207
Cdd:cd14158  70 KCQHENLVELLGYSCDGPQLCLVYTYMPNGSLLDRLACLN-DTPPLSWHMRCKIAQGTANGINYLH--ENNHIHRDIKSA 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 208 NILLDSEYNAKLSDFGLAKDGPIGDKSHVSTRVMGTHGYAAPEYLaTGHLTTKSDVYSFGVVLLELLSGRRAVDKNRpsg 287
Cdd:cd14158 147 NILLDETFVPKISDFGLARASEKFSQTIMTERIVGTTAYMAPEAL-RGEITPKSDIFSFGVVLLEIITGLPPVDENR--- 222
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15222437 288 ERNLVEWAKPYLVNKRK-IFRVIDNRLQDqYSMEEACKVATLSLRCLTTEIKLRPNMSEVVSHLEHI 353
Cdd:cd14158 223 DPQLLLDIKEEIEDEEKtIEDYVDKKMGD-WDSTSIEAMYSVASQCLNDKKNRRPDIAKVQQLLQEL 288
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
74-353 2.64e-58

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: 192.35  E-value: 2.64e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKgwideksltASRPGTglVIAVKKLNQDGwqgHQEW-------LAEVNYLGQFSHRHLVKLIGYCLEDEH 146
Cdd:cd14159   1 IGEGGFGCVYQ---------AVMRNT--EYAVKRLKEDS---ELDWsvvknsfLTEVEKLSRFRHPNIVDLAGYSAQQGN 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 147 RLLVYEFMPRGSLENHLFRRGlYFQPLSWKLRLKVALGAAKGLAFLHSSETRVIYRDFKTSNILLDSEYNAKLSDFGLAK 226
Cdd:cd14159  67 YCLIYVYLPNGSLEDRLHCQV-SCPCLSWSQRLHVLLGTARAIQYLHSDSPSLIHGDVKSSNILLDAALNPKLGDFGLAR 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 227 -------DGPIGDKSHVSTrVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVD---KNRPSGERNLVE--- 293
Cdd:cd14159 146 fsrrpkqPGMSSTLARTQT-VRGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLTGRRAMEvdsCSPTKYLKDLVKeee 224
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15222437 294 ---------------WAKPYLVNkrkIFRV-IDNRLQdQYSMEEACKVATLSLRCLTTEIKLRPNMSEVVSHLEHI 353
Cdd:cd14159 225 eaqhtpttmthsaeaQAAQLATS---ICQKhLDPQAG-PCPPELGIEISQLACRCLHRRAKKRPPMTEVFQELERL 296
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
73-350 6.25e-55

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: 182.31  E-value: 6.25e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437    73 VLGEGGFGCVFKGWideksLTASRPGTGLVIAVKKLNQD-GWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVY 151
Cdd:pfam07714   6 KLGEGAFGEVYKGT-----LKGEGENTKIKVAVKTLKEGaDEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437   152 EFMPRGSLENHLFRRGlyfQPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPIG 231
Cdd:pfam07714  81 EYMPGGDLLDFLRKHK---RKLTLKDLLSMALQIAKGMEYLESK--NFVHRDLAARNCLVSENLVVKISDFGLSRDIYDD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437   232 DKSHVST------RVMgthgyaAPEYLATGHLTTKSDVYSFGVVLLELLSGrravdknrpsGErnlvewaKPY--LVNKR 303
Cdd:pfam07714 156 DYYRKRGggklpiKWM------APESLKDGKFTSKSDVWSFGVLLWEIFTL----------GE-------QPYpgMSNEE 212
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 15222437   304 KIFRVID-NRL-QDQYSMEEackVATLSLRCLTTEIKLRPNMSEVVSHL 350
Cdd:pfam07714 213 VLEFLEDgYRLpQPENCPDE---LYDLMKQCWAYDPEDRPTFSELVEDL 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
71-350 1.09e-52

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 176.57  E-value: 1.09e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437     71 DSVLGEGGFGCVFKGWIDEKSltasrPGTGLVIAVKKLNQD-GWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLL 149
Cdd:smart00219   4 GKKLGEGAFGEVYKGKLKGKG-----GKKKVEVAVKTLKEDaSEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437    150 VYEFMPRGSLENHLFRRGlyfQPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAKDGP 229
Cdd:smart00219  79 VMEYMEGGDLLSYLRKNR---PKLSLSDLLSFALQIARGMEYLESK--NFIHRDLAARNCLVGENLVVKISDFGLSRDLY 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437    230 igdkSHVSTRVMGTHG---YAAPEYLATGHLTTKSDVYSFGVVLLELLSGrravdknrpsGErnlvewaKPY--LVNKRK 304
Cdd:smart00219 154 ----DDDYYRKRGGKLpirWMAPESLKEGKFTSKSDVWSFGVLLWEIFTL----------GE-------QPYpgMSNEEV 212
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 15222437    305 IFRVID-NRLqdqySMEEAC--KVATLSLRCLTTEIKLRPNMSEVVSHL 350
Cdd:smart00219 213 LEYLKNgYRL----PQPPNCppELYDLMLQCWAEDPEDRPTFSELVEIL 257
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
71-350 2.02e-52

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: 175.81  E-value: 2.02e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437     71 DSVLGEGGFGCVFKGWideksLTASRPGTGLVIAVKKLNQD-GWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLL 149
Cdd:smart00221   4 GKKLGEGAFGEVYKGT-----LKGKGDGKEVEVAVKTLKEDaSEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437    150 VYEFMPRGSLENHLFRRGLYFqpLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAKDGP 229
Cdd:smart00221  79 VMEYMPGGDLLDYLRKNRPKE--LSLSDLLSFALQIARGMEYLESK--NFIHRDLAARNCLVGENLVVKISDFGLSRDLY 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437    230 IGD-KSHVSTRV----MgthgyaAPEYLATGHLTTKSDVYSFGVVLLELLSGrravdknrpsGErnlvewaKPY--LVNK 302
Cdd:smart00221 155 DDDyYKVKGGKLpirwM------APESLKEGKFTSKSDVWSFGVLLWEIFTL----------GE-------EPYpgMSNA 211
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 15222437    303 RKIFRVID-NRLQdqysMEEAC--KVATLSLRCLTTEIKLRPNMSEVVSHL 350
Cdd:smart00221 212 EVLEYLKKgYRLP----KPPNCppELYKLMLQCWAEDPEDRPTFSELVEIL 258
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
73-351 3.18e-52

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: 175.42  E-value: 3.18e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKGWIDEKsltasrPGTGLVIAVKKLNQDG-WQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVY 151
Cdd:cd00192   2 KLGEGAFGEVYKGKLKGG------DGKTVDVAVKTLKEDAsESERKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 152 EFMPRGSLENHLFRRGLYF-----QPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAK 226
Cdd:cd00192  76 EYMEGGDLLDFLRKSRPVFpspepSTLSLKDLLSFAIQIAKGMEYLASK--KFVHRDLAARNCLVGEDLVVKISDFGLSR 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 227 DGPIGDKshvstRVMGTHG-----YAAPEYLATGHLTTKSDVYSFGVVLLELLS-GrravdknrpsgernlvewAKPY-- 298
Cdd:cd00192 154 DIYDDDY-----YRKKTGGklpirWMAPESLKDGIFTSKSDVWSFGVLLWEIFTlG------------------ATPYpg 210
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15222437 299 LVNKrkifRVIDnRLQDQYSME--EAC--KVATLSLRCLTTEIKLRPNMSEVVSHLE 351
Cdd:cd00192 211 LSNE----EVLE-YLRKGYRLPkpENCpdELYELMLSCWQLDPEDRPTFSELVERLE 262
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
74-273 6.41e-50

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


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 167.83  E-value: 6.41e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQDGWQG-HQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYE 152
Cdd:cd00180   1 LGKGSFGKVYK---------ARDKETGKKVAVKVIPKEKLKKlLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVME 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMPRGSLENHLFRRglyFQPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPIGD 232
Cdd:cd00180  72 YCEGGSLKDLLKEN---KGPLSEEEALSILRQLLSALEYLHSN--GIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDD 146
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 15222437 233 KSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLEL 273
Cdd:cd00180 147 SLLKTTGGTTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL 187
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
68-349 2.96e-47

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 162.31  E-value: 2.96e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437     68 FRPDSVLGEGGFGCVFKgwideksltASRPGTGLVIAVKKLN-QDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEH 146
Cdd:smart00220   1 YEILEKLGEGSFGKVYL---------ARDKKTGKLVAIKVIKkKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDK 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437    147 RLLVYEFMPRGSLENHLFRRGlyfqPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAK 226
Cdd:smart00220  72 LYLVMEYCEGGDLFDLLKKRG----RLSEDEARFYLRQILSALEYLHSK--GIVHRDLKPENILLDEDGHVKLADFGLAR 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437    227 DgpIGDKSHVSTRVmGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRravdknRP-SGERNLVEwakpylvnkrkI 305
Cdd:smart00220 146 Q--LDPGEKLTTFV-GTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGK------PPfPGDDQLLE-----------L 205
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 15222437    306 FRVIDNRLQDQYSMEEACKVATLSL--RCLTTEIKLRPNMSEVVSH 349
Cdd:smart00220 206 FKKIGKPKPPFPPPEWDISPEAKDLirKLLVKDPEKRLTAEEALQH 251
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
67-359 2.25e-45

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 163.26  E-value: 2.25e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGCVFKGWideksltasRPGTGLVIAVKKLNQDgWQGHQEWLA----EVNYLGQFSHRHLVKLIGYCL 142
Cdd:COG0515   8 RYRILRLLGRGGMGVVYLAR---------DLRLGRPVALKVLRPE-LAADPEARErfrrEARALARLNHPNIVRVYDVGE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 143 EDEHRLLVYEFMPRGSLENHLFRRGlyfqPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDF 222
Cdd:COG0515  78 EDGRPYLVMEYVEGESLADLLRRRG----PLPPAEALRILAQLAEALAAAHAA--GIVHRDIKPANILLTPDGRVKLIDF 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 223 GLAKdgPIGDKSHVST-RVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRravdknRPSGERNLVEWAKPYLVN 301
Cdd:COG0515 152 GIAR--ALGGATLTQTgTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGR------PPFDGDSPAELLRAHLRE 223
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15222437 302 KRKIFRVIDNRLQDQysmeeackVATLSLRCLTTEIKLRP-NMSEVVSHLEHIQSLNAA 359
Cdd:COG0515 224 PPPPPSELRPDLPPA--------LDAIVLRALAKDPEERYqSAAELAAALRAVLRSLAA 274
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
67-352 9.61e-42

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: 147.73  E-value: 9.61e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQDGWQGHQEW---LAEVNYLGQFSHRHLVKLIGYCLE 143
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYR---------ARDTLLGRPVAIKVLRPELAEDEEFRerfLREARALARLSHPNIVRVYDVGED 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 144 DEHRLLVYEFMPRGSLENHLFRRGlyfqPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFG 223
Cdd:cd14014  72 DGRPYIVMEYVEGGSLADLLRERG----PLPPREALRILAQIADALAAAHRA--GIVHRDIKPANILLTEDGRVKLTDFG 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 224 LAKDGPIGDKSHVSTrVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRravdknRPSGERNLVEWAKPYLVNKR 303
Cdd:cd14014 146 IARALGDSGLTQTGS-VLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGR------PPFDGDSPAAVLAKHLQEAP 218
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 15222437 304 KIFRVIDNRLQDQysmeeackVATLSLRCLTTEIKLRP-NMSEVVSHLEH 352
Cdd:cd14014 219 PPPSPLNPDVPPA--------LDAIILRALAKDPEERPqSAAELLAALRA 260
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
74-346 2.42e-39

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: 141.82  E-value: 2.42e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWidEKSLtasrpgtGLVIAVKKL--NQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVY 151
Cdd:cd13978   1 LGSGGFGTVSKAR--HVSW-------FGMVAIKCLhsSPNCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVM 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 152 EFMPRGSLeNHLFRRglYFQPLSWKLRLKVALGAAKGLAFLHSSETRVIYRDFKTSNILLDSEYNAKLSDFGLAKdgpIG 231
Cdd:cd13978  72 EYMENGSL-KSLLER--EIQDVPWSLRFRIIHEIALGMNFLHNMDPPLLHHDLKPENILLDNHFHVKISDFGLSK---LG 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 232 DKSHVSTRVMGT---HG---YAAPEYLATGHL--TTKSDVYSFGVVLLELLSGRravdKNRPSGERNLVEWAKPYLVNkR 303
Cdd:cd13978 146 MKSISANRRRGTenlGGtpiYMAPEAFDDFNKkpTSKSDVYSFAIVIWAVLTRK----EPFENAINPLLIMQIVSKGD-R 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 15222437 304 KIFRVIDnRLQDQYSMEEACKvatLSLRCLTTEIKLRPNMSEV 346
Cdd:cd13978 221 PSLDDIG-RLKQIENVQELIS---LMIRCWDGNPDARPTFLEC 259
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
74-351 5.41e-38

Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. 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 (a pseudokinase in the case of IRAK3), 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. IRAK3 (or IRAK-M) is the only IRAK that does not show kinase activity. It is found only in monocytes and macrophages in humans, and functions as a negative regulator of TLR signaling including TLR-2 induced p38 activation. It also negatively regulates the alternative NFkB pathway in a TLR-2 specific manner. IRAK3 is downregulated in the monocytes of obese people, and is associated with high SOD2, a marker of mitochondrial oxidative stress. It is an important inhibitor of inflammation in association with obesity and metabolic syndrome. The IRAK3 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: 271062 [Multi-domain]  Cd Length: 276  Bit Score: 138.48  E-value: 5.41e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWIDEKSLTasrpgtglVIAVKKLNQDGWQGHQE-WLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYE 152
Cdd:cd14160   1 IGEGEIFEVYRVRIGNRSYA--------VKLFKQEKKMQWKKHWKrFLSELEVLLLFQHPNILELAAYFTETEKFCLVYP 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMPRGSLENHLFRRGLYfQPLSWKLRLKVALGAAKGLAFLHSSE-TRVIYRDFKTSNILLDSEYNAKLSDFGLAKDGP-I 230
Cdd:cd14160  73 YMQNGTLFDRLQCHGVT-KPLSWHERINILIGIAKAIHYLHNSQpCTVICGNISSANILLDDQMQPKLTDFALAHFRPhL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 231 GDKShvSTRVMGTH-----GYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAV-DKNRPSGERNLVEwakpYLVNKRK 304
Cdd:cd14160 152 EDQS--CTINMTTAlhkhlWYMPEEYIRQGKLSVKTDVYSFGIVIMEVLTGCKVVlDDPKHLQLRDLLH----ELMEKRG 225
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 15222437 305 I---FRVIDNRLQdQYSMEEACKVATLSLRCLTTEIKLRPNMSEVVSHLE 351
Cdd:cd14160 226 LdscLSFLDLKFP-PCPRNFSAKLFRLAGRCTATKAKLRPDMDEVLQRLE 274
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
72-277 1.34e-35

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: 131.17  E-value: 1.34e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  72 SVLGEGGFGCVFKGWiDEKsltasrpgTGLVIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVY 151
Cdd:cd05122   6 EKIGKGGFGVVYKAR-HKK--------TGQIVAIKKINLESKEKKESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVM 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 152 EFMPRGSLENhLFRrgLYFQPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAKDgpiG 231
Cdd:cd05122  77 EFCSGGSLKD-LLK--NTNKTLTEQQIAYVCKEVLKGLEYLHSH--GIIHRDIKAANILLTSDGEVKLIDFGLSAQ---L 148
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15222437 232 DKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd05122 149 SDGKTRNTFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGK 194
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
66-275 5.77e-35

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: 130.58  E-value: 5.77e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  66 RNFRPDSVLGEGGFGCVFKGwidekSLTASRPGTGLVIAVKKLNQDGWQGHQE-WLAEVNYLGQFSHRHLVKLIGYClED 144
Cdd:cd05038   4 RHLKFIKQLGEGHFGSVELC-----RYDPLGDNTGEQVAVKSLQPSGEEQHMSdFKREIEILRTLDHEYIVKYKGVC-ES 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 145 EHR---LLVYEFMPRGSLENHLfrRGLYFQpLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSD 221
Cdd:cd05038  78 PGRrslRLIMEYLPSGSLRDYL--QRHRDQ-IDLKRLLLFASQICKGMEYLGSQ--RYIHRDLAARNILVESEDLVKISD 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15222437 222 FGLAKDGPIGDKSHVST--RVMGTHGYaAPEYLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:cd05038 153 FGLAKVLPEDKEYYYVKepGESPIFWY-APECLRESRFSSASDVWSFGVTLYELFT 207
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
72-353 4.24e-34

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: 127.47  E-value: 4.24e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  72 SVLGEGGFGCVFKG-WIDEKsltasrpgtglvIAVKKLNQDGwQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLV 150
Cdd:cd05039  12 ELIGKGEFGDVMLGdYRGQK------------VAVKCLKDDS-TAAQAFLAEASVMTTLRHPNLVQLLGVVLEGNGLYIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 151 YEFMPRGSLENHLFRRGLyfQPLSWKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAKDgpi 230
Cdd:cd05039  79 TEYMAKGSLVDYLRSRGR--AVITRKDQLGFALDVCEGMEYLESKK--FVHRDLAARNVLVSEDNVAKVSDFGLAKE--- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 231 GDKSHVSTR--VMGThgyaAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAvdknrpsgernlvewakPYlvnKRKIFRV 308
Cdd:cd05039 152 ASSNQDGGKlpIKWT----APEALREKKFSTKSDVWSFGILLWEIYSFGRV-----------------PY---PRIPLKD 207
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 15222437 309 IDNRLQDQYSME--EAC--KVATLSLRCLTTEIKLRPNMSEVVSHLEHI 353
Cdd:cd05039 208 VVPHVEKGYRMEapEGCppEVYKVMKNCWELDPAKRPTFKQLREKLEHI 256
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
73-278 1.57e-31

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


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 120.70  E-value: 1.57e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKGwIDEKsltasrpgTGLVIAVKKLN-QDGWQGHQEWL-AEVNYLGQFSHRHLVKLIGYCLEDEHRLLV 150
Cdd:cd06606   7 LLGKGSFGSVYLA-LNLD--------TGELMAVKEVElSGDSEEELEALeREIRILSSLKHPNIVRYLGTERTENTLNIF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 151 YEFMPRGSLENHLFRrglyFQPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPI 230
Cdd:cd06606  78 LEYVPGGSLASLLKK----FGKLPEPVVRKYTRQILEGLEYLHSN--GIVHRDIKGANILVDSDGVVKLADFGCAKRLAE 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15222437 231 GDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRR 278
Cdd:cd06606 152 IATGEGTKSLRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKP 199
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
74-276 2.20e-31

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: 120.02  E-value: 2.20e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGwIDEKsltasrpgTGLVIAVK--KLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVY 151
Cdd:cd06627   8 IGRGAFGSVYKG-LNLN--------TGEFVAIKqiSLEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIIL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 152 EFMPRGSLENHLFRrglyFQPLSWKLrlkVALGAA---KGLAFLHssETRVIYRDFKTSNILLDSEYNAKLSDFGLAKDG 228
Cdd:cd06627  79 EYVENGSLASIIKK----FGKFPESL---VAVYIYqvlEGLAYLH--EQGVIHRDIKGANILTTKDGLVKLADFGVATKL 149
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15222437 229 PIGDKSHVStrVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd06627 150 NEVEKDENS--VVGTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTG 195
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
74-351 8.11e-30

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: 116.29  E-value: 8.11e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWIDekslTASRPGTGLVIAVKKLNQDGWQGHQ-EWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYE 152
Cdd:cd05032  14 LGQGSFGMVYEGLAK----GVVKGEPETRVAIKTVNENASMRERiEFLNEASVMKEFNCHHVVRLLGVVSTGQPTLVVME 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMPRGSLENHLFRR------GLYFQPLSWKLRLKVALGAAKGLAFLHssETRVIYRDFKTSNILLDSEYNAKLSDFGLAK 226
Cdd:cd05032  90 LMAKGDLKSYLRSRrpeaenNPGLGPPTLQKFIQMAAEIADGMAYLA--AKKFVHRDLAARNCMVAEDLTVKIGDFGMTR 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 227 D-------GPIGdKSHVSTRVMgthgyaAPEYLATGHLTTKSDVYSFGVVLLELLSgrravdknrpsgernLVEwaKPY- 298
Cdd:cd05032 168 DiyetdyyRKGG-KGLLPVRWM------APESLKDGVFTTKSDVWSFGVVLWEMAT---------------LAE--QPYq 223
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15222437 299 -LVNKRKIFRVIDNRLQDQysmEEAC--KVATLSLRCLTTEIKLRPNMSEVVSHLE 351
Cdd:cd05032 224 gLSNEEVLKFVIDGGHLDL---PENCpdKLLELMRMCWQYNPKMRPTFLEIVSSLK 276
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
66-351 5.97e-29

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: 114.23  E-value: 5.97e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  66 RNFRPDSVLGEGGFGCVfkgwidekSLTASRP---GTGLVIAVKKLNQDGWQGHQE-WLAEVNYLGQFSHRHLVKLIGYC 141
Cdd:cd05080   4 RYLKKIRDLGEGHFGKV--------SLYCYDPtndGTGEMVAVKALKADCGPQHRSgWKQEIDILKTLYHENIVKYKGCC 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 142 LE--DEHRLLVYEFMPRGSLENHLFRRGLYFQPLswklrLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKL 219
Cdd:cd05080  76 SEqgGKSLQLIMEYVPLGSLRDYLPKHSIGLAQL-----LLFAQQICEGMAYLHSQ--HYIHRDLAARNVLLDNDRLVKI 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 220 SDFGLAKDGPIGDKSH-VSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSgrRAVDKNRPSGERNLVEWAKPY 298
Cdd:cd05080 149 GDFGLAKAVPEGHEYYrVREDGDSPVFWYAPECLKEYKFYYASDVWSFGVTLYELLT--HCDSSQSPPTKFLEMIGIAQG 226
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 15222437 299 LVNKRKIFRVIDNRLQDQYSMEEACKVATLSLRCLTTEIKLRPNMSEVVSHLE 351
Cdd:cd05080 227 QMTVVRLIELLERGERLPCPDKCPQEVYHLMKNCWETEASFRPTFENLIPILK 279
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
73-278 6.46e-29

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: 114.05  E-value: 6.46e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKG-WIDEKSltasrpGTGLVIAVKKLNQD-GWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHrLLV 150
Cdd:cd05057  14 VLGSGAFGTVYKGvWIPEGE------KVKIPVAIKVLREEtGPKANEEILDEAYVMASVDHPHLVRLLGICLSSQV-QLI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 151 YEFMPRGSL----ENHLFRRGLYfQPLSWKLRLkvalgaAKGLAFLhsSETRVIYRDFKTSNILLDSEYNAKLSDFGLAK 226
Cdd:cd05057  87 TQLMPLGCLldyvRNHRDNIGSQ-LLLNWCVQI------AKGMSYL--EEKRLVHRDLAARNVLVKTPNHVKITDFGLAK 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15222437 227 DGPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLS-GRR 278
Cdd:cd05057 158 LLDVDEKEYHAEGGKVPIKWMALESIQYRIYTHKSDVWSYGVTVWELMTfGAK 210
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
73-276 8.99e-29

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


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 113.26  E-value: 8.99e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKG-WIDEksltasrpgtglVIAVKKLNQDGWQGHQEWLA----EVNYLGQFSHRHLVKLIGYCLEDEHR 147
Cdd:cd14061   1 VIGVGGFGKVYRGiWRGE------------EVAVKAARQDPDEDISVTLEnvrqEARLFWMLRHPNIIALRGVCLQPPNL 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 148 LLVYEFMPRGSLENHLFRRGLyfQP---LSWklrlkvALGAAKGLAFLHS-SETRVIYRDFKTSNILLDSEYNA------ 217
Cdd:cd14061  69 CLVMEYARGGALNRVLAGRKI--PPhvlVDW------AIQIARGMNYLHNeAPVPIIHRDLKSSNILILEAIENedlenk 140
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15222437 218 --KLSDFGLAKDgpigdkSHVSTRV--MGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14061 141 tlKITDFGLARE------WHKTTRMsaAGTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTG 197
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
71-352 2.83e-28

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: 112.08  E-value: 2.83e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  71 DSVLGEGGFGCVFKGWIdekSLTASRPgtgLVIAVKKLnQDGWQGHQEW--LAEVNYLGQFSHRHLVKLIGYCLEDEHRL 148
Cdd:cd05033   9 EKVIGGGEFGEVCSGSL---KLPGKKE---IDVAIKTL-KSGYSDKQRLdfLTEASIMGQFDHPNVIRLEGVVTKSRPVM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 LVYEFMPRGSLENHLFRRGLYFQPLswKLrLKVALGAAKGLAFLhsSETRVIYRDFKTSNILLDSEYNAKLSDFGLAKDg 228
Cdd:cd05033  82 IVTEYMENGSLDKFLRENDGKFTVT--QL-VGMLRGIASGMKYL--SEMNYVHRDLAARNILVNSDLVCKVSDFGLSRR- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 229 pIGDKSHVSTrvmgTHG------YAAPEYLATGHLTTKSDVYSFGVVLLELLSgrravdknrpSGERnlvewakPY--LV 300
Cdd:cd05033 156 -LEDSEATYT----TKGgkipirWTAPEAIAYRKFTSASDVWSFGIVMWEVMS----------YGER-------PYwdMS 213
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 15222437 301 NKRKIFRVIDN-RLQDqySMEEACKVATLSLRCLTTEIKLRPNMSEVVSHLEH 352
Cdd:cd05033 214 NQDVIKAVEDGyRLPP--PMDCPSALYQLMLDCWQKDRNERPTFSQIVSTLDK 264
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
74-353 5.32e-28

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


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 110.99  E-value: 5.32e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKG-WideksltasrpgTGLVIAVKKLNQDGWQghQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYE 152
Cdd:cd14058   1 VGRGSFGVVCKArW------------RNQIVAVKIIESESEK--KAFEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVME 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMPRGSLENHLFRRGL-----YFQPLSWklrlkvALGAAKGLAFLHSSETR-VIYRDFKTSNILLDSEY-NAKLSDFGLA 225
Cdd:cd14058  67 YAEGGSLYNVLHGKEPkpiytAAHAMSW------ALQCAKGVAYLHSMKPKaLIHRDLKPPNLLLTNGGtVLKICDFGTA 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 226 kdgpiGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVDKnrPSGERNLVEWA-----KPYLV 300
Cdd:cd14058 141 -----CDISTHMTNNKGSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPFDH--IGGPAFRIMWAvhngeRPPLI 213
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 15222437 301 nkrkifRVIDNRLQDqysmeeackvatLSLRCLTTEIKLRPNMSEVVSHLEHI 353
Cdd:cd14058 214 ------KNCPKPIES------------LMTRCWSKDPEKRPSMKEIVKIMSHL 248
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
74-350 1.02e-27

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: 110.13  E-value: 1.02e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWIDEKSltasrpGTGLVIAVKKLNQDG-WQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEdEHRLLVYE 152
Cdd:cd05060   3 LGHGNFGSVRKGVYLMKS------GKEVEVAVKTLKQEHeKAGKKEFLREASVMAQLDHPCIVRLIGVCKG-EPLMLVME 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMPRGSLENHLFRRGlYFQPLSWKLrlkVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPIGD 232
Cdd:cd05060  76 LAPLGPLLKYLKKRR-EIPVSDLKE---LAHQVAMGMAYLESK--HFVHRDLAARNVLLVNRHQAKISDFGMSRALGAGS 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 233 KSHVSTrvmgTHG-----YAAPEYLATGHLTTKSDVYSFGVVLLELLS-GrravdknrpsgernlvewAKPYlvnKRKIF 306
Cdd:cd05060 150 DYYRAT----TAGrwplkWYAPECINYGKFSSKSDVWSYGVTLWEAFSyG------------------AKPY---GEMKG 204
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 15222437 307 RVIDNRLQDQYSME--EAC--KVATLSLRCLTTEIKLRPNMSEVVSHL 350
Cdd:cd05060 205 PEVIAMLESGERLPrpEECpqEIYSIMLSCWKYRPEDRPTFSELESTF 252
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
100-350 2.51e-27

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: 109.40  E-value: 2.51e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 100 GLVIAVKKLNQDGWQGHQEwLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEFMPRGSLENHLFRRGlyfQPLSWKLRL 179
Cdd:cd13992  25 GRTVAIKHITFSRTEKRTI-LQELNQLKELVHDNLNKFIGICINPPNIAVVTEYCTRGSLQDVLLNRE---IKMDWMFKS 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 180 KVALGAAKGLAFLHSSETRVIYRdFKTSNILLDSEYNAKLSDFGLA---KDGPIGDKSHVSTRVMGThgYAAPEYL---A 253
Cdd:cd13992 101 SFIKDIVKGMNYLHSSSIGYHGR-LKSSNCLVDSRWVVKLTDFGLRnllEEQTNHQLDEDAQHKKLL--WTAPELLrgsL 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 254 TGH-LTTKSDVYSFGVVLLELLSgrravdKNRPSGERNLVEWAKPYLVNKRKIFRVIDNRLQDQYSMEeackVATLSLRC 332
Cdd:cd13992 178 LEVrGTQKGDVYSFAIILYEILF------RSDPFALEREVAIVEKVISGGNKPFRPELAVLLDEFPPR----LVLLVKQC 247
                       250
                ....*....|....*...
gi 15222437 333 LTTEIKLRPNMSEVVSHL 350
Cdd:cd13992 248 WAENPEKRPSFKQIKKTL 265
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
73-350 5.47e-27

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: 108.86  E-value: 5.47e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKG----------WIDEKSLTASRPGTGLVIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCL 142
Cdd:cd14000   1 LLGDGGFGSVYRAsykgepvavkIFNKHTSSNFANVPADTMLRHLRATDAMKNFRLLRQELTVLSHLHHPSIVYLLGIGI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 143 EDehRLLVYEFMPRGSLENHLFRRGLYFQPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEY-----NA 217
Cdd:cd14000  81 HP--LMLVLELAPLGSLDHLLQQDSRSFASLGRTLQQRIALQVADGLRYLHSA--MIIYRDLKSHNVLVWTLYpnsaiII 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 218 KLSDFGLAKDG-PIGDKShvstrVMGTHGYAAPEyLATGHL--TTKSDVYSFGVVLLELLSGRR-AVDKNRPSGERNLVE 293
Cdd:cd14000 157 KIADYGISRQCcRMGAKG-----SEGTPGFRAPE-IARGNViyNEKVDVFSFGMLLYEILSGGApMVGHLKFPNEFDIHG 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15222437 294 WAKPYLvnkrkifrvidnrlqDQYSMEEACKVATLSLRCLTTEIKLRPNMSEVVSHL 350
Cdd:cd14000 231 GLRPPL---------------KQYECAPWPEVEVLMKKCWKENPQQRPTAVTVVSIL 272
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
67-351 5.47e-27

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: 108.90  E-value: 5.47e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGCVFKGWIDEkslTASRPGTGLViAVKKLNQDGWQGH-QEWLAEVNYLGQFSHRHLVKLIGYCLEDE 145
Cdd:cd05045   1 NLVLGKTLGEGEFGKVVKATAFR---LKGRAGYTTV-AVKMLKENASSSElRDLLSEFNLLKQVNHPHVIKLYGACSQDG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 146 HRLLVYEFMPRGSLENHL---------------FRRGLYF-----QPLSWKLRLKVALGAAKGLAFLhsSETRVIYRDFK 205
Cdd:cd05045  77 PLLLIVEYAKYGSLRSFLresrkvgpsylgsdgNRNSSYLdnpdeRALTMGDLISFAWQISRGMQYL--AEMKLVHRDLA 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 206 TSNILLDSEYNAKLSDFGLAKDGPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSgrravdknrp 285
Cdd:cd05045 155 ARNVLVAEGRKMKISDFGLSRDVYEEDSYVKRSKGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVT---------- 224
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15222437 286 sgernlvEWAKPYL-VNKRKIFrvidNRLQDQYSME--EAC--KVATLSLRCLTTEIKLRPNMSEVVSHLE 351
Cdd:cd05045 225 -------LGGNPYPgIAPERLF----NLLKTGYRMErpENCseEMYNLMLTCWKQEPDKRPTFADISKELE 284
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
74-346 6.38e-27

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: 107.88  E-value: 6.38e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQDGWQG--HQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVY 151
Cdd:cd08529   8 LGKGSFGVVYK---------VVRKVDGRVYALKQIDISRMSRkmREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 152 EFMPRGSLENHLFR-RGlyfQPLS----WKLRLKVALGaakgLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAK 226
Cdd:cd08529  79 EYAENGDLHSLIKSqRG---RPLPedqiWKFFIQTLLG----LSHLHSK--KILHRDIKSMNIFLDKGDNVKIGDLGVAK 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 227 dgPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVDKNrpsGERNLVewakpylvnkRKIF 306
Cdd:cd08529 150 --ILSDTTNFAQTIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQ---NQGALI----------LKIV 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 15222437 307 RVIDNRLQDQYSMEeackVATLSLRCLTTEIKLRPNMSEV 346
Cdd:cd08529 215 RGKYPPISASYSQD----LSQLIDSCLTKDYRQRPDTTEL 250
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
74-276 8.37e-27

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: 107.53  E-value: 8.37e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWIDeksltasrpGTGLVIAVKKLNQDGWQGH-QEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYE 152
Cdd:cd05041   3 IGRGNFGDVYRGVLK---------PDNTEVAVKTCRETLPPDLkRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMIVME 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMPRGSLENHLFRRGlyfQPLSWKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPIGD 232
Cdd:cd05041  74 LVPGGSLLTFLRKKG---ARLTVKQLLQMCLDAAAGMEYLESKN--CIHRDLAARNCLVGENNVLKISDFGMSREEEDGE 148
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 15222437 233 KSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd05041 149 YTVSDGLKQIPIKWTAPEALNYGRYTSESDVWSFGILLWEIFSL 192
STKc_IRAK2 cd14157
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; ...
76-351 8.57e-27

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; 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. IRAK2 plays a role in mediating NFkB activation by TLR3, TLR4, and TLR8. It is specifically targeted by the viral protein A52, which is important for virulence, to inhibit all IL-1/TLR pathways, indicating that IRAK2 has a predominant role in NFkB activation. It is redundant with IRAK1 in early signaling but is critical for late and sustained activation. The IRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271059 [Multi-domain]  Cd Length: 289  Bit Score: 108.39  E-value: 8.57e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  76 EGGFGCVFKGWIDeksltasrpgtGLVIAVKKLNQDGWQGHQE----WLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVY 151
Cdd:cd14157   3 EGTFADIYKGYRH-----------GKQYVIKRLKETECESPKSterfFQTEVQICFRCCHPNILPLLGFCVESDCHCLIY 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 152 EFMPRGSLENHLFRRGLYfQPLSWKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLaKDGPIG 231
Cdd:cd14157  72 PYMPNGSLQDRLQQQGGS-HPLPWEQRLSISLGLLKAVQHLHNFG--ILHGNIKSSNVLLDGNLLPKLGHSGL-RLCPVD 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 232 DKS---HVSTRVMGTHGYAAPE-YLATGHLTTKSDVYSFGVVLLELLSGRRAVDKNR-PSGERNL----VEWAKPYLVNK 302
Cdd:cd14157 148 KKSvytMMKTKVLQISLAYLPEdFVRHGQLTEKVDIFSCGVVLAEILTGIKAMDEFRsPVYLKDLlleeIQRAKEGSQSK 227
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15222437 303 RKIF-----RVIDNRLQDQYS--MEEACKVATLSLRCLTTEiKLRPNMSEVVSHLE 351
Cdd:cd14157 228 HKSPeslaaKEICSKYLDKRAglLPENVAFSLAFAACLCLR-KKNPLLPEVYEIVE 282
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
66-277 1.50e-26

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: 107.38  E-value: 1.50e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  66 RNFRPDSVLGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQDGWQGHQE-WLAEVNYLGQFSHRHLVKLIGYCLED 144
Cdd:cd13996   6 NDFEEIELLGSGGFGSVYK---------VRNKVDGVTYAIKKIRLTEKSSASEkVLREVKALAKLNHPNIVRYYTAWVEE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 145 EHRLLVYEFMPRGSLENHLFRRGLyFQPLSWKLRLKVALGAAKGLAFLHSseTRVIYRDFKTSNILLDSE-YNAKLSDFG 223
Cdd:cd13996  77 PPLYIQMELCEGGTLRDWIDRRNS-SSKNDRKLALELFKQILKGVSYIHS--KGIVHRDLKPSNIFLDNDdLQVKIGDFG 153
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15222437 224 LAK------------DGPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd13996 154 LATsignqkrelnnlNNNNNGNTSNNSVGIGTPLYASPEQLDGENYNEKADIYSLGIILFEMLHPF 219
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
74-351 2.30e-26

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: 106.50  E-value: 2.30e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWIdeksltasrpgTGLVIAVKKLNQDgwQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDeHRLLVYEF 153
Cdd:cd05083  14 IGEGEFGAVLQGEY-----------MGQKVAVKNIKCD--VTAQAFLEETAVMTKLQHKNLVRLLGVILHN-GLYIVMEL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 154 MPRGSLENHLFRRGLYFQPLSWKLRLkvALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPIG-D 232
Cdd:cd05083  80 MSKGNLVNFLRSRGRALVPVIQLLQF--SLDVAEGMEYLESK--KLVHRDLAARNILVSEDGVAKISDFGLAKVGSMGvD 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 233 KSHVSTRvmgthgYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAvdknrpsgernlvewakPYlvnKRKIFRVIDNR 312
Cdd:cd05083 156 NSRLPVK------WTAPEALKNKKFSSKSDVWSYGVLLWEVFSYGRA-----------------PY---PKMSVKEVKEA 209
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 15222437 313 LQDQYSME--EAC--KVATLSLRCLTTEIKLRPNMSEVVSHLE 351
Cdd:cd05083 210 VEKGYRMEppEGCppDVYSIMTSCWEAEPGKRPSFKKLREKLE 252
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
74-288 3.05e-26

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: 106.19  E-value: 3.05e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKG-WIDEKSltasrpgtglvIAVKKLnQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYE 152
Cdd:cd05112  12 IGSGQFGLVHLGyWLNKDK-----------VAIKTI-REGAMSEEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMPRGSLENHL-FRRGLyfqpLSWKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAKdGPIG 231
Cdd:cd05112  80 FMEHGCLSDYLrTQRGL----FSAETLLGMCLDVCEGMAYLEEAS--VIHRDLAARNCLVGENQVVKVSDFGMTR-FVLD 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15222437 232 DKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVDKNRPSGE 288
Cdd:cd05112 153 DQYTSSTGTKFPVKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSEGKIPYENRSNSE 209
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
73-353 3.12e-26

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: 106.60  E-value: 3.12e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKGWIdeksltaSRPGTGLV-IAVKKLnQDGW--QGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLL 149
Cdd:cd05063  12 VIGAGEFGEVFRGIL-------KMPGRKEVaVAIKTL-KPGYteKQRQDFLSEASIMGQFSHHNIIRLEGVVTKFKPAMI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 150 VYEFMPRGSLENHLFRRGLYFQPLSWKLRLKvalGAAKGLAFLhsSETRVIYRDFKTSNILLDSEYNAKLSDFGLAK--- 226
Cdd:cd05063  84 ITEYMENGALDKYLRDHDGEFSSYQLVGMLR---GIAAGMKYL--SDMNYVHRDLAARNILVNSNLECKVSDFGLSRvle 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 227 DGPIGDKSHVSTRVmgTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSgrravdknrpSGERnlvewakPYL-VNKRKI 305
Cdd:cd05063 159 DDPEGTYTTSGGKI--PIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMS----------FGER-------PYWdMSNHEV 219
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 15222437 306 FRVIDNRLQDQYSMEEACKVATLSLRCLTTEIKLRPNMSEVVSHLEHI 353
Cdd:cd05063 220 MKAINDGFRLPAPMDCPSAVYQLMLQCWQQDRARRPRFVDIVNLLDKL 267
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
73-355 5.59e-26

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: 105.63  E-value: 5.59e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKG-WIDEKsltasrpGTGLVIAVKKLNQ-DGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHR-LL 149
Cdd:cd05058   2 VIGKGHFGCVYHGtLIDSD-------GQKIHCAVKSLNRiTDIEEVEQFLKEGIIMKDFSHPNVLSLLGICLPSEGSpLV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 150 VYEFMPRGSLENhlFRRGLYFQPlSWKLRLKVALGAAKGLAFLhsSETRVIYRDFKTSNILLDSEYNAKLSDFGLAKDgp 229
Cdd:cd05058  75 VLPYMKHGDLRN--FIRSETHNP-TVKDLIGFGLQVAKGMEYL--ASKKFVHRDLAARNCMLDESFTVKVADFGLARD-- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 230 IGDKSHVSTRvMGTHG-----YAAPEYLATGHLTTKSDVYSFGVVLLELLSgrRAVDKNRPSGERNLVEwakpYLVNKRK 304
Cdd:cd05058 148 IYDKEYYSVH-NHTGAklpvkWMALESLQTQKFTTKSDVWSFGVLLWELMT--RGAPPYPDVDSFDITV----YLLQGRR 220
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 15222437 305 IfrvidnrLQDQYSMEeacKVATLSLRCLTTEIKLRPNMSEVVSHLEHIQS 355
Cdd:cd05058 221 L-------LQPEYCPD---PLYEVMLSCWHPKPEMRPTFSELVSRISQIFS 261
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
77-291 6.61e-26

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


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 105.87  E-value: 6.61e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  77 GGFGCVFKGWIDEKsltasrpgtglVIAVKKLNQdgwQGHQEWLAEVNY--LGQFSHRHLVKLIG-----YCLEDEHrLL 149
Cdd:cd14053   6 GRFGAVWKAQYLNR-----------LVAVKIFPL---QEKQSWLTEREIysLPGMKHENILQFIGaekhgESLEAEY-WL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 150 VYEFMPRGSLENHLfrrglYFQPLSWKLRLKVALGAAKGLAFLHS--------SETRVIYRDFKTSNILLDSEYNAKLSD 221
Cdd:cd14053  71 ITEFHERGSLCDYL-----KGNVISWNELCKIAESMARGLAYLHEdipatnggHKPSIAHRDFKSKNVLLKSDLTACIAD 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 222 FGLA----KDGPIGDkSHVStrvMGTHGYAAPEYL--ATgHLTTKS----DVYSFGVVLLELLSgrRAVDKNRPSGERNL 291
Cdd:cd14053 146 FGLAlkfePGKSCGD-THGQ---VGTRRYMAPEVLegAI-NFTRDAflriDMYAMGLVLWELLS--RCSVHDGPVDEYQL 218
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
75-351 6.72e-26

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


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 105.04  E-value: 6.72e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  75 GEGGFGCVFKG-WIDEksltasrpgtGLVIAVKKLNQDGwqghqewlAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEF 153
Cdd:cd14060   2 GGGSFGSVYRAiWVSQ----------DKEVAVKKLLKIE--------KEAEILSVLSHRNIIQFYGAILEAPNYGIVTEY 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 154 MPRGSLENHLFRRGL----YFQPLSWklrlkvALGAAKGLAFLHS-SETRVIYRDFKTSNILLDSEYNAKLSDFGLAKdg 228
Cdd:cd14060  64 ASYGSLFDYLNSNESeemdMDQIMTW------ATDIAKGMHYLHMeAPVKVIHRDLKSRNVVIAADGVLKICDFGASR-- 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 229 PIGDKSHVStrVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSgrRAVDKNRPSGERnlVEWAkpylvnkrkifrV 308
Cdd:cd14060 136 FHSHTTHMS--LVGTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLT--REVPFKGLEGLQ--VAWL------------V 197
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 15222437 309 IDNrlQDQYSMEEAC--KVATLSLRCLTTEIKLRPNMSEVVSHLE 351
Cdd:cd14060 198 VEK--NERPTIPSSCprSFAELMRRCWEADVKERPSFKQIIGILE 240
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
66-353 7.69e-26

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: 105.06  E-value: 7.69e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  66 RNFRPDSVLGEGGFGCVFKGwiDEKsltasrpgtGLVIAVKKLNQDGwqGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDE 145
Cdd:cd05082   6 KELKLLQTIGKGEFGDVMLG--DYR---------GNKVAVKCIKNDA--TAQAFLAEASVMTQLRHSNLVQLLGVIVEEK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 146 HRL-LVYEFMPRGSLENHLFRRGLYFqpLSWKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGL 224
Cdd:cd05082  73 GGLyIVTEYMAKGSLVDYLRSRGRSV--LGGDCLLKFSLDVCEAMEYLEGNN--FVHRDLAARNVLVSEDNVAKVSDFGL 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 225 AKD-GPIGDKSHVSTRvmgthgYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAvdknrpsgernlvewakPYlvnKR 303
Cdd:cd05082 149 TKEaSSTQDTGKLPVK------WTAPEALREKKFSTKSDVWSFGILLWEIYSFGRV-----------------PY---PR 202
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 15222437 304 KIFRVIDNRLQDQYSME--EACKVATLSL--RCLTTEIKLRPNMSEVVSHLEHI 353
Cdd:cd05082 203 IPLKDVVPRVEKGYKMDapDGCPPAVYDVmkNCWHLDAAMRPSFLQLREQLEHI 256
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
72-349 8.07e-26

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: 104.91  E-value: 8.07e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  72 SVLGEGGFGCVFKGwIDEKsltasrpgTGLVIAVKKLN----QDGWQGHQEwlAEVNYLGQFSHRHLVKLIGYcLEDEHR 147
Cdd:cd14003   6 KTLGEGSFGKVKLA-RHKL--------TGEKVAIKIIDksklKEEIEEKIK--REIEIMKLLNHPNIIKLYEV-IETENK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 148 L-LVYEFMPRGSLENHLFRRG--------LYFQPLSwklrlkvalgaaKGLAFLHSSetRVIYRDFKTSNILLDSEYNAK 218
Cdd:cd14003  74 IyLVMEYASGGELFDYIVNNGrlsedearRFFQQLI------------SAVDYCHSN--GIVHRDLKLENILLDKNGNLK 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 219 LSDFGLAKDGPIGDKSHvsTRVmGTHGYAAPEYLA-TGHLTTKSDVYSFGVVLLELLSGRravdknRPSGERNLVEwakp 297
Cdd:cd14003 140 IIDFGLSNEFRGGSLLK--TFC-GTPAYAAPEVLLgRKYDGPKADVWSLGVILYAMLTGY------LPFDDDNDSK---- 206
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 15222437 298 ylvNKRKIFRVIdnrLQDQYSMEEACKvaTLSLRCLTTEIKLRPNMSEVVSH 349
Cdd:cd14003 207 ---LFRKILKGK---YPIPSHLSPDAR--DLIRRMLVVDPSKRITIEEILNH 250
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
74-275 9.13e-26

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: 105.54  E-value: 9.13e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWIdeksLTASRPGTGLVIAVKKLNQDGW-QGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYE 152
Cdd:cd05048  13 LGEGAFGKVYKGEL----LGPSSEESAISVAIKTLKENASpKTQQDFRREAELMSDLQHPNIVCLLGVCTKEQPQCMLFE 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMPRGSLENHLFRRGLYFQP------------LSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLS 220
Cdd:cd05048  89 YMAHGDLHEFLVRHSPHSDVgvssdddgtassLDQSDFLHIAIQIAAGMEYLSSH--HYVHRDLAARNCLVGDGLTVKIS 166
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15222437 221 DFGLAKDGPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:cd05048 167 DFGLSRDIYSSDYYRVQSKSLLPVRWMPPEAILYGKFTTESDVWSFGVVLWEIFS 221
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
74-277 1.18e-25

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: 104.14  E-value: 1.18e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQDGWQGHQEW---LAEVNYLGQFSHRHLVKLIgYCLEDEHRL-L 149
Cdd:cd05123   1 LGKGSFGKVLL---------VRKKDTGKLYAMKVLRKKEIIKRKEVehtLNERNILERVNHPFIVKLH-YAFQTEEKLyL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 150 VYEFMPRGSLENHLFRRGlYFqPLSWklrlkVALGAAK---GLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAK 226
Cdd:cd05123  71 VLDYVPGGELFSHLSKEG-RF-PEER-----ARFYAAEivlALEYLHSL--GIIYRDLKPENILLDSDGHIKLTDFGLAK 141
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15222437 227 DGpIGDKSHVSTRVmGTHGYAAPEYL-ATGHltTKS-DVYSFGVVLLELLSGR 277
Cdd:cd05123 142 EL-SSDGDRTYTFC-GTPEYLAPEVLlGKGY--GKAvDWWSLGVLLYEMLTGK 190
Pkinase pfam00069
Protein kinase domain;
68-277 1.25e-25

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 103.48  E-value: 1.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437    68 FRPDSVLGEGGFGCVFKgwideksltASRPGTGLVIAVKKLN--QDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDE 145
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYK---------AKHRDTGKIVAIKKIKkeKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437   146 HRLLVYEFMPRGSLENHLfRRGLYFQPlswklrlkvalgaakglaflhsSETRVIyrdfkTSNILLdseynaklsdfGLA 225
Cdd:pfam00069  72 NLYLVLEYVEGGSLFDLL-SEKGAFSE----------------------REAKFI-----MKQILE-----------GLE 112
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15222437   226 KDgpigdkSHVSTRVmGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:pfam00069 113 SG------SSLTTFV-GTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGK 157
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
73-349 1.62e-25

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: 104.10  E-value: 1.62e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQDGWQGHQE--WLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLV 150
Cdd:cd05117   7 VLGRGSFGVVRL---------AVHKKTGEEYAVKIIDKKKLKSEDEemLRREIEILKRLDHPNIVKLYEVFEDDKNLYLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 151 YEFMPRGSLENHLFRRGLY---------FQPLSwklrlkvalgaakGLAFLHSSEtrVIYRDFKTSNILLDSEYNA---K 218
Cdd:cd05117  78 MELCTGGELFDRIVKKGSFsereaakimKQILS-------------AVAYLHSQG--IVHRDLKPENILLASKDPDspiK 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 219 LSDFGLAKDgpIGDKSHVSTRVmGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRravdknRPSGERNLVEwakpy 298
Cdd:cd05117 143 IIDFGLAKI--FEEGEKLKTVC-GTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGY------PPFYGETEQE----- 208
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15222437 299 lvnkrkIFRVIdnrLQDQYSME--------EACKvaTLSLRCLTTEIKLRPNMSEVVSH 349
Cdd:cd05117 209 ------LFEKI---LKGKYSFDspewknvsEEAK--DLIKRLLVVDPKKRLTAAEALNH 256
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
72-366 3.90e-25

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: 103.66  E-value: 3.90e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  72 SVLGEGGFGCVFKGWIdeksltasrPGTGLVIAVKKLNQDGWQG-HQEWLAEVNYLGQFSHRHLVKLIGYCLeDEHRLLV 150
Cdd:cd06621   7 SSLGEGAGGSVTKCRL---------RNTKTIFALKTITTDPNPDvQKQILRELEINKSCASPYIVKYYGAFL-DEQDSSI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 151 Y---EFMPRGSLENhlfrrgLYFQPLSWKLR------LKVALGAAKGLAFLHssETRVIYRDFKTSNILLDSEYNAKLSD 221
Cdd:cd06621  77 GiamEYCEGGSLDS------IYKKVKKKGGRigekvlGKIAESVLKGLSYLH--SRKIIHRDIKPSNILLTRKGQVKLCD 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 222 FGLAkdGPIGDKshVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAV--DKNRPSGERNLVEwakpYL 299
Cdd:cd06621 149 FGVS--GELVNS--LAGTFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFppEGEPPLGPIELLS----YI 220
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15222437 300 VNKrKIFRVIDNrlqdqysmEEACKVATLSLR-----CLTTEIKLRPNMSEVVSHLEHIQSLNAAIggNMDK 366
Cdd:cd06621 221 VNM-PNPELKDE--------PENGIKWSESFKdfiekCLEKDGTRRPGPWQMLAHPWIKAQEKKKV--NMAK 281
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
74-354 4.60e-25

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: 103.56  E-value: 4.60e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWIDeksltASRPGTGLVIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHR--LLVY 151
Cdd:cd14205  12 LGKGNFGSVEMCRYD-----PLQDNTGEVVAVKKLQHSTEEHLRDFEREIEILKSLQHDNIVKYKGVCYSAGRRnlRLIM 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 152 EFMPRGSLENHLFRRGlyfQPLSWKLRLKVALGAAKGLAFLhsSETRVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPiG 231
Cdd:cd14205  87 EYLPYGSLRDYLQKHK---ERIDHIKLLQYTSQICKGMEYL--GTKRYIHRDLATRNILVENENRVKIGDFGLTKVLP-Q 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 232 DKSHVSTRVMGTHG--YAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAvDKNRPSGERNLVEWAKPylvNKRKIFRVI 309
Cdd:cd14205 161 DKEYYKVKEPGESPifWYAPESLTESKFSVASDVWSFGVVLYELFTYIEK-SKSPPAEFMRMIGNDKQ---GQMIVFHLI 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 15222437 310 DnRLQDQYSM--EEAC--KVATLSLRCLTTEIKLRPNMSEVVSHLEHIQ 354
Cdd:cd14205 237 E-LLKNNGRLprPDGCpdEIYMIMTECWNNNVNQRPSFRDLALRVDQIR 284
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
74-350 6.35e-25

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: 102.57  E-value: 6.35e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQDGWQGhqEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEF 153
Cdd:cd14065   1 LGKGFFGEVYK---------VTHRETGKVMVMKELKRFDEQR--SFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEY 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 154 MPRGSLENHLFRRGlyfQPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILL---DSEYNAKLSDFGLAKDGPI 230
Cdd:cd14065  70 VNGGTLEELLKSMD---EQLPWSQRVSLAKDIASGMAYLHSK--NIIHRDLNSKNCLVreaNRGRNAVVADFGLAREMPD 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 231 -----GDKSHVSTrVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLsGRRAVDknrpsgernlvewakPYLVNKRKI 305
Cdd:cd14065 145 ektkkPDRKKRLT-VVGSPYWMAPEMLRGESYDEKVDVFSFGIVLCEII-GRVPAD---------------PDYLPRTMD 207
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 15222437 306 FRVIDNRLQDQYSMEEACKVATLSLRCLTTEIKLRPNMSEVVSHL 350
Cdd:cd14065 208 FGLDVRAFRTLYVPDCPPSFLPLAIRCCQLDPEKRPSFVELEHHL 252
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
74-275 8.55e-25

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: 102.50  E-value: 8.55e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGwideKSLTASRPGTGLV-IAVKKLNQDGW-QGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVY 151
Cdd:cd05044   3 LGSGAFGEVFEG----TAKDILGDGSGETkVAVKTLRKGATdQEKAEFLKEAHLMSNFKHPNILKLLGVCLDNDPQYIIL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 152 EFMPRGSLENHLfR--RGLYFQP--LSWKLRLKVALGAAKGLAFLHssETRVIYRDFKTSNILLDSEYNA----KLSDFG 223
Cdd:cd05044  79 ELMEGGDLLSYL-RaaRPTAFTPplLTLKDLLSICVDVAKGCVYLE--DMHFVHRDLAARNCLVSSKDYRervvKIGDFG 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15222437 224 LAKDGPIGD------KSHVSTRVMgthgyaAPEYLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:cd05044 156 LARDIYKNDyyrkegEGLLPVRWM------APESLVDGVFTTQSDVWAFGVLMWEILT 207
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
73-349 8.84e-25

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: 102.16  E-value: 8.84e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQDG--WQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLV 150
Cdd:cd08215   7 VIGKGSFGSAYL---------VRRKSDGKLYVLKEIDLSNmsEKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 151 YEFMPRGSLENHLFRRGLYFQPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAKDgpI 230
Cdd:cd08215  78 MEYADGGDLAQKIKKQKKKGQPFPEEQILDWFVQICLALKYLHSR--KILHRDLKTQNIFLTKDGVVKLGDFGISKV--L 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 231 GDKSHVSTRVMGTHGYAAPE------YlatghlTTKSDVYSFGVVLLELLSGRRAVD-KNRPSgernlvewakpyLVNkr 303
Cdd:cd08215 154 ESTTDLAKTVVGTPYYLSPElcenkpY------NYKSDIWALGCVLYELCTLKHPFEaNNLPA------------LVY-- 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 15222437 304 KIFRVIDNRLQDQYSMEeackVATLSLRCLTTEIKLRPNMSEVVSH 349
Cdd:cd08215 214 KIVKGQYPPIPSQYSSE----LRDLVNSMLQKDPEKRPSANEILSS 255
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
74-350 8.88e-25

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR1 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR1 results in a slow but sustained receptor activation. DDR1 binds to all collagens tested to date (types I-IV). It is widely expressed in many tissues. It is abundant in the brain and is also found in keratinocytes, colonic mucosa epithelium, lung epithelium, thyroid follicles, and the islets of Langerhans. During embryonic development, it is found in the developing neuroectoderm. DDR1 is a key regulator of cell morphogenesis, differentiation and proliferation. It is important in the development of the mammary gland, the vasculator and the kidney. DDR1 is also found in human leukocytes, where it facilitates cell adhesion, migration, maturation, and cytokine production. The DDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133227 [Multi-domain]  Cd Length: 304  Bit Score: 103.09  E-value: 8.88e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWIDEKSLTAS-------RPGTGLVIAVKKLNQDGWQ-GHQEWLAEVNYLGQFSHRHLVKLIGYCLEDE 145
Cdd:cd05096  13 LGEGQFGEVHLCEVVNPQDLPTlqfpfnvRKGRPLLVAVKILRPDANKnARNDFLKEVKILSRLKDPNIIRLLGVCVDED 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 146 HRLLVYEFMPRGSLENHLFRRGLY---------------FQPLSWKLRLKVALGAAKGLAFLhsSETRVIYRDFKTSNIL 210
Cdd:cd05096  93 PLCMITEYMENGDLNQFLSSHHLDdkeengndavppahcLPAISYSSLLHVALQIASGMKYL--SSLNFVHRDLATRNCL 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 211 LDSEYNAKLSDFGLAKDGPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSgrraVDKNRPSGE-- 288
Cdd:cd05096 171 VGENLTIKIADFGMSRNLYAGDYYRIQGRAVLPIRWMAWECILMGKFTTASDVWAFGVTLWEILM----LCKEQPYGElt 246
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15222437 289 -RNLVEwakpylvNKRKIFRviDNRLQDQYSMEEACK--VATLSLRCLTTEIKLRPNMSEVVSHL 350
Cdd:cd05096 247 dEQVIE-------NAGEFFR--DQGRQVYLFRPPPCPqgLYELMLQCWSRDCRERPSFSDIHAFL 302
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
74-355 9.69e-25

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


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 101.78  E-value: 9.69e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKgwideksltASRPGTGLVIAVK--KLNQDgwqgHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVY 151
Cdd:cd14155   1 IGSGFFSEVYK---------VRHRTSGQVMALKmnTLSSN----RANMLREVQLMNRLSHPNILRFMGVCVHQGQLHALT 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 152 EFMPRGSLENHLFRRglyfQPLSWKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSE---YNAKLSDFGLAKDG 228
Cdd:cd14155  68 EYINGGNLEQLLDSN----EPLSWTVRVKLALDIARGLSYLHSKG--IFHRDLTSKNCLIKRDengYTAVVGDFGLAEKI 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 229 PIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVDKNRPSGERNLVEWAKpylvnkrkiFRv 308
Cdd:cd14155 142 PDYSDGKEKLAVVGSPYWMAPEVLRGEPYNEKADVFSYGIILCEIIARIQADPDYLPRTEDFGLDYDA---------FQ- 211
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 15222437 309 idnrlqdqySMEEACKVATLSL--RCLTTEIKLRPNMSEVVSHLEHIQS 355
Cdd:cd14155 212 ---------HMVGDCPPDFLQLafNCCNMDPKSRPSFHDIVKTLEEILE 251
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
68-275 1.32e-24

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: 101.74  E-value: 1.32e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  68 FRPDSVLGEGGFGCVFKG-WIDeksltaSRPgtglvIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEH 146
Cdd:cd05148   8 FTLERKLGSGYFGEVWEGlWKN------RVR-----VAIKILKSDDLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGEP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 147 RLLVYEFMPRGSLenHLFRRGLYFQPLSWKLRLKVALGAAKGLAFLHssETRVIYRDFKTSNILLDSEYNAKLSDFGLAK 226
Cdd:cd05148  77 VYIITELMEKGSL--LAFLRSPEGQVLPVASLIDMACQVAEGMAYLE--EQNSIHRDLAARNILVGEDLVCKVADFGLAR 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15222437 227 dgPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:cd05148 153 --LIKEDVYLSSDKKIPYKWTAPEAASHGTFSTKSDVWSFGILLYEMFT 199
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
73-346 5.02e-24

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


Pssm-ID: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 100.87  E-value: 5.02e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCV-------FKGWIDEKSLTASRPGTGLVIAVKKLNQDG-WQGHQEWLAEVNYLGQFSHRHLVKLIGYCLED 144
Cdd:cd05051  12 KLGEGQFGEVhlceangLSDLTSDDFIGNDNKDEPVLVAVKMLRPDAsKNAREDFLKEVKIMSQLKDPNIVRLLGVCTRD 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 145 EHRLLVYEFMPRGSLENHLFRR--------GLYFQPLSWKLRLKVALGAAKGLAFLhsSETRVIYRDFKTSNILLDSEYN 216
Cdd:cd05051  92 EPLCMIVEYMENGDLNQFLQKHeaetqgasATNSKTLSYGTLLYMATQIASGMKYL--ESLNFVHRDLATRNCLVGPNYT 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 217 AKLSDFGLAKDGPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLS-GRRavdknrpsgernlvewa 295
Cdd:cd05051 170 IKIADFGMSRNLYSGDYYRIEGRAVLPIRWMAWESILLGKFTTKSDVWAFGVTLWEILTlCKE----------------- 232
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15222437 296 KPYlvNKRKIFRVIDN--RLQDQYSMEE------AC--KVATLSLRCLTTEIKLRPNMSEV 346
Cdd:cd05051 233 QPY--EHLTDEQVIENagEFFRDDGMEVylsrppNCpkEIYELMLECWRRDEEDRPTFREI 291
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
74-356 6.20e-24

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: 99.88  E-value: 6.20e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKgwideksLTASRPGTGLVIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCleDEHRLLVYEF 153
Cdd:cd14025   4 VGSGGFGQVYK-------VRHKHWKTWLAIKCPPSLHVDDSERMELLEEAKKMEMAKFRHILPVYGIC--SEPVGLVMEY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 154 MPRGSLENHLFRrglyfQPLSWKLRLKVALGAAKGLAFLHSSETRVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPIGDK 233
Cdd:cd14025  75 METGSLEKLLAS-----EPLPWELRFRIIHETAVGMNFLHCMKPPLLHLDLKPANILLDAHYHVKISDFGLAKWNGLSHS 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 234 SHVSTRVM-GTHGYAAPEYLATGH--LTTKSDVYSFGVVLLELLSGRRAVdknrpSGERNLVEWAKPYLVNKRKIFRVI- 309
Cdd:cd14025 150 HDLSRDGLrGTIAYLPPERFKEKNrcPDTKHDVYSFAIVIWGILTQKKPF-----AGENNILHIMVKVVKGHRPSLSPIp 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 15222437 310 DNRLQdqysmeEACKVATLSLRCLTTEIKLRPNMSEVVSHLEHIQSL 356
Cdd:cd14025 225 RQRPS------ECQQMICLMKRCWDQDPRKRPTFQDITSETENLLSL 265
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
73-275 7.55e-24

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


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 100.23  E-value: 7.55e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKGwideKSLTASRPGTGLVIAVKKLnQDGW--QGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLV 150
Cdd:cd05049  12 ELGEGAFGKVFLG----ECYNLEPEQDKMLVAVKTL-KDASspDARKDFEREAELLTNLQHENIVKFYGVCTEGDPLLMV 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 151 YEFMPRGSLENHLFRRG----LYFQPLSWKLRL------KVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLS 220
Cdd:cd05049  87 FEYMEHGDLNKFLRSHGpdaaFLASEDSAPGELtlsqllHIAVQIASGMVYLASQ--HFVHRDLATRNCLVGTNLVVKIG 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15222437 221 DFGLAKDGPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:cd05049 165 DFGMSRDIYSTDYYRVGGHTMLPIRWMPPESILYRKFTTESDVWSFGVVLWEIFT 219
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
74-289 7.94e-24

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: 99.34  E-value: 7.94e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKG-WIDEKsltasrpGTGLVIAVKKLNQDGWQGH---QEWLAEVNYLGQFSHRHLVKLIGYCLeDEHRLL 149
Cdd:cd05040   3 LGDGSFGVVRRGeWTTPS-------GKVIQVAVKCLKSDVLSQPnamDDFLKEVNAMHSLDHPNLIRLYGVVL-SSPLMM 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 150 VYEFMPRGSLENHLFRRGLYFqPLSwklRL-KVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAKDG 228
Cdd:cd05040  75 VTELAPLGSLLDRLRKDQGHF-LIS---TLcDYAVQIANGMAYLESK--RFIHRDLAARNILLASKDKVKIGDFGLMRAL 148
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15222437 229 PIGDKSHvstrVMGTH-----GYAAPEYLATGHLTTKSDVYSFGVVLLEL----------LSGR---RAVDKNrpsGER 289
Cdd:cd05040 149 PQNEDHY----VMQEHrkvpfAWCAPESLKTRKFSHASDVWMFGVTLWEMftygeepwlgLNGSqilEKIDKE---GER 220
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
73-346 8.26e-24

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: 99.77  E-value: 8.26e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKGwideksltASRpgtGLVIAVKKLN--QDGWQGHQEWLAEVNYLgQFSHRHLVKLIGY---CLEDEHR 147
Cdd:cd13979  10 PLGSGGFGSVYKA--------TYK---GETVAVKIVRrrRKNRASRQSFWAELNAA-RLRHENIVRVLAAetgTDFASLG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 148 LLVYEFMPRGSLENHLFRRglyFQPLSWKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLA-K 226
Cdd:cd13979  78 LIIMEYCGNGTLQQLIYEG---SEPLPLAHRILISLDIARALRFCHSHG--IVHLDVKPANILISEQGVCKLCDFGCSvK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 227 DGPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRravdknRP-SGERNLVewakPYLVNKRKI 305
Cdd:cd13979 153 LGEGNEVGTPRSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRE------LPyAGLRQHV----LYAVVAKDL 222
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 15222437 306 fRVIDNRLQDQysmEEACKVATLSLRCLTTEIKLRPNMSEV 346
Cdd:cd13979 223 -RPDLSGLEDS---EFGQRLRSLISRCWSAQPAERPNADES 259
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
74-277 8.88e-24

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: 99.99  E-value: 8.88e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQDGWQGHQE---WLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLV 150
Cdd:cd14026   5 LSRGAFGTVSR---------ARHADWRVTVAIKCLKLDSPVGDSErncLLKEAEILHKARFSYILPILGICNEPEFLGIV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 151 YEFMPRGSLENHLFRRGLYfQPLSWKLRLKVALGAAKGLAFLHSSETRVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPI 230
Cdd:cd14026  76 TEYMTNGSLNELLHEKDIY-PDVAWPLRLRILYEIALGVNYLHNMSPPLLHHDLKTQNILLDGEFHVKIADFGLSKWRQL 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15222437 231 G---DKSHVSTRVMGTHGYAAPEYLATGHLT---TKSDVYSFGVVLLELLSGR 277
Cdd:cd14026 155 SisqSRSSKSAPEGGTIIYMPPEEYEPSQKRrasVKHDIYSYAIIMWEVLSRK 207
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
66-277 9.70e-24

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


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 99.22  E-value: 9.70e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  66 RNFRPDSVLGEGGFGCVFKGwIDEKsltasrpgTGLVIA--VKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLE 143
Cdd:cd13983   1 RYLKFNEVLGRGSFKTVYRA-FDTE--------EGIEVAwnEIKLRKLPKAERQRFKQEIEILKSLKHPNIIKFYDSWES 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 144 DEHRLLVY--EFMPRGSLENHLFRrglyFQPLSWKLRLKVALGAAKGLAFLHSSETRVIYRDFKTSNILLDSEYNA-KLS 220
Cdd:cd13983  72 KSKKEVIFitELMTSGTLKQYLKR----FKRLKLKVIKSWCRQILEGLNYLHTRDPPIIHRDLKCDNIFINGNTGEvKIG 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15222437 221 DFGLAKdgpIGDKSHVSTrVMGTHGYAAPEyLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd13983 148 DLGLAT---LLRQSFAKS-VIGTPEFMAPE-MYEEHYDEKVDIYAFGMCLLEMATGE 199
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
67-351 1.01e-23

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: 99.46  E-value: 1.01e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGCVFKGWIDEKSLTasrpGTGLVIAVKKLNQ-DGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDE 145
Cdd:cd05046   6 NLQEITTLGRGEFGEVFLAKAKGIEEE----GGETLVLVKALQKtKDENLQSEFRRELDMFRKLSHKNVVRLLGLCREAE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 146 HRLLVYEFMPRGSLENHLF-----RRGLYFQPLSWKLRLKVALGAAKGLAflHSSETRVIYRDFKTSNILLDSEYNAKLS 220
Cdd:cd05046  82 PHYMILEYTDLGDLKQFLRatkskDEKLKPPPLSTKQKVALCTQIALGMD--HLSNARFVHRDLAARNCLVSSQREVKVS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 221 DFGLAKDgPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSgrravdknrpSGERNLVEWAKPYLV 300
Cdd:cd05046 160 LLSLSKD-VYNSEYYKLRNALIPLRWLAPEAVQEDDFSTKSDVWSFGVLMWEVFT----------QGELPFYGLSDEEVL 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 15222437 301 NKRKIFRVidnrlqdQYSMEEAC--KVATLSLRCLTTEIKLRPNMSEVVSHLE 351
Cdd:cd05046 229 NRLQAGKL-------ELPVPEGCpsRLYKLMTRCWAVNPKDRPSFSELVSALG 274
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
73-273 1.12e-23

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: 99.37  E-value: 1.12e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFK--GWIDeksltasrpgtGLVIAVKKLNQDGWQGH-QEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLL 149
Cdd:cd14046  13 VLGKGAFGQVVKvrNKLD-----------GRYYAIKKIKLRSESKNnSRILREVMLLSRLNHQHVVRYYQAWIERANLYI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 150 VYEFMPRGSLEnHLFRRGLYFQP-LSWKLRLKVAlgaaKGLAFLHSSETrvIYRDFKTSNILLDSEYNAKLSDFGLAKD- 227
Cdd:cd14046  82 QMEYCEKSTLR-DLIDSGLFQDTdRLWRLFRQIL----EGLAYIHSQGI--IHRDLKPVNIFLDSNGNVKIGDFGLATSn 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15222437 228 --------GPIGDKSHV-------STRVMGTHGYAAPEYL--ATGHLTTKSDVYSFGVVLLEL 273
Cdd:cd14046 155 klnvelatQDINKSTSAalgssgdLTGNVGTALYVAPEVQsgTKSTYNEKVDMYSLGIIFFEM 217
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
73-353 1.22e-23

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: 99.53  E-value: 1.22e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKGWIDEKSltasrpGTGLVIAVKKLNQDG--WQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHR--- 147
Cdd:cd05035   6 ILGEGEFGSVMEAQLKQDD------GSQLKVAVKTMKVDIhtYSEIEEFLSEAACMKDFDHPNVMRLIGVCFTASDLnkp 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 148 ---LLVYEFMPRGSLENHLFRRGLYFQPLSWKLR--LKVALGAAKGLAFLhsSETRVIYRDFKTSNILLDSEYNAKLSDF 222
Cdd:cd05035  80 pspMVILPFMKHGDLHSYLLYSRLGGLPEKLPLQtlLKFMVDIAKGMEYL--SNRNFIHRDLAARNCMLDENMTVCVADF 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 223 GLAKDGPIGD---KSHVSTRVMgthGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAvdknrpsgernlvewakPYL 299
Cdd:cd05035 158 GLSRKIYSGDyyrQGRISKMPV---KWIALESLADNVYTSKSDVWSFGVTMWEIATRGQT-----------------PYP 217
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15222437 300 -VNKRKIFRVI--DNRL-QDQYSMEEackVATLSLRCLTTEIKLRPNMSEVVSHLEHI 353
Cdd:cd05035 218 gVENHEIYDYLrnGNRLkQPEDCLDE---VYFLMYFCWTVDPKDRPTFTKLREVLENI 272
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
66-275 1.58e-23

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: 99.20  E-value: 1.58e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  66 RNFRPDSVLGEGGFGCVfkgwidekSLTASRP---GTGLVIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCL 142
Cdd:cd05081   4 RHLKYISQLGKGNFGSV--------ELCRYDPlgdNTGALVAVKQLQHSGPDQQRDFQREIQILKALHSDFIVKYRGVSY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 143 EDEHR--LLVYEFMPRGSLENHLFRRGLYFQPLSWKLrlkVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLS 220
Cdd:cd05081  76 GPGRRslRLVMEYLPSGCLRDFLQRHRARLDASRLLL---YSSQICKGMEYLGSR--RCVHRDLAARNILVESEAHVKIA 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15222437 221 DFGLAKDGPIgDKSHVSTRVMGTHG--YAAPEYLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:cd05081 151 DFGLAKLLPL-DKDYYVVREPGQSPifWYAPESLSDNIFSRQSDVWSFGVVLYELFT 206
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
74-275 1.64e-23

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: 99.14  E-value: 1.64e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGwiDEKSLTASRPGTglVIAVKKLNQDG-WQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYE 152
Cdd:cd05050  13 IGQGAFGRVFQA--RAPGLLPYEPFT--MVAVKMLKEEAsADMQADFQREAALMAEFDHPNIVKLLGVCAVGKPMCLLFE 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMPRGSLENHLFRRGLYFQ------------------PLSWKLRLKVALGAAKGLAFLhsSETRVIYRDFKTSNILLDSE 214
Cdd:cd05050  89 YMAYGDLNEFLRHRSPRAQcslshstssarkcglnplPLSCTEQLCIAKQVAAGMAYL--SERKFVHRDLATRNCLVGEN 166
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15222437 215 YNAKLSDFGLAKDGPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:cd05050 167 MVVKIADFGLSRNIYSADYYKASENDAIPIRWMPPESIFYNRYTTESDVWAYGVVLWEIFS 227
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
73-275 1.69e-23

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: 98.54  E-value: 1.69e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKGWIDEKSltasrpgtglVIAVKKLNQDGWQGHQ-EWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVY 151
Cdd:cd05085   3 LLGKGNFGEVYKGTLKDKT----------PVAVKTCKEDLPQELKiKFLSEARILKQYDHPNIVKLIGVCTQRQPIYIVM 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 152 EFMPRGSLENHLFRRGlyfQPLSWKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPIG 231
Cdd:cd05085  73 ELVPGGDFLSFLRKKK---DELKTKQLVKFSLDAAAGMAYLESKN--CIHRDLAARNCLVGENNALKISDFGMSRQEDDG 147
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 15222437 232 DKSHVSTRVMGTHgYAAPEYLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:cd05085 148 VYSSSGLKQIPIK-WTAPEALNYGRYSSESDVWSFGILLWETFS 190
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
73-277 5.47e-23

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: 97.51  E-value: 5.47e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKGwideksLTAsrpgTGLVIAVKK--LNQDGW----QGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEH 146
Cdd:cd06631   8 VLGKGAYGTVYCG------LTS----TGQLIAVKQveLDTSDKekaeKEYEKLQEEVDLLKTLKHVNIVGYLGTCLEDNV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 147 RLLVYEFMPRGSLENHLFRrglyFQPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAK 226
Cdd:cd06631  78 VSIFMEFVPGGSIASILAR----FGALEEPVFCRYTKQILEGVAYLHNN--NVIHRDIKGNNIMLMPNGVIKLIDFGCAK 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15222437 227 ----DGPIGDKSHVSTRVMGTHGYAAPEYLA-TGHlTTKSDVYSFGVVLLELLSGR 277
Cdd:cd06631 152 rlciNLSSGSQSQLLKSMRGTPYWMAPEVINeTGH-GRKSDIWSIGCTVFEMATGK 206
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
74-275 6.47e-23

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: 97.46  E-value: 6.47e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGwideksLTASRPG--TGLVIAVKKLNQD-GWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLV 150
Cdd:cd05036  14 LGQGAFGEVYEG------TVSGMPGdpSPLQVAVKTLPELcSEQDEMDFLMEALIMSKFNHPNIVRCIGVCFQRLPRFIL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 151 YEFMPRGSLENHLFR-RGLYFQPLSWKLR--LKVALGAAKGLAFLhsSETRVIYRDFKTSNILL---DSEYNAKLSDFGL 224
Cdd:cd05036  88 LELMAGGDLKSFLREnRPRPEQPSSLTMLdlLQLAQDVAKGCRYL--EENHFIHRDIAARNCLLtckGPGRVAKIGDFGM 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15222437 225 AKDGPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:cd05036 166 ARDIYRADYYRKGGKAMLPVKWMPPEAFLDGIFTSKTDVWSFGVLLWEIFS 216
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
73-281 1.09e-22

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: 96.21  E-value: 1.09e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKG-WIDEK-SLTASR--PGTGLVIAVKKLNQdgwqghqewlaEVNYLGQFSHRHLVKLIGYCLEDEHRL 148
Cdd:cd14148   1 IIGVGGFGKVYKGlWRGEEvAVKAARqdPDEDIAVTAENVRQ-----------EARLFWMLQHPNIIALRGVCLNPPHLC 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 LVYEFMPRGSLEnhlfrRGLYFQPLSWKLRLKVALGAAKGLAFLHSSE-TRVIYRDFKTSNILLD--------SEYNAKL 219
Cdd:cd14148  70 LVMEYARGGALN-----RALAGKKVPPHVLVNWAVQIARGMNYLHNEAiVPIIHRDLKSSNILILepienddlSGKTLKI 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15222437 220 SDFGLAKDGpigdksHVSTRV--MGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR---RAVD 281
Cdd:cd14148 145 TDFGLAREW------HKTTKMsaAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEvpyREID 205
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
74-275 1.22e-22

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: 96.57  E-value: 1.22e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWIDEKSLTASRpgtgLVIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEF 153
Cdd:cd05092  13 LGEGAFGKVFLAECHNLLPEQDK----MLVAVKALKEATESARQDFQREAELLTVLQHQHIVRFYGVCTEGEPLIMVFEY 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 154 MPRGSLeNHLFR------------RGLYFQPLSWKLRLKVALGAAKGLAFLHSseTRVIYRDFKTSNILLDSEYNAKLSD 221
Cdd:cd05092  89 MRHGDL-NRFLRshgpdakildggEGQAPGQLTLGQMLQIASQIASGMVYLAS--LHFVHRDLATRNCLVGQGLVVKIGD 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15222437 222 FGLAKDGPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:cd05092 166 FGMSRDIYSTDYYRVGGRTMLPIRWMPPESILYRKFTTESDIWSFGVVLWEIFT 219
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
74-276 1.36e-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: 95.64  E-value: 1.36e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWI-DEKsltasrpgtglvIAVKKLNQdgwqghqEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYE 152
Cdd:cd14059   1 LGSGAQGAVFLGKFrGEE------------VAVKKVRD-------EKETDIKHLRKLNHPNIIKFKGVCTQAPCYCILME 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMPRGSLENhLFRRGlyfQPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAKDgpIGD 232
Cdd:cd14059  62 YCPYGQLYE-VLRAG---REITPSLLVDWSKQIASGMNYLHLH--KIIHRDLKSPNVLVTYNDVLKISDFGTSKE--LSE 133
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 15222437 233 KShVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14059 134 KS-TKMSFAGTVAWMAPEVIRNEPCSEKVDIWSFGVVLWELLTG 176
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
65-275 1.39e-22

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: 96.56  E-value: 1.39e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  65 TRNFRPDSVLGEGGFGCVFKG-WIDEksltasrpGTGLVIAVK-KLNQDgWQGHQEWLAEVNYL---GQFSHRHLVKLIG 139
Cdd:cd05111   6 ETELRKLKVLGSGVFGTVHKGiWIPE--------GDSIKIPVAiKVIQD-RSGRQSFQAVTDHMlaiGSLDHAYIVRLLG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 140 YCLEDEHRLlVYEFMPRGSLENHLFRRGLYFQP---LSWKLRLkvalgaAKGLAFLHssETRVIYRDFKTSNILLDSEYN 216
Cdd:cd05111  77 ICPGASLQL-VTQLLPLGSLLDHVRQHRGSLGPqllLNWCVQI------AKGMYYLE--EHRMVHRNLAARNVLLKSPSQ 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15222437 217 AKLSDFGLAKDGPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:cd05111 148 VQVADFGVADLLYPDDKKYFYSEAKTPIKWMALESIHFGKYTHQSDVWSYGVTVWEMMT 206
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
68-277 1.54e-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: 96.48  E-value: 1.54e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  68 FRPDSVLGEGGFGCVFKgwideksltASRPGTGLVIAVKKLnqDGWQGHQEW----LAEVNYLGQFSHRHLVKLIGYCLE 143
Cdd:cd07840   1 YEKIAQIGEGTYGQVYK---------ARNKKTGELVALKKI--RMENEKEGFpitaIREIKLLQKLDHPNVVRLKEIVTS 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 144 DEHRL------LVYEFMPR---GSLENHLFRRGL-----YFQPLswklrlkvalgaAKGLAFLHSSetRVIYRDFKTSNI 209
Cdd:cd07840  70 KGSAKykgsiyMVFEYMDHdltGLLDNPEVKFTEsqikcYMKQL------------LEGLQYLHSN--GILHRDIKGSNI 135
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15222437 210 LLDSEYNAKLSDFGLAKdgPI-GDKSHVSTRVMGTHGYAAPEYL--ATgHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd07840 136 LINNDGVLKLADFGLAR--PYtKENNADYTNRVITLWYRPPELLlgAT-RYGPEVDMWSVGCILAELFTGK 203
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
44-351 1.58e-22

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 100.31  E-value: 1.58e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437   44 EGEILQSPNLKSFSFAELKSATRNfrpDSVLGEGGFGCVFKGwideKSLTasrpgTGLVIAVKKLNQDgwqgHQEWLAEV 123
Cdd:PLN00113 671 ELQFFDSKVSKSITINDILSSLKE---ENVISRGKKGASYKG----KSIK-----NGMQFVVKEINDV----NSIPSSEI 734
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  124 NYLGQFSHRHLVKLIGYCLEDEHRLLVYEFMPRGSLENHLfrRGLyfqplSWKLRLKVALGAAKGLAFLHSS-ETRVIYR 202
Cdd:PLN00113 735 ADMGKLQHPNIVKLIGLCRSEKGAYLIHEYIEGKNLSEVL--RNL-----SWERRRKIAIGIAKALRFLHCRcSPAVVVG 807
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  203 DFKTSNILLDSEYNAKLSdfgLAKDGPIGdkshVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVDK 282
Cdd:PLN00113 808 NLSPEKIIIDGKDEPHLR---LSLPGLLC----TDTKCFISSAYVAPETRETKDITEKSDIYGFGLILIELLTGKSPADA 880
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15222437  283 NRpSGERNLVEWAKpYLVNKRKIFRVIDNRLQDQYSM--EEACKVATLSLRCLTTEIKLRPNMSEVVSHLE 351
Cdd:PLN00113 881 EF-GVHGSIVEWAR-YCYSDCHLDMWIDPSIRGDVSVnqNEIVEVMNLALHCTATDPTARPCANDVLKTLE 949
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
74-277 2.66e-22

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: 95.16  E-value: 2.66e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWIDEksltasrpgTGLVIAVKKLN-----QDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEhRL 148
Cdd:cd06632   8 LGSGSFGSVYEGFNGD---------TGDFFAVKEVSlvdddKKSRESVKQLEQEIALLSKLRHPNIVQYYGTEREED-NL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 LVY-EFMPRGSLENHLFRRGLYFQPLSwKLRLKVALgaaKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAKd 227
Cdd:cd06632  78 YIFlEYVPGGSIHKLLQRYGAFEEPVI-RLYTRQIL---SGLAYLHSR--NTVHRDIKGANILVDTNGVVKLADFGMAK- 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15222437 228 gpigdksHVSTRVM-----GTHGYAAPEYLATGHLTTKS--DVYSFGVVLLELLSGR 277
Cdd:cd06632 151 -------HVEAFSFaksfkGSPYWMAPEVIMQKNSGYGLavDIWSLGCTVLEMATGK 200
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
74-277 3.04e-22

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: 94.85  E-value: 3.04e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKgwIDEKSltasrpgTGLVIAVKKLN----QDGWQGHQewLA-EVNYLGQFSHRHLVKLIGYcLEDEHRL 148
Cdd:cd14007   8 LGKGKFGNVYL--AREKK-------SGFIVALKVISksqlQKSGLEHQ--LRrEIEIQSHLRHPNILRLYGY-FEDKKRI 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 -LVYEFMPRGSLENHLFRRG--------LYFQPLswklrlkvalgaAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKL 219
Cdd:cd14007  76 yLILEYAPNGELYKELKKQKrfdekeaaKYIYQL------------ALALDYLHSK--NIIHRDIKPENILLGSNGELKL 141
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15222437 220 SDFGLAKDGPigdkSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd14007 142 ADFGWSVHAP----SNRRKTFCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGK 195
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
74-349 3.33e-22

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: 94.93  E-value: 3.33e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQDGWQGH---QEWLAEVNYLGQFSHRHLVKLIGyCLEDEHRL-L 149
Cdd:cd14099   9 LGKGGFAKCYE---------VTDMSTGKVYAGKVVPKSSLTKPkqrEKLKSEIKIHRSLKHPNIVKFHD-CFEDEENVyI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 150 VYEFMPRGSLENHLFRRGLYFQPlswklrlKVA---LGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLA- 225
Cdd:cd14099  79 LLELCSNGSLMELLKRRKALTEP-------EVRyfmRQILSGVKYLHSN--RIIHRDLKLGNLFLDENMNVKIGDFGLAa 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 226 KDGPIGDKshvSTRVMGTHGYAAPEYLA--TGHlTTKSDVYSFGVVLLELLSGrravdknRPsgernlvewakPYLVNKR 303
Cdd:cd14099 150 RLEYDGER---KKTLCGTPNYIAPEVLEkkKGH-SFEVDIWSLGVILYTLLVG-------KP-----------PFETSDV 207
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 15222437 304 K-IFRVIDNRlqdQYSMEEACKVAT----LSLRCLTTEIKLRPNMSEVVSH 349
Cdd:cd14099 208 KeTYKRIKKN---EYSFPSHLSISDeakdLIRSMLQPDPTKRPSLDEILSH 255
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
72-277 3.74e-22

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: 94.97  E-value: 3.74e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  72 SVLGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQDGWQGHQEWLA-EVNYLGQFSHRHLVKLIGYCLEDEHRLLV 150
Cdd:cd06623   7 KVLGQGSSGVVYK---------VRHKPTGKIYALKKIHVDGDEEFRKQLLrELKTLRSCESPYVVKCYGAFYKEGEISIV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 151 YEFMPRGSLENHLFRRGLYFQP-LSwklrlKVALGAAKGLAFLHSsETRVIYRDFKTSNILLDSEYNAKLSDFGLAKD-G 228
Cdd:cd06623  78 LEYMDGGSLADLLKKVGKIPEPvLA-----YIARQILKGLDYLHT-KRHIIHRDIKPSNLLINSKGEVKIADFGISKVlE 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15222437 229 PIGDKSHvsTRVmGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd06623 152 NTLDQCN--TFV-GTVTYMSPERIQGESYSYAADIWSLGLTLLECALGK 197
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
74-277 3.87e-22

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: 94.66  E-value: 3.87e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKG-WideksltasrPGTGLViAVKKLNQdGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYE 152
Cdd:cd05034   3 LGAGQFGEVWMGvW----------NGTTKV-AVKTLKP-GTMSPEAFLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMPRGSLENHLFR---RGLYFQPLswklrLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLA---K 226
Cdd:cd05034  71 LMSKGSLLDYLRTgegRALRLPQL-----IDMAAQIASGMAYLESR--NYIHRDLAARNILVGENNVCKVADFGLArliE 143
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15222437 227 DGPIGDKSHVSTRVMGThgyaAPEYLATGHLTTKSDVYSFGVVLLELLS-GR 277
Cdd:cd05034 144 DDEYTAREGAKFPIKWT----APEAALYGRFTIKSDVWSFGILLYEIVTyGR 191
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
73-281 4.63e-22

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: 94.72  E-value: 4.63e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKG-W-IDEKSLTASR--PGTGLVIAVKKLNQdgwqghqewlaEVNYLGQFSHRHLVKLIGYCLEDEHRL 148
Cdd:cd14146   1 IIGVGGFGKVYRAtWkGQEVAVKAARqdPDEDIKATAESVRQ-----------EAKLFSMLRHPNIIKLEGVCLEEPNLC 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 LVYEFMPRGSLENHL--------FRRGLYFQP---LSWKLRLkvalgaAKGLAFLHSSE-TRVIYRDFKTSNILL----- 211
Cdd:cd14146  70 LVMEFARGGTLNRALaaanaapgPRRARRIPPhilVNWAVQI------ARGMLYLHEEAvVPILHRDLKSSNILLlekie 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15222437 212 -DSEYNA--KLSDFGLAKDGpigdksHVSTRV--MGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR---RAVD 281
Cdd:cd14146 144 hDDICNKtlKITDFGLAREW------HRTTKMsaAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEvpyRGID 215
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
99-353 5.17e-22

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: 94.51  E-value: 5.17e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  99 TGLVIAVKKLNQDGWQghQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEFMPRGSLENHLFRRGLyfqPLSWKLR 178
Cdd:cd14156  17 TGKVMVVKIYKNDVDQ--HKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCLEELLAREEL---PLSWREK 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 179 LKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYN---AKLSDFGLAK---DGPIGDKSHvSTRVMGTHGYAAPEYL 252
Cdd:cd14156  92 VELACDISRGMVYLHSKN--IYHRDLNSKNCLIRVTPRgreAVVTDFGLARevgEMPANDPER-KLSLVGSAFWMAPEML 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 253 ATGHLTTKSDVYSFGVVLLELLsGRRAVDknrpsgernlvewakPYLVNKRKIFRVidnrlqDQYSMEEAC-----KVAT 327
Cdd:cd14156 169 RGEPYDRKVDVFSFGIVLCEIL-ARIPAD---------------PEVLPRTGDFGL------DVQAFKEMVpgcpePFLD 226
                       250       260
                ....*....|....*....|....*.
gi 15222437 328 LSLRCLTTEIKLRPNMSEVVSHLEHI 353
Cdd:cd14156 227 LAASCCRMDAFKRPSFAELLDELEDI 252
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
67-349 6.55e-22

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: 94.00  E-value: 6.55e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQdGWQGHQE---WLAEVNYLGQFSHRHLvklIGY--C 141
Cdd:cd08530   1 DFKVLKKLGKGSYGSVYK---------VKRLSDNQVYALKEVNL-GSLSQKEredSVNEIRLLASVNHPNI---IRYkeA 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 142 LEDEHRL-LVYEFMPRGSLENHLFRRGLYFQPLSWKLRLKVALGAAKGLAFLHssETRVIYRDFKTSNILLDSEYNAKLS 220
Cdd:cd08530  68 FLDGNRLcIVMEYAPFGDLSKLISKRKKKRRLFPEDDIWRIFIQMLRGLKALH--DQKILHRDLKSANILLSAGDLVKIG 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 221 DFGLAKDGpigdKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRravdknRPSGERNLVEWAkpylv 300
Cdd:cd08530 146 DLGISKVL----KKNLAKTQIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFR------PPFEARTMQELR----- 210
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 15222437 301 nkRKIFRVIDNRLQDQYS--MEEACKvatlslRCLTTEIKLRPNMSEVVSH 349
Cdd:cd08530 211 --YKVCRGKFPPIPPVYSqdLQQIIR------SLLQVNPKKRPSCDKLLQS 253
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
74-281 6.67e-22

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: 94.50  E-value: 6.67e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEF 153
Cdd:cd14154   1 LGKGFFGQAIK---------VTHRETGEVMVMKELIRFDEEAQRNFLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEY 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 154 MPRGSLENHLFRRGlyfQPLSWKLRLKVALGAAKGLAFLHSseTRVIYRDFKTSNILLDSEYNAKLSDFGLAK------- 226
Cdd:cd14154  72 IPGGTLKDVLKDMA---RPLPWAQRVRFAKDIASGMAYLHS--MNIIHRDLNSHNCLVREDKTVVVADFGLARliveerl 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15222437 227 ----DGPIGDKSHVSTR-------VMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLsGRRAVD 281
Cdd:cd14154 147 psgnMSPSETLRHLKSPdrkkrytVVGNPYWMAPEMLNGRSYDEKVDIFSFGIVLCEII-GRVEAD 211
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
74-346 7.12e-22

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


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 95.04  E-value: 7.12e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFG----CVFKGWIDEKSLTASR-PGTGLVIAVKKLNQDGWQ-GHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHR 147
Cdd:cd05097  13 LGEGQFGevhlCEAEGLAEFLGEGAPEfDGQPVLVAVKMLRADVTKtARNDFLKEIKIMSRLKNPNIIRLLGVCVSDDPL 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 148 LLVYEFMPRGSLENHLFRRGLYFQ--------PLSWKLRLKVALGAAKGLAFLHSseTRVIYRDFKTSNILLDSEYNAKL 219
Cdd:cd05097  93 CMITEYMENGDLNQFLSQREIESTfthannipSVSIANLLYMAVQIASGMKYLAS--LNFVHRDLATRNCLVGNHYTIKI 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 220 SDFGLAKDGPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSgrraVDKNRPSG---ERNLVEwak 296
Cdd:cd05097 171 ADFGMSRNLYSGDYYRIQGRAVLPIRWMAWESILLGKFTTASDVWAFGVTLWEMFT----LCKEQPYSllsDEQVIE--- 243
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 15222437 297 pylvNKRKIFRviDNRLQDQYSMEEAC--KVATLSLRCLTTEIKLRPNMSEV 346
Cdd:cd05097 244 ----NTGEFFR--NQGRQIYLSQTPLCpsPVFKLMMRCWSRDIKDRPTFNKI 289
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
68-349 8.88e-22

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: 93.87  E-value: 8.88e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  68 FRPDSVLGEGGFGCVFKG-WIDeksltasrpgTGLVIAVKKLNQDGwqGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEH 146
Cdd:cd06612   5 FDILEKLGEGSYGSVYKAiHKE----------TGQVVAIKVVPVEE--DLQEIIKEISILKQCDSPYIVKYYGSYFKNTD 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 147 RLLVYEFMPRGSLENHLFRRGlyfQPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAk 226
Cdd:cd06612  73 LWIVMEYCGAGSVSDIMKITN---KTLTEEEIAAILYQTLKGLEYLHSN--KKIHRDIKAGNILLNEEGQAKLADFGVS- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 227 dGPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVDKNRPSgernlvewakpylvnkRKIF 306
Cdd:cd06612 147 -GQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYSDIHPM----------------RAIF 209
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 15222437 307 RVIDN-----RLQDQYSMEEACKVAtlslRCLTTEIKLRPNMSEVVSH 349
Cdd:cd06612 210 MIPNKppptlSDPEKWSPEFNDFVK----KCLVKDPEERPSAIQLLQH 253
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
68-276 1.07e-21

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


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 93.55  E-value: 1.07e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  68 FRPDSVLGEGGFGCVFkgwidekslTASRPGTGLVIAVKKLNQDGWQGhqEWL----AEVNYLGQFSHRHLVKLIGYCLE 143
Cdd:cd14069   3 WDLVQTLGEGAFGEVF---------LAVNRNTEEAVAVKFVDMKRAPG--DCPenikKEVCIQKMLSHKNVVRFYGHRRE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 144 DEHRLLVYEFMPRGSL----------ENHLFRRglYFQPLswklrlkvalgaAKGLAFLHSSEtrVIYRDFKTSNILLDS 213
Cdd:cd14069  72 GEFQYLFLEYASGGELfdkiepdvgmPEDVAQF--YFQQL------------MAGLKYLHSCG--ITHRDIKPENLLLDE 135
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15222437 214 EYNAKLSDFGLAKDGPIGDKSHVSTRVMGTHGYAAPEYLA-TGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14069 136 NDNLKISDFGLATVFRYKGKERLLNKMCGTLPYVAPELLAkKKYRAEPVDVWSCGIVLFAMLAG 199
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
70-353 1.21e-21

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: 93.64  E-value: 1.21e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  70 PDSVLGEGGFGCVFKG-WIDEKsltasrpGTGLVIAVKKLNQDGWQGHQE-WLAEVNYLGQFSHRHLVKLIGYClEDEHR 147
Cdd:cd05056  10 LGRCIGEGQFGDVYQGvYMSPE-------NEKIAVAVKTCKNCTSPSVREkFLQEAYIMRQFDHPHIVKLIGVI-TENPV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 148 LLVYEFMPRGSLENHLFRRGlyfQPLSWKLRLKVALGAAKGLAFLHSseTRVIYRDFKTSNILLDSEYNAKLSDFGLAKd 227
Cdd:cd05056  82 WIVMELAPLGELRSYLQVNK---YSLDLASLILYAYQLSTALAYLES--KRFVHRDIAARNVLVSSPDCVKLGDFGLSR- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 228 gPIGDKSHV-STRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSgrRAVdknrpsgernlvewaKPYL-VNKRKI 305
Cdd:cd05056 156 -YMEDESYYkASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILM--LGV---------------KPFQgVKNNDV 217
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 15222437 306 FRVIDNrlQDQYSMEEACKVATLSL--RCLTTEIKLRPNMSEVVSHLEHI 353
Cdd:cd05056 218 IGRIEN--GERLPMPPNCPPTLYSLmtKCWAYDPSKRPRFTELKAQLSDI 265
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
71-351 1.36e-21

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: 93.40  E-value: 1.36e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  71 DSVLGEGGFGCVFKGWIdeksltaSRPGTG-LVIAVKKLnQDGWQGHQ--EWLAEVNYLGQFSHRHLVKLIGYCLEDEHR 147
Cdd:cd05065   9 EEVIGAGEFGEVCRGRL-------KLPGKReIFVAIKTL-KSGYTEKQrrDFLSEASIMGQFDHPNIIHLEGVVTKSRPV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 148 LLVYEFMPRGSLENHLFRRGLYFQPLSWKLRLKvalGAAKGLAFLhsSETRVIYRDFKTSNILLDSEYNAKLSDFGLAKD 227
Cdd:cd05065  81 MIITEFMENGALDSFLRQNDGQFTVIQLVGMLR---GIAAGMKYL--SEMNYVHRDLAARNILVNSNLVCKVSDFGLSRF 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 228 GPIGDKSHVSTRVMGTH---GYAAPEYLATGHLTTKSDVYSFGVVLLELLSgrravdknrpSGERnlvewakPYL-VNKR 303
Cdd:cd05065 156 LEDDTSDPTYTSSLGGKipiRWTAPEAIAYRKFTSASDVWSYGIVMWEVMS----------YGER-------PYWdMSNQ 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 15222437 304 KIFRVIDNRLQDQYSMEEACKVATLSLRCLTTEIKLRPNMSEVVSHLE 351
Cdd:cd05065 219 DVINAIEQDYRLPPPMDCPTALHQLMLDCWQKDRNLRPKFGQIVNTLD 266
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
74-276 1.47e-21

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: 93.28  E-value: 1.47e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCV----FKGWIDeksltasrpgtglvIAVKKLNQdGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLL 149
Cdd:cd05059  12 LGSGQFGVVhlgkWRGKID--------------VAIKMIKE-GSMSEDDFIEEAKVMMKLSHPKLVQLYGVCTKQRPIFI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 150 VYEFMPRGSLENHLFRRGLYFQPlswKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAKdgP 229
Cdd:cd05059  77 VTEYMANGCLLNYLRERRGKFQT---EQLLEMCKDVCEAMEYLESNG--FIHRDLAARNCLVGEQNVVKVSDFGLAR--Y 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15222437 230 IGDKSHVSTrvMGTH---GYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd05059 150 VLDDEYTSS--VGTKfpvKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSE 197
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
74-277 1.86e-21

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: 93.36  E-value: 1.86e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFkgwidekslTASRPGTGLVIAVKKLNQDGW---QGHQEWLAEVNYLGQFSHRHLVKLiGYCLEDEHRL-L 149
Cdd:cd05577   1 LGRGGFGEVC---------ACQVKATGKMYACKKLDKKRIkkkKGETMALNEKIILEKVSSPFIVSL-AYAFETKDKLcL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 150 VYEFMPRGSLENHLFRRGLYFQPLSwklrlKVALGAAK---GLAFLHssETRVIYRDFKTSNILLDSEYNAKLSDFGLAK 226
Cdd:cd05577  71 VLTLMNGGDLKYHIYNVGTRGFSEA-----RAIFYAAEiicGLEHLH--NRFIVYRDLKPENILLDDHGHVRISDLGLAV 143
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15222437 227 DGPIGDKSHVStrvMGTHGYAAPEYLATGHLTTKS-DVYSFGVVLLELLSGR 277
Cdd:cd05577 144 EFKGGKKIKGR---VGTHGYMAPEVLQKEVAYDFSvDWFALGCMLYEMIAGR 192
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
74-351 3.71e-21

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: 92.72  E-value: 3.71e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGwiDEKSLTASRPGTGlvIAVKKLNQDG-WQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYE 152
Cdd:cd05061  14 LGQGSFGMVYEG--NARDIIKGEAETR--VAVKTVNESAsLRERIEFLNEASVMKGFTCHHVVRLLGVVSKGQPTLVVME 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMPRGSLENHLfrRGLYFQ--------PLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGL 224
Cdd:cd05061  90 LMAHGDLKSYL--RSLRPEaennpgrpPPTLQEMIQMAAEIADGMAYLNAK--KFVHRDLAARNCMVAHDFTVKIGDFGM 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 225 AKDGPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSgrravdknrpsgernLVEwaKPY--LVNK 302
Cdd:cd05061 166 TRDIYETDYYRKGGKGLLPVRWMAPESLKDGVFTTSSDMWSFGVVLWEITS---------------LAE--QPYqgLSNE 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 15222437 303 RKIFRVIDNRLQDQysmEEAC--KVATLSLRCLTTEIKLRPNMSEVVSHLE 351
Cdd:cd05061 229 QVLKFVMDGGYLDQ---PDNCpeRVTDLMRMCWQFNPKMRPTFLEIVNLLK 276
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
72-276 3.98e-21

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


Pssm-ID: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 91.89  E-value: 3.98e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  72 SVLGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQDGwQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVY 151
Cdd:cd06614   6 EKIGEGASGEVYK---------ATDRATGKEVAIKKMRLRK-QNKELIINEILIMKECKHPNIVDYYDSYLVGDELWVVM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 152 EFMPRGSLENHLFRrglYFQPLSWKLRLKVALGAAKGLAFLHSseTRVIYRDFKTSNILLDSEYNAKLSDFGLAKDGpig 231
Cdd:cd06614  76 EYMDGGSLTDIITQ---NPVRMNESQIAYVCREVLQGLEYLHS--QNVIHRDIKSDNILLSKDGSVKLADFGFAAQL--- 147
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15222437 232 dKSHVSTR--VMGTHGYAAPEyLATGHL-TTKSDVYSFGVVLLELLSG 276
Cdd:cd06614 148 -TKEKSKRnsVVGTPYWMAPE-VIKRKDyGPKVDIWSLGIMCIEMAEG 193
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
74-349 4.22e-21

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: 91.86  E-value: 4.22e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVfkgwideKSLTASRPGTGLVIAVKKLNQDgwQGHQEWLA-----EVNYLGQFSHRHLVKLIGYcLEDEHRL 148
Cdd:cd14080   8 IGEGSYSKV-------KLAEYTKSGLKEKVACKIIDKK--KAPKDFLEkflprELEILRKLRHPNIIQVYSI-FERGSKV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 -LVYEFMPRGSLENHLFRRGLYFQPLSWKLRLKVALGaakgLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAKD 227
Cdd:cd14080  78 fIFMEYAEHGDLLEYIQKRGALSESQARIWFRQLALA----VQYLHSLD--IAHRDLKCENILLDSNNNVKLSDFGFARL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 228 GPIGDKSHVSTRVMGTHGYAAPEYL-ATGHLTTKSDVYSFGVVLLELLSGRravdknRPSGERNLvewakpylvnKRKIF 306
Cdd:cd14080 152 CPDDDGDVLSKTFCGSAAYAAPEILqGIPYDPKKYDIWSLGVILYIMLCGS------MPFDDSNI----------KKMLK 215
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 15222437 307 RVIDNRLQDQYSmeeackVATLSLRC-------LTTEIKLRPNMSEVVSH 349
Cdd:cd14080 216 DQQNRKVRFPSS------VKKLSPECkdlidqlLEPDPTKRATIEEILNH 259
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
72-277 6.63e-21

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: 92.00  E-value: 6.63e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  72 SVLGEGGFGCVFKgwideksltASRPGTGLVIAVKKL--NQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLL 149
Cdd:cd07833   7 GVVGEGAYGVVLK---------CRNKATGEIVAIKKFkeSEDDEDVKKTALREVKVLRQLRHENIVNLKEAFRRKGRLYL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 150 VYEFMPRGSLEN-HLFRRGL---YFQPLSWKLrlkvalgaAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLA 225
Cdd:cd07833  78 VFEYVERTLLELlEASPGGLppdAVRSYIWQL--------LQAIAYCHSHN--IIHRDIKPENILVSESGVLKLCDFGFA 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15222437 226 KDGPIGDKSHVSTRVmGTHGYAAPEYLATGHLTTKS-DVYSFGVVLLELLSGR 277
Cdd:cd07833 148 RALTARPASPLTDYV-ATRWYRAPELLVGDTNYGKPvDVWAIGCIMAELLDGE 199
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
72-277 7.38e-21

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: 90.76  E-value: 7.38e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  72 SVLGEGGFGCVFKGwIDEKsltasrpgTGLVIAVKKLNQDgWQGHQEWLAEVNYLGQF----SHRHLVKLIG--YCLEDE 145
Cdd:cd05118   5 RKIGEGAFGTVWLA-RDKV--------TGEKVAIKKIKND-FRHPKAALREIKLLKHLndveGHPNIVKLLDvfEHRGGN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 146 HRLLVYEFMPrgslENHLFRRGLYFQPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNA-KLSDFGL 224
Cdd:cd05118  75 HLCLVFELMG----MNLYELIKDYPRGLPLDLIKSYLYQLLQALDFLHSN--GIIHRDLKPENILINLELGQlKLADFGL 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15222437 225 AK---DGPIGDKshVSTRvmgthGYAAPEYLAT-GHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd05118 149 ARsftSPPYTPY--VATR-----WYRAPEVLLGaKPYGSSIDIWSLGCILAELLTGR 198
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
66-351 1.15e-20

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: 90.86  E-value: 1.15e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  66 RNFRPDSVLGEGGFGCVFKG-WideksltasrpgTGLVIAVKKLNQDGWQG----HQEWLAEVNYLGQFSHRHLVKLIGY 140
Cdd:cd14147   3 QELRLEEVIGIGGFGKVYRGsW------------RGELVAVKAARQDPDEDisvtAESVRQEARLFAMLAHPNIIALKAV 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 141 CLEDEHRLLVYEFMPRGSLENHLFRRGLYFQPL-SWKLRLkvalgaAKGLAFLHSSE-TRVIYRDFKTSNILL------- 211
Cdd:cd14147  71 CLEEPNLCLVMEYAAGGPLSRALAGRRVPPHVLvNWAVQI------ARGMHYLHCEAlVPVIHRDLKSNNILLlqpiend 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 212 DSEYNA-KLSDFGLAKDGpigdksHVSTRV--MGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR---RAVDKnrp 285
Cdd:cd14147 145 DMEHKTlKITDFGLAREW------HKTTQMsaAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEvpyRGIDC--- 215
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15222437 286 sgernlveWAKPYLVNKRKIFRVIDNRLQDQYsmeeackvATLSLRCLTTEIKLRPNMSEVVSHLE 351
Cdd:cd14147 216 --------LAVAYGVAVNKLTLPIPSTCPEPF--------AQLMADCWAQDPHRRPDFASILQQLE 265
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
73-281 2.05e-20

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


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 90.01  E-value: 2.05e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKGWIDEKSltasrpgtglvIAVKKLNQDgwQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDehRLLVYE 152
Cdd:cd14068   1 LLGDGGFGSVYRAVYRGED-----------VAVKIFNKH--TSFRLLRQELVVLSHLHHPSLVALLAAGTAP--RMLVME 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMPRGSLEnHLFRRGLyfQPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILL-----DSEYNAKLSDFGLAKD 227
Cdd:cd14068  66 LAPKGSLD-ALLQQDN--ASLTRTLQHRIALHVADGLRYLHSA--MIIYRDLKPHNVLLftlypNCAIIAKIADYGIAQY 140
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15222437 228 G-PIGDKShvstrVMGTHGYAAPEyLATGHL--TTKSDVYSFGVVLLELLS-GRRAVD 281
Cdd:cd14068 141 CcRMGIKT-----SEGTPGFRAPE-VARGNViyNQQADVYSFGLLLYDILTcGERIVE 192
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
71-281 2.72e-20

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: 89.72  E-value: 2.72e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  71 DSVLGEGGFGCVFKG-WI-DEKSLTASRpgtglviavKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRL 148
Cdd:cd14145  11 EEIIGIGGFGKVYRAiWIgDEVAVKAAR---------HDPDEDISQTIENVRQEAKLFAMLKHPNIIALRGVCLKEPNLC 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 LVYEFMPRGSLENHLfrRGLYFQP---LSWKLRLkvalgaAKGLAFLHSSE-TRVIYRDFKTSNILLD--------SEYN 216
Cdd:cd14145  82 LVMEFARGGPLNRVL--SGKRIPPdilVNWAVQI------ARGMNYLHCEAiVPVIHRDLKSSNILILekvengdlSNKI 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 217 AKLSDFGLAKDGpigdksHVSTRV--MGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR---RAVD 281
Cdd:cd14145 154 LKITDFGLAREW------HRTTKMsaAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEvpfRGID 217
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
65-277 3.10e-20

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: 90.25  E-value: 3.10e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  65 TRNFRPDSVLGEGGFGCVFKGWIDEksltasrpgTGLVIAVKKLNQDGWQGHQEwlaeVNYLGQFSHRHLVKLIGYC--- 141
Cdd:cd14137   3 EISYTIEKVIGSGSFGVVYQAKLLE---------TGEVVAIKKVLQDKRYKNRE----LQIMRRLKHPNIVKLKYFFyss 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 142 LEDEHRL---LVYEFMPrGSLEN---HLFRRGLYFQPLSWKLR---LkvalgaAKGLAFLHSseTRVIYRDFKTSNILLD 212
Cdd:cd14137  70 GEKKDEVylnLVMEYMP-ETLYRvirHYSKNKQTIPIIYVKLYsyqL------FRGLAYLHS--LGICHRDIKPQNLLVD 140
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 213 SE-YNAKLSDFGLAKDGPIGDK--SHVSTRVmgthgYAAPEYL--ATgHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd14137 141 PEtGVLKLCDFGSAKRLVPGEPnvSYICSRY-----YRAPELIfgAT-DYTTAIDIWSAGCVLAELLLGQ 204
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
68-277 3.31e-20

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: 89.33  E-value: 3.31e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  68 FRPDSVLGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQDGWQGHQEWLA---EVNYLGQFSHrhLVKLIGYCLED 144
Cdd:cd06605   3 LEYLGELGEGNGGVVSK---------VRHRPSGQIMAVKVIRLEIDEALQKQILrelDVLHKCNSPY--IVGFYGAFYSE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 145 EHRLLVYEFMPRGSLENHLFRRG-LYFQPLSwklrlKVALGAAKGLAFLHSsETRVIYRDFKTSNILLDSEYNAKLSDFG 223
Cdd:cd06605  72 GDISICMEYMDGGSLDKILKEVGrIPERILG-----KIAVAVVKGLIYLHE-KHKIIHRDVKPSNILVNSRGQVKLCDFG 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15222437 224 lakdgpigdkshVSTRVM--------GTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd06605 146 ------------VSGQLVdslaktfvGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGR 195
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
72-275 3.85e-20

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


Pssm-ID: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 90.11  E-value: 3.85e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  72 SVLGEGGFGCVFKGWIDEKsltasrpgtglVIAVKKLNQdGWqgHQEWLAEVN-Y-LGQFSHRHLVKLIGYC------LE 143
Cdd:cd14054   1 QLIGQGRYGTVWKGSLDER-----------PVAVKVFPA-RH--RQNFQNEKDiYeLPLMEHSNILRFIGADerptadGR 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 144 DEHrLLVYEFMPRGSLENHLFRrglyfQPLSWKLRLKVALGAAKGLAFLHSSETR-------VIYRDFKTSNILLDSEYN 216
Cdd:cd14054  67 MEY-LLVLEYAPKGSLCSYLRE-----NTLDWMSSCRMALSLTRGLAYLHTDLRRgdqykpaIAHRDLNSRNVLVKADGS 140
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15222437 217 AKLSDFGLA--------KDGPIGDKSHVSTRVMGTHGYAAPEYLaTGHLTTKS--------DVYSFGVVLLELLS 275
Cdd:cd14054 141 CVICDFGLAmvlrgsslVRGRPGAAENASISEVGTLRYMAPEVL-EGAVNLRDcesalkqvDVYALGLVLWEIAM 214
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
74-274 4.20e-20

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: 89.23  E-value: 4.20e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGcvfkgwideKSLTASRPGTGLVIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEF 153
Cdd:cd14222   1 LGKGFFG---------QAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEF 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 154 MPRGSLENHLfRRGLYFqplSWKLRLKVALGAAKGLAFLHSseTRVIYRDFKTSNILLDSEYNAKLSDFGLA------KD 227
Cdd:cd14222  72 IEGGTLKDFL-RADDPF---PWQQKVSFAKGIASGMAYLHS--MSIIHRDLNSHNCLIKLDKTVVVADFGLSrliveeKK 145
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15222437 228 GPIGDKSHVSTR------------VMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELL 274
Cdd:cd14222 146 KPPPDKPTTKKRtlrkndrkkrytVVGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCEII 204
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
67-351 7.38e-20

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: 88.38  E-value: 7.38e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGCVFKGWIdekSLTASRPgtgLVIAVKKLnQDGWQGHQ--EWLAEVNYLGQFSHRHLVKLIGYCLED 144
Cdd:cd05066   5 CIKIEKVIGAGEFGEVCSGRL---KLPGKRE---IPVAIKTL-KAGYTEKQrrDFLSEASIMGQFDHPNIIHLEGVVTRS 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 145 EHRLLVYEFMPRGSLENHLFRRGLYFQPLSWKLRLKvalGAAKGLAFLhsSETRVIYRDFKTSNILLDSEYNAKLSDFGL 224
Cdd:cd05066  78 KPVMIVTEYMENGSLDAFLRKHDGQFTVIQLVGMLR---GIASGMKYL--SDMGYVHRDLAARNILVNSNLVCKVSDFGL 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 225 AK---DGPigDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSgrravdknrpSGERnlvewakPYL-V 300
Cdd:cd05066 153 SRvleDDP--EAAYTTRGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMS----------YGER-------PYWeM 213
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 15222437 301 NKRKIFRVIDNRLQDQYSMEEACKVATLSLRCLTTEIKLRPNMSEVVSHLE 351
Cdd:cd05066 214 SNQDVIKAIEEGYRLPAPMDCPAALHQLMLDCWQKDRNERPKFEQIVSILD 264
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
67-277 7.61e-20

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: 88.18  E-value: 7.61e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGCVFkgwidekslTASRPGTGLVIAVKKLNQDgwQGHQEWLAEVNYLGQ-------FSHRHLVKLIG 139
Cdd:cd06625   1 NWKQGKLLGQGAFGQVY---------LCYDADTGRELAVKQVEID--PINTEASKEVKALECeiqllknLQHERIVQYYG 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 140 yCLEDEHRLLVY-EFMPRGSLENHLFRRGlyfqPLSWKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAK 218
Cdd:cd06625  70 -CLQDEKSLSIFmEYMPGGSVKDEIKAYG----ALTENVTRKYTRQILEGLAYLHSNM--IVHRDIKGANILRDSNGNVK 142
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 219 LSDFGLAKD-GPIGDKSHVSTrVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd06625 143 LGDFGASKRlQTICSSTGMKS-VTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTK 201
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
74-351 8.90e-20

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: 88.55  E-value: 8.90e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWidEKSLTASRPGTGlvIAVKKLNQDGWQGHQ-EWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYE 152
Cdd:cd05062  14 LGQGSFGMVYEGI--AKGVVKDEPETR--VAIKTVNEAASMRERiEFLNEASVMKEFNCHHVVRLLGVVSQGQPTLVIME 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMPRGSLENHLfrRGLY--------FQPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGL 224
Cdd:cd05062  90 LMTRGDLKSYL--RSLRpemennpvQAPPSLKKMIQMAGEIADGMAYLNAN--KFVHRDLAARNCMVAEDFTVKIGDFGM 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 225 AKDGPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSgrravdknrpsgernLVEWAKPYLVNKRK 304
Cdd:cd05062 166 TRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTYSDVWSFGVVLWEIAT---------------LAEQPYQGMSNEQV 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 15222437 305 IFRVIDNRLQDQysmEEACKVATLSL--RCLTTEIKLRPNMSEVVSHLE 351
Cdd:cd05062 231 LRFVMEGGLLDK---PDNCPDMLFELmrMCWQYNPKMRPSFLEIISSIK 276
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
68-277 1.00e-19

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: 88.31  E-value: 1.00e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  68 FRPDSVLGEGGFGCVFKGWiDEKsltasrpgTGLVIAVKKLNQDgwqghQEW-------LAEVNYLGQFSHRHLVKLIGY 140
Cdd:cd07829   1 YEKLEKLGEGTYGVVYKAK-DKK--------TGEIVALKKIRLD-----NEEegipstaLREISLLKELKHPNIVKLLDV 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 141 CLEDEHRLLVYEFMPRgSLENHLFRRGLYFQPLSWKLRLKVALgaaKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLS 220
Cdd:cd07829  67 IHTENKLYLVFEYCDQ-DLKKYLDKRPGPLPPNLIKSIMYQLL---RGLAYCHSH--RILHRDLKPQNLLINRDGVLKLA 140
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15222437 221 DFGLAKDGPIGDKSHvSTRVMgTHGYAAPEYL-ATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd07829 141 DFGLARAFGIPLRTY-THEVV-TLWYRAPEILlGSKHYSTAVDIWSVGCIFAELITGK 196
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
111-351 1.09e-19

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: 88.10  E-value: 1.09e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 111 DGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLedeHRL-LVYEFMPRGSL-----ENHlfrRGLYFQPLSWKLRLKVALG 184
Cdd:cd14067  49 DAMKNFSEFRQEASMLHSLQHPCIVYLIGISI---HPLcFALELAPLGSLntvleENH---KGSSFMPLGHMLTFKIAYQ 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 185 AAKGLAFLHssETRVIYRDFKTSNILLDS-----EYNAKLSDFGLAK----DGPIGdkshvstrVMGTHGYAAPEYLATG 255
Cdd:cd14067 123 IAAGLAYLH--KKNIIFCDLKSDNILVWSldvqeHINIKLSDYGISRqsfhEGALG--------VEGTPGYQAPEIRPRI 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 256 HLTTKSDVYSFGVVLLELLSGRR-AVDKNRPSGERNLVEWAKPYLVNKRKI-FRvidnRLQdqysmeeackvaTLSLRCL 333
Cdd:cd14067 193 VYDEKVDMFSYGMVLYELLSGQRpSLGHHQLQIAKKLSKGIRPVLGQPEEVqFF----RLQ------------ALMMECW 256
                       250
                ....*....|....*...
gi 15222437 334 TTEIKLRPNMSEVVSHLE 351
Cdd:cd14067 257 DTKPEKRPLACSVVEQMK 274
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
74-348 1.27e-19

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: 87.75  E-value: 1.27e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVfkgwideKSLTASRPGTGLVIAVKKLNQDGWQGHQE-----WLAEVNYLGQFSHRHLVKLIGYCL-EDEHR 147
Cdd:cd13994   1 IGKGATSVV-------RIVTKKNPRSGVLYAVKEYRRRDDESKRKdyvkrLTSEYIISSKLHHPNIVKVLDLCQdLHGKW 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 148 LLVYEFMPRGSLeNHLFRRGLYFQPLSWKLRLKVALgaaKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAKD 227
Cdd:cd13994  74 CLVMEYCPGGDL-FTLIEKADSLSLEEKDCFFKQIL---RGVAYLHSH--GIAHRDLKPENILLDEDGVLKLTDFGTAEV 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 228 --GPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKS-DVYSFGVVLLELLSGRRAVDKNRPSGERnlvewakpYlvnkrK 304
Cdd:cd13994 148 fgMPAEKESPMSAGLCGSEPYMAPEVFTSGSYDGRAvDVWSCGIVLFALFTGRFPWRSAKKSDSA--------Y-----K 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 15222437 305 IFRVIDNRLQDQY-----SMEEACKvaTLSLRCLTTEIKLRPNMSEVVS 348
Cdd:cd13994 215 AYEKSGDFTNGPYepienLLPSECR--RLIYRMLHPDPEKRITIDEALN 261
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
74-273 2.11e-19

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: 88.17  E-value: 2.11e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFkgwidekslTASRPGTGLVIAVKKLNQDGWQGHQEW---LAEVNYLGQFSHRHLVKLIGYCLEDEHRLLV 150
Cdd:cd06633  29 IGHGSFGAVY---------FATNSHTNEVVAIKKMSYSGKQTNEKWqdiIKEVKFLQQLKHPNTIEYKGCYLKDHTAWLV 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 151 YEFMpRGSLENHLfrrGLYFQPLSWKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAKdgpi 230
Cdd:cd06633 100 MEYC-LGSASDLL---EVHKKPLQEVEIAAITHGALQGLAYLHSHN--MIHRDIKAGNILLTEPGQVKLADFGSAS---- 169
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15222437 231 gdKSHVSTRVMGTHGYAAPEYLAT---GHLTTKSDVYSFGVVLLEL 273
Cdd:cd06633 170 --IASPANSFVGTPYWMAPEVILAmdeGQYDGKVDIWSLGITCIEL 213
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
74-276 2.12e-19

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: 86.81  E-value: 2.12e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWIDEKsltasrpgtglVIAVKKLNQDGWQGHQE---WLAEVNYLGQFSHRHLVKLIGYCLED-EHRLL 149
Cdd:cd14064   1 IGSGSFGKVYKGRCRNK-----------IVAIKRYRANTYCSKSDvdmFCREVSILCRLNHPCVIQFVGACLDDpSQFAI 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 150 VYEFMPRGSLEN--HLFRRGLYFQPlswklRLKVALGAAKGLAFLHSSETRVIYRDFKTSNILLDSEYNAKLSDFGLAKD 227
Cdd:cd14064  70 VTQYVSGGSLFSllHEQKRVIDLQS-----KLIIAVDVAKGMEYLHNLTQPIIHRDLNSHNILLYEDGHAVVADFGESRF 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15222437 228 GPIGDKSHVsTRVMGTHGYAAPE-YLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14064 145 LQSLDEDNM-TKQPGNLRWMAPEvFTQCTRYSIKADVFSYALCLWELLTG 193
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
67-277 2.50e-19

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: 87.63  E-value: 2.50e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGCVFKGwIDEKsltasrpgTGLVIAVKKLNQDGWQGHQEWLA-----EVNYLGQFSHRHLVKLIGYC 141
Cdd:cd07841   1 RYEKGKKLGEGTYAVVYKA-RDKE--------TGRIVAIKKIKLGERKEAKDGINftalrEIKLLQELKHPNIIGLLDVF 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 142 LEDEHRLLVYEFMPrGSLENHLFRRGLYFQPLSWKLRLKVALgaaKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSD 221
Cdd:cd07841  72 GHKSNINLVFEFME-TDLEKVIKDKSIVLTPADIKSYMLMTL---RGLEYLHSNW--ILHRDLKPNNLLIASDGVLKLAD 145
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15222437 222 FGLAKDgpIGD-KSHVSTRVMgTHGYAAPEYL-ATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd07841 146 FGLARS--FGSpNRKMTHQVV-TRWYRAPELLfGARHYGVGVDMWSVGCIFAELLLRV 200
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
73-275 2.60e-19

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: 87.81  E-value: 2.60e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKG-WIDEKSlTASRPgtglvIAVKKLNQD-GWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLlV 150
Cdd:cd05110  14 VLGSGAFGTVYKGiWVPEGE-TVKIP-----VAIKILNETtGPKANVEFMDEALIMASMDHPHLVRLLGVCLSPTIQL-V 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 151 YEFMPRGSLENHLFRrglYFQPLSWKLRLKVALGAAKGLAFLHssETRVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPI 230
Cdd:cd05110  87 TQLMPHGCLLDYVHE---HKDNIGSQLLLNWCVQIAKGMMYLE--ERRLVHRDLAARNVLVKSPNHVKITDFGLARLLEG 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 15222437 231 GDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:cd05110 162 DEKEYNADGGKMPIKWMALECIHYRKFTHQSDVWSYGVTIWELMT 206
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
74-276 2.67e-19

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: 86.68  E-value: 2.67e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKG-WideksltasrpgTGLViAVKKLN--QDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEhRLLV 150
Cdd:cd14062   1 IGSGSFGTVYKGrW------------HGDV-AVKKLNvtDPTPSQLQAFKNEVAVLRKTRHVNILLFMGYMTKPQ-LAIV 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 151 YEFMPRGSLENHLFRRGLYFQPLSWklrLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPI 230
Cdd:cd14062  67 TQWCEGSSLYKHLHVLETKFEMLQL---IDIARQTAQGMDYLHAK--NIIHRDLKSNNIFLHEDLTVKIGDFGLATVKTR 141
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15222437 231 GDKSHVSTRVMGTHGYAAPEYLATGHL---TTKSDVYSFGVVLLELLSG 276
Cdd:cd14062 142 WSGSQQFEQPTGSILWMAPEVIRMQDEnpySFQSDVYAFGIVLYELLTG 190
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
74-275 3.13e-19

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: 87.37  E-value: 3.13e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWIDEKSLTASRpgtgLVIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEF 153
Cdd:cd05094  13 LGEGAFGKVFLAECYNLSPTKDK----MLVAVKTLKDPTLAARKDFQREAELLTNLQHDHIVKFYGVCGDGDPLIMVFEY 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 154 MPRGSLENHLFRRG------LYFQPLSWK------LRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSD 221
Cdd:cd05094  89 MKHGDLNKFLRAHGpdamilVDGQPRQAKgelglsQMLHIATQIASGMVYLASQH--FVHRDLATRNCLVGANLLVKIGD 166
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15222437 222 FGLAKDGPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:cd05094 167 FGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFT 220
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
73-273 3.34e-19

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: 86.91  E-value: 3.34e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKGWIDEKSltasrpGTGLVIAVKKLNQDGWQGHQ--EWLAEVNYLGQFSHRHLVKLIGYCLEDEHR--- 147
Cdd:cd14204  14 VLGEGEFGSVMEGELQQPD------GTNHKVAVKTMKLDNFSQREieEFLSEAACMKDFNHPNVIRLLGVCLEVGSQrip 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 148 --LLVYEFMPRGSLENHLFRRGLYFQPLSWKLR--LKVALGAAKGLAFLhsSETRVIYRDFKTSNILLDSEYNAKLSDFG 223
Cdd:cd14204  88 kpMVILPFMKYGDLHSFLLRSRLGSGPQHVPLQtlLKFMIDIALGMEYL--SSRNFLHRDLAARNCMLRDDMTVCVADFG 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15222437 224 LAKDGPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLEL 273
Cdd:cd14204 166 LSKKIYSGDYYRQGRIAKMPVKWIAVESLADRVYTVKSDVWAFGVTMWEI 215
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
74-350 3.50e-19

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


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 86.14  E-value: 3.50e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWIdeksltasRPGTGLViAVKKLNQDGWQGHQ-EWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYE 152
Cdd:cd05084   4 IGRGNFGEVFSGRL--------RADNTPV-AVKSCRETLPPDLKaKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVME 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMPRGSLENHLFRRGlyfQPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPIGD 232
Cdd:cd05084  75 LVQGGDFLTFLRTEG---PRLKVKELIRMVENAAAGMEYLESK--HCIHRDLAARNCLVTEKNVLKISDFGMSREEEDGV 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 233 KSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSgRRAVDKNRPSGERNLVEWAKPYlvnkrkifrvidnR 312
Cdd:cd05084 150 YAATGGMKQIPVKWTAPEALNYGRYSSESDVWSFGILLWETFS-LGAVPYANLSNQQTREAVEQGV-------------R 215
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 15222437 313 LQdqysMEEAC--KVATLSLRCLTTEIKLRPNMSEVVSHL 350
Cdd:cd05084 216 LP----CPENCpdEVYRLMEQCWEYDPRKRPSFSTVHQDL 251
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
73-275 3.72e-19

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: 87.11  E-value: 3.72e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKGWIDEKsltasrpgtglVIAVKKLNqdgWQGHQEWLAEVNYLG--QFSHRHLVKLIGYCLEDEHR--- 147
Cdd:cd13998   2 VIGKGRFGEVWKASLKNE-----------PVAVKIFS---SRDKQSWFREKEIYRtpMLKHENILQFIAADERDTALrte 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 148 -LLVYEFMPRGSLENHLFRrglyfQPLSWKLRLKVALGAAKGLAFLHSSETR-------VIYRDFKTSNILLDSEYNAKL 219
Cdd:cd13998  68 lWLVTAFHPNGSL*DYLSL-----HTIDWVSLCRLALSVARGLAHLHSEIPGctqgkpaIAHRDLKSKNILVKNDGTCCI 142
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15222437 220 SDFGLA-------KDGPIGDKSHVstrvmGTHGYAAPEYLATG----HLTT--KSDVYSFGVVLLELLS 275
Cdd:cd13998 143 ADFGLAvrlspstGEEDNANNGQV-----GTKRYMAPEVLEGAinlrDFESfkRVDIYAMGLVLWEMAS 206
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
73-349 4.18e-19

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: 86.44  E-value: 4.18e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKgwIDEKSltasrpgTGLVIAVKKLNQDGWQGH--QEWLAEVNYLGQFSHRHLVKLIG-YCLEDEHRL- 148
Cdd:cd08217   7 TIGKGSFGTVRK--VRRKS-------DGKILVWKEIDYGKMSEKekQQLVSEVNILRELKHPNIVRYYDrIVDRANTTLy 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 LVYEFMPRGSLEN---HLFRRGLYF-QPLSWKLRLKVALGaakgLAFLHSSET---RVIYRDFKTSNILLDSEYNAKLSD 221
Cdd:cd08217  78 IVMEYCEGGDLAQlikKCKKENQYIpEEFIWKIFTQLLLA----LYECHNRSVgggKILHRDLKPANIFLDSDNNVKLGD 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 222 FGLAKdgPIGDKSHV-STRVmGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRravdknRPSGERNLVEWAKpyLV 300
Cdd:cd08217 154 FGLAR--VLSHDSSFaKTYV-GTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALH------PPFQAANQLELAK--KI 222
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 15222437 301 NKRKIfrvidNRLQDQYSMEeackvatLSL---RCLTTEIKLRPNMSEVVSH 349
Cdd:cd08217 223 KEGKF-----PRIPSRYSSE-------LNEvikSMLNVDPDKRPSVEELLQL 262
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
66-353 4.22e-19

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: 86.90  E-value: 4.22e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  66 RNFRPDSVLGEGGFGCVfkgwidEKSLTASRPGTGLVIAVKKLNQDGWQGH--QEWLAEVNYLGQFSHRHLVKLIGYCLE 143
Cdd:cd05074   9 QQFTLGRMLGKGEFGSV------REAQLKSEDGSFQKVAVKMLKADIFSSSdiEEFLREAACMKEFDHPNVIKLIGVSLR 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 144 DEHR------LLVYEFMPRGSLENHLFRRGLYFQPLSWKLR--LKVALGAAKGLAFLhsSETRVIYRDFKTSNILLDSEY 215
Cdd:cd05074  83 SRAKgrlpipMVILPFMKHGDLHTFLLMSRIGEEPFTLPLQtlVRFMIDIASGMEYL--SSKNFIHRDLAARNCMLNENM 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 216 NAKLSDFGLAKDGPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSgrravdknrpSGErnlvewa 295
Cdd:cd05074 161 TVCVADFGLSKKIYSGDYYRQGCASKLPVKWLALESLADNVYTTHSDVWAFGVTMWEIMT----------RGQ------- 223
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15222437 296 KPYL-VNKRKIFRVI--DNRL-QDQYSMEEackVATLSLRCLTTEIKLRPNMSEVVSHLEHI 353
Cdd:cd05074 224 TPYAgVENSEIYNYLikGNRLkQPPDCLED---VYELMCQCWSPEPKCRPSFQHLRDQLELI 282
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
74-275 4.57e-19

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: 86.63  E-value: 4.57e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGwideKSLTASRPGTGLVIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEF 153
Cdd:cd05093  13 LGEGAFGKVFLA----ECYNLCPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEY 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 154 MPRGSLENHL---------FRRGLYFQPLSWKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGL 224
Cdd:cd05093  89 MKHGDLNKFLrahgpdavlMAEGNRPAELTQSQMLHIAQQIAAGMVYLASQH--FVHRDLATRNCLVGENLLVKIGDFGM 166
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15222437 225 AKDGPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:cd05093 167 SRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFT 217
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
74-346 6.72e-19

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


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 86.59  E-value: 6.72e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFG----CVFKG---WIDEKSLTASRPGTGLVIAVKKLNQDGWQ-GHQEWLAEVNYLGQFSHRHLVKLIGYCLEDE 145
Cdd:cd05095  13 LGEGQFGevhlCEAEGmekFMDKDFALEVSENQPVLVAVKMLRADANKnARNDFLKEIKIMSRLKDPNIIRLLAVCITDD 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 146 HRLLVYEFMPRGSLENHLFRRGLYFQPLSWKLRLKV--------ALGAAKGLAFLhsSETRVIYRDFKTSNILLDSEYNA 217
Cdd:cd05095  93 PLCMITEYMENGDLNQFLSRQQPEGQLALPSNALTVsysdlrfmAAQIASGMKYL--SSLNFVHRDLATRNCLVGKNYTI 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 218 KLSDFGLAKDGPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVDKNRPSGERnLVEwakp 297
Cdd:cd05095 171 KIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETLTFCREQPYSQLSDEQ-VIE---- 245
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 15222437 298 ylvNKRKIFRviDNRLQDQYSMEEAC--KVATLSLRCLTTEIKLRPNMSEV 346
Cdd:cd05095 246 ---NTGEFFR--DQGRQTYLPQPALCpdSVYKLMLSCWRRDTKDRPSFQEI 291
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
74-275 7.18e-19

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: 86.14  E-value: 7.18e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWIDEKSltasrPGTGLVIAVKKLNQDGWQGHQEWL-AEVNYLGQFSHRHLVKLIGYCLEDEHR--LLV 150
Cdd:cd05079  12 LGEGHFGKVELCRYDPEG-----DNTGEQVAVKSLKPESGGNHIADLkKEIEILRNLYHENIVKYKGICTEDGGNgiKLI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 151 YEFMPRGSLENHLFRRGlyfQPLSWKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAK---- 226
Cdd:cd05079  87 MEFLPSGSLKEYLPRNK---NKINLKQQLKYAVQICKGMDYLGSRQ--YVHRDLAARNVLVESEHQVKIGDFGLTKaiet 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15222437 227 -DGPIGDKSHVSTRVMgthgYAAPEYLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:cd05079 162 dKEYYTVKDDLDSPVF----WYAPECLIQSKFYIASDVWSFGVTLYELLT 207
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
73-349 7.29e-19

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: 85.55  E-value: 7.29e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFkgwideksLTASRPGTGLVIaVKKLNQDGW--QGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLV 150
Cdd:cd08220   7 VVGRGAYGTVY--------LCRRKDDNKLVI-IKQIPVEQMtkEERQAALNEVKVLSMLHHPNIIEYYESFLEDKALMIV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 151 YEFMPRGSLENHLFRRGLYFQPLSWKLRLKVALGAAkgLAFLHSSEtrVIYRDFKTSNILLDSEYN-AKLSDFGLAKDgp 229
Cdd:cd08220  78 MEYAPGGTLFEYIQQRKGSLLSEEEILHFFVQILLA--LHHVHSKQ--ILHRDLKTQNILLNKKRTvVKIGDFGISKI-- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 230 IGDKSHVSTrVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVDKnrpsgeRNLvewakPYLVnkRKIFRVI 309
Cdd:cd08220 152 LSSKSKAYT-VVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEA------ANL-----PALV--LKIMRGT 217
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 15222437 310 DNRLQDQYSMEeackVATLSLRCLTTEIKLRPNMSEVVSH 349
Cdd:cd08220 218 FAPISDRYSEE----LRHLILSMLHLDPNKRPTLSEIMAQ 253
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
74-317 1.09e-18

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: 85.01  E-value: 1.09e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWIDEKSltasrpgTGLVIAVKKLNQDGWQG--HQEWLAEVNYLGQFSHRHLVKLIGYClEDEHRLLVY 151
Cdd:cd05116   3 LGSGNFGTVKKGYYQMKK-------VVKTVAVKILKNEANDPalKDELLREANVMQQLDNPYIVRMIGIC-EAESWMLVM 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 152 EFMPRGSLENHLFRRglyfQPLSWKLRLKVALGAAKGLAFLHssETRVIYRDFKTSNILLDSEYNAKLSDFGLAKdGPIG 231
Cdd:cd05116  75 EMAELGPLNKFLQKN----RHVTEKNITELVHQVSMGMKYLE--ESNFVHRDLAARNVLLVTQHYAKISDFGLSK-ALRA 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 232 DKSHVSTRvmgTHG-----YAAPEYLATGHLTTKSDVYSFGVVLLELLS-GRRA--------VDKNRPSGER-------- 289
Cdd:cd05116 148 DENYYKAQ---THGkwpvkWYAPECMNYYKFSSKSDVWSFGVLMWEAFSyGQKPykgmkgneVTQMIEKGERmecpagcp 224
                       250       260       270
                ....*....|....*....|....*....|..
gi 15222437 290 ----NLVEWAKPYLVNKRKIFRVIDNRLQDQY 317
Cdd:cd05116 225 pemyDLMKLCWTYDVDERPGFAAVELRLRNYY 256
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
73-276 1.28e-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: 85.32  E-value: 1.28e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFkgwidekslTASRPGTGLVIAVKKLNQD-----GWQGHQewLAEVNYLGQFSHRHLVKLIGyCLEDEHR 147
Cdd:cd05580   8 TLGTGSFGRVR---------LVKHKDSGKYYALKILKKAkiiklKQVEHV--LNEKRILSEVRHPFIVNLLG-SFQDDRN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 148 L-LVYEFMPRGSLENHLFRRGlyfqplswKLRLKVAL-GAAK---GLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDF 222
Cdd:cd05580  76 LyMVMEYVPGGELFSLLRRSG--------RFPNDVAKfYAAEvvlALEYLHSLD--IVYRDLKPENLLLDSDGHIKITDF 145
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15222437 223 GLAKdgpigdksHVSTR---VMGTHGYAAPE-YLATGHltTKS-DVYSFGVVLLELLSG 276
Cdd:cd05580 146 GFAK--------RVKDRtytLCGTPEYLAPEiILSKGH--GKAvDWWALGILIYEMLAG 194
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
72-277 1.36e-18

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: 85.91  E-value: 1.36e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  72 SVLGEGGFGcvfkgwideKSLTASRPGTGLVIAVKKLNQDGWQGHQE---WLAEVNYLGQFSHRHLVKLIGYCLEDEHRL 148
Cdd:cd05587   2 MVLGKGSFG---------KVMLAERKGTDELYAIKILKKDVIIQDDDvecTMVEKRVLALSGKPPFLTQLHSCFQTMDRL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 L-VYEFMPRGSLENHLFRRGLYFQPLSWKLRLKVALGaakgLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAKD 227
Cdd:cd05587  73 YfVMEYVNGGDLMYHIQQVGKFKEPVAVFYAAEIAVG----LFFLHSK--GIIYRDLKLDNVMLDAEGHIKIADFGMCKE 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15222437 228 GPIGDKshvSTRVM-GTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd05587 147 GIFGGK---TTRTFcGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQ 194
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
74-353 1.44e-18

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: 84.78  E-value: 1.44e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWIDEKSLTasrpgtglvIAVKKLNQDGWQGHqEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEF 153
Cdd:cd05052  14 LGGGQYGEVYEGVWKKYNLT---------VAVKTLKEDTMEVE-EFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 154 MPRGSLENHLFRRGLyfQPLSWKLRLKVALGAAKGLAFLhssETR-VIYRDFKTSNILLDSEYNAKLSDFGLAkdgpigd 232
Cdd:cd05052  84 MPYGNLLDYLRECNR--EELNAVVLLYMATQIASAMEYL---EKKnFIHRDLAARNCLVGENHLVKVADFGLS------- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 233 kshvstRVMGTHGY------------AAPEYLATGHLTTKSDVYSFGVVLLEL----LSGRRAVDknrpsgernlvewak 296
Cdd:cd05052 152 ------RLMTGDTYtahagakfpikwTAPESLAYNKFSIKSDVWAFGVLLWEIatygMSPYPGID--------------- 210
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15222437 297 pylvnkrkiFRVIDNRLQDQYSME--EAC--KVATLSLRCLTTEIKLRPNMSEVVSHLEHI 353
Cdd:cd05052 211 ---------LSQVYELLEKGYRMErpEGCppKVYELMRACWQWNPSDRPSFAEIHQALETM 262
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
100-273 1.74e-18

Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-A binds and is activated by the atrial and B-type natriuretic peptides, ANP and BNP, which are important in blood pressure regulation and cardiac pathophysiology. GC-B binds the C-type natriuretic peptide, CNP, which is a potent vasorelaxant and functions in vascular remodeling and bone growth regulation. 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 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-A/B 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: 270944 [Multi-domain]  Cd Length: 279  Bit Score: 84.95  E-value: 1.74e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 100 GLVIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEFMPRGSL----ENHLFRrglyfqpLSW 175
Cdd:cd14042  30 GNLVAIKKVNKKRIDLTREVLKELKHMRDLQHDNLTRFIGACVDPPNICILTEYCPKGSLqdilENEDIK-------LDW 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 176 KLRLKVALGAAKGLAFLHSSETRViYRDFKTSNILLDSEYNAKLSDFGLA--KDGpigdkshvSTRVMGTHGYA------ 247
Cdd:cd14042 103 MFRYSLIHDIVKGMHYLHDSEIKS-HGNLKSSNCVVDSRFVLKITDFGLHsfRSG--------QEPPDDSHAYYakllwt 173
                       170       180       190
                ....*....|....*....|....*....|
gi 15222437 248 APEYLATGHL----TTKSDVYSFGVVLLEL 273
Cdd:cd14042 174 APELLRDPNPpppgTQKGDVYSFGIILQEI 203
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
72-277 2.12e-18

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: 84.23  E-value: 2.12e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  72 SVLGEGGFGCVFKGwideksltaSRPGTGLVIAVKKLNQDGwQGHQEWLA---EVNYLGQFSHRHLVKLIGyCLEDEHRL 148
Cdd:cd14002   7 ELIGEGSFGKVYKG---------RRKYTGQVVALKFIPKRG-KSEKELRNlrqEIEILRKLNHPNIIEMLD-SFETKKEF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 -LVYEFMpRGSLenhlfrrglyFQPLSWKLRL------KVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSD 221
Cdd:cd14002  76 vVVTEYA-QGEL----------FQILEDDGTLpeeevrSIAKQLVSALHYLHSN--RIIHRDMKPQNILIGKGGVVKLCD 142
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15222437 222 FGLAKDGPIGdkSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd14002 143 FGFARAMSCN--TLVLTSIKGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQ 196
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
74-277 2.45e-18

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: 85.30  E-value: 2.45e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGwIDEKsltasrpgTGLVIAVKKL-----NQdgwQGHQEWLAEVNYLGQFS-HRHLVKLIgycleDEHR 147
Cdd:cd07852  15 LGKGAYGIVWKA-IDKK--------TGEVVALKKIfdafrNA---TDAQRTFREIMFLQELNdHPNIIKLL-----NVIR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 148 -------LLVYEFMP--------RGSLEN-HlfRRGLYFQPLswklrlkvalgaaKGLAFLHSSEtrVIYRDFKTSNILL 211
Cdd:cd07852  78 aendkdiYLVFEYMEtdlhavirANILEDiH--KQYIMYQLL-------------KALKYLHSGG--VIHRDLKPSNILL 140
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15222437 212 DSEYNAKLSDFGLAKDGPIGDKSH--------VSTRvmgthGYAAPEYLATGHLTTKS-DVYSFGVVLLELLSGR 277
Cdd:cd07852 141 NSDCRVKLADFGLARSLSQLEEDDenpvltdyVATR-----WYRAPEILLGSTRYTKGvDMWSVGCILGEMLLGK 210
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
100-288 2.78e-18

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


Pssm-ID: 270947 [Multi-domain]  Cd Length: 269  Bit Score: 84.14  E-value: 2.78e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 100 GLVIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEFMPRGSLENHLFRRGLyfqPLSWKLRL 179
Cdd:cd14045  30 GRTVAIKKIAKKSFTLSKRIRKEVKQVRELDHPNLCKFIGGCIEVPNVAIITEYCPKGSLNDVLLNEDI---PLNWGFRF 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 180 KVALGAAKGLAFLHssETRVIYRDFKTSNILLDSEYNAKLSDFGLA----KDGPIGDKSHVStRVMGThgYAAPEY--LA 253
Cdd:cd14045 107 SFATDIARGMAYLH--QHKIYHGRLKSSNCVIDDRWVCKIADYGLTtyrkEDGSENASGYQQ-RLMQV--YLPPENhsNT 181
                       170       180       190
                ....*....|....*....|....*....|....*
gi 15222437 254 TGHLTTKSDVYSFGVVLLELLSGRRAVDKNRPSGE 288
Cdd:cd14045 182 DTEPTQATDVYSYAIILLEIATRNDPVPEDDYSLD 216
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
115-277 2.79e-18

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: 84.09  E-value: 2.79e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 115 GHQE-WLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEFMPRGSLENHLFRRGLyfqPLSWKLRlkVALGAAKGLAFLH 193
Cdd:cd14027  33 EHNEaLLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNLMHVLKKVSV---PLSVKGR--IILEIIEGMAYLH 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 194 ssETRVIYRDFKTSNILLDSEYNAKLSDFGLAK----DGPIGDKSHVSTRVMGTHG-------YAAPEYLATGHL--TTK 260
Cdd:cd14027 108 --GKGVIHKDLKPENILVDNDFHIKIADLGLASfkmwSKLTKEEHNEQREVDGTAKknagtlyYMAPEHLNDVNAkpTEK 185
                       170
                ....*....|....*..
gi 15222437 261 SDVYSFGVVLLELLSGR 277
Cdd:cd14027 186 SDVYSFAIVLWAIFANK 202
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
71-278 2.90e-18

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: 83.82  E-value: 2.90e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  71 DSVLGEGGFGCVFKGWIdekSLTASRPgtgLVIAVKKLnQDGWQGHQE--WLAEVNYLGQFSHRHLVKLIGYCLEDEHRL 148
Cdd:cd05064  10 ERILGTGRFGELCRGCL---KLPSKRE---LPVAIHTL-RAGCSDKQRrgFLAEALTLGQFDHSNIVRLEGVITRGNTMM 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 LVYEFMPRGSLENHLFRrglYFQPLSWKLRLKVALGAAKGLAFLhsSETRVIYRDFKTSNILLDSEYNAKLSDFGLAKDg 228
Cdd:cd05064  83 IVTEYMSNGALDSFLRK---HEGQLVAGQLMGMLPGLASGMKYL--SEMGYVHKGLAAHKVLVNSDLVCKISGFRRLQE- 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15222437 229 pigDKSHVSTRVMGTHG---YAAPEYLATGHLTTKSDVYSFGVVLLELLS-GRR 278
Cdd:cd05064 157 ---DKSEAIYTTMSGKSpvlWAAPEAIQYHHFSSASDVWSFGIVMWEVMSyGER 207
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
74-277 3.84e-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: 84.03  E-value: 3.84e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVfkgwidekSLTASRPgTGLVIAVKKLNQDGWQGHQ-EWLAEVNYLGQFSHRHLVKLIGYCL-EDEHRLLVY 151
Cdd:cd06620  13 LGAGNGGSV--------SKVLHIP-TGTIMAKKVIHIDAKSSVRkQILRELQILHECHSPYIVSFYGAFLnENNNIIICM 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 152 EFMPRGSLENhLFRRGLYFQPLSWKlrlKVALGAAKGLAFLHSsETRVIYRDFKTSNILLDSEYNAKLSDFGLAKD--GP 229
Cdd:cd06620  84 EYMDCGSLDK-ILKKKGPFPEEVLG---KIAVAVLEGLTYLYN-VHRIIHRDIKPSNILVNSKGQIKLCDFGVSGEliNS 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15222437 230 IGDkshvsTRVmGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd06620 159 IAD-----TFV-GTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGE 200
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
68-293 4.38e-18

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: 83.92  E-value: 4.38e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  68 FRPDSVLGEGGFGCVfkgwideksLTASRPGTGLVIAVKKLNQD---GWQGHQEWLAEVNYLGQFSHRHLVKLiGYCLED 144
Cdd:cd05630   2 FRQYRVLGKGGFGEV---------CACQVRATGKMYACKKLEKKrikKRKGEAMALNEKQILEKVNSRFVVSL-AYAYET 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 145 EHRL-LVYEFMPRGSLENHLFRRGLYFQPlswklRLKVALGAAK---GLAFLHssETRVIYRDFKTSNILLDSEYNAKLS 220
Cdd:cd05630  72 KDALcLVLTLMNGGDLKFHIYHMGQAGFP-----EARAVFYAAEiccGLEDLH--RERIVYRDLKPENILLDDHGHIRIS 144
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15222437 221 DFGLAKDGPIGDKshVSTRVmGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVDKNRPSGERNLVE 293
Cdd:cd05630 145 DLGLAVHVPEGQT--IKGRV-GTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVE 214
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
67-276 4.39e-18

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: 83.20  E-value: 4.39e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQD--GWQGHQEWLAEVN---YLGQfsHRHLVKLIGYC 141
Cdd:cd13997   1 HFHELEQIGSGSFSEVFK---------VRSKVDGCLYAVKKSKKPfrGPKERARALREVEahaALGQ--HPNIVRYYSSW 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 142 LEDEHRLLVYEFMPRGSLENHLFRRGLyFQPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSD 221
Cdd:cd13997  70 EEGGHLYIQMELCENGSLQDALEELSP-ISKLSEAEVWDLLLQVALGLAFIHSK--GIVHLDIKPDNIFISNKGTCKIGD 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 222 FGLAkdgpigdkSHVSTRVM---GTHGYAAPEYLAtGHLT--TKSDVYSFGVVLLELLSG 276
Cdd:cd13997 147 FGLA--------TRLETSGDveeGDSRYLAPELLN-ENYThlPKADIFSLGVTVYEAATG 197
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
72-277 4.50e-18

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: 83.35  E-value: 4.50e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  72 SVLGEGGFGCVFKGwideksLTASrpgTGLVIAVKK--LNQDGWQGHQ------EWLA-EVNYLGQFSHRHLVKLIGYCL 142
Cdd:cd06628   6 ALIGSGSFGSVYLG------MNAS---SGELMAVKQveLPSVSAENKDrkksmlDALQrEIALLRELQHENIVQYLGSSS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 143 EDEHRLLVYEFMPRGSLENHLFRRGLYFQPLSWKLRLKVAlgaaKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDF 222
Cdd:cd06628  77 DANHLNIFLEYVPGGSVATLLNNYGAFEESLVRNFVRQIL----KGLNYLHNRG--IIHRDIKGANILVDNKGGIKISDF 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15222437 223 GLAK----DGPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd06628 151 GISKkleaNSLSTKNNGARPSLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGT 209
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
74-273 5.00e-18

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: 83.52  E-value: 5.00e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWIDEKsltasrpGTGLVIAVK--KLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHR---- 147
Cdd:cd05075   8 LGEGEFGSVMEGQLNQD-------DSVLKVAVKtmKIAICTRSEMEDFLSEAVCMKEFDHPNVMRLIGVCLQNTESegyp 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 148 --LLVYEFMPRGSLENHLFRRGLYFQP--LSWKLRLKVALGAAKGLAFLhsSETRVIYRDFKTSNILLDSEYNAKLSDFG 223
Cdd:cd05075  81 spVVILPFMKHGDLHSFLLYSRLGDCPvyLPTQMLVKFMTDIASGMEYL--SSKNFIHRDLAARNCMLNENMNVCVADFG 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15222437 224 LAKDGPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLEL 273
Cdd:cd05075 159 LSKKIYNGDYYRQGRISKMPVKWIAIESLADRVYTTKSDVWSFGVTMWEI 208
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
67-277 5.43e-18

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: 83.42  E-value: 5.43e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGCVFKGWidEKSltasrpgTGLVIAVKKLNQDgwQGHQEwlAEVNY-------LGQFSHRHLVKLIg 139
Cdd:cd05581   2 DFKFGKPLGEGSYSTVVLAK--EKE-------TGKEYAIKVLDKR--HIIKE--KKVKYvtiekevLSRLAHPGIVKLY- 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 140 YCLEDEHRL-LVYEFMPRGSLENHLFRRGlyfqPLSWK-LRLKVALgAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNA 217
Cdd:cd05581  68 YTFQDESKLyFVLEYAPNGDLLEYIRKYG----SLDEKcTRFYTAE-IVLALEYLHSK--GIIHRDLKPENILLDEDMHI 140
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15222437 218 KLSDFGLAKDGPIGDKSHVSTRVM---------------GTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd05581 141 KITDFGTAKVLGPDSSPESTKGDAdsqiaynqaraasfvGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGK 215
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
67-277 5.65e-18

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: 83.39  E-value: 5.65e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRpdsVLGEGGFGCVFkgwidekslTASRPGTGLVIAVKKLNQDGW---QGHQEWLAEVNYLGQFSHRHLVKLiGYCLE 143
Cdd:cd05608   5 DFR---VLGKGGFGEVS---------ACQMRATGKLYACKKLNKKRLkkrKGYEGAMVEKRILAKVHSRFIVSL-AYAFQ 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 144 DEHRL-LVYEFMPRGSLENHLFR-----------RGLYF--QPLSwklrlkvalgaakGLAFLHssETRVIYRDFKTSNI 209
Cdd:cd05608  72 TKTDLcLVMTIMNGGDLRYHIYNvdeenpgfqepRACFYtaQIIS-------------GLEHLH--QRRIIYRDLKPENV 136
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15222437 210 LLDSEYNAKLSDFGLA---KDGPIGDKSHVstrvmGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd05608 137 LLDDDGNVRISDLGLAvelKDGQTKTKGYA-----GTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAAR 202
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
74-277 5.68e-18

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: 82.66  E-value: 5.68e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWIDEksltasrpgTGLVIAVKKLNQDGWQGH-QEWL-AEVNYLGQFSHRHLVKLIGyCLEDEHRL-LV 150
Cdd:cd14009   1 IGRGSFATVWKGRHKQ---------TGEVVAIKEISRKKLNKKlQENLeSEIAILKSIKHPNIVRLYD-VQKTEDFIyLV 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 151 YEFMPRGSLENHLFRRGLyfqpLSWKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNA---KLSDFGLAKd 227
Cdd:cd14009  71 LEYCAGGDLSQYIRKRGR----LPEAVARHFMQQLASGLKFLRSKN--IIHRDLKPQNLLLSTSGDDpvlKIADFGFAR- 143
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15222437 228 gpigdksHVSTRVM-----GTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd14009 144 -------SLQPASMaetlcGSPLYMAPEILQFQKYDAKADLWSVGAILFEMLVGK 191
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
68-275 6.23e-18

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: 83.92  E-value: 6.23e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  68 FRPDSVLGEGGFGCVFKG-WIDEKSltasrpGTGLVIAVKKLNQ-DGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDE 145
Cdd:cd05108   9 FKKIKVLGSGAFGTVYKGlWIPEGE------KVKIPVAIKELREaTSPKANKEILDEAYVMASVDNPHVCRLLGICLTST 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 146 HRLlVYEFMPRGSLENHLFRR-----GLYFqpLSWKLRLkvalgaAKGLAFLHssETRVIYRDFKTSNILLDSEYNAKLS 220
Cdd:cd05108  83 VQL-ITQLMPFGCLLDYVREHkdnigSQYL--LNWCVQI------AKGMNYLE--DRRLVHRDLAARNVLVKTPQHVKIT 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15222437 221 DFGLAKDGPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:cd05108 152 DFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMT 206
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
73-275 6.61e-18

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: 83.69  E-value: 6.61e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKGwidekslTA---SRPGTGLVIAVKKLNQDGWQGHQEWLAE----VNYLGQfsHRHLVKLIGYCLEDE 145
Cdd:cd05055  42 TLGAGAFGKVVEA-------TAyglSKSDAVMKVAVKMLKPTAHSSEREALMSelkiMSHLGN--HENIVNLLGACTIGG 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 146 HRLLVYEFMPRGSLENHLFRRGLYFqpLSWKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLA 225
Cdd:cd05055 113 PILVITEYCCYGDLLNFLRRKRESF--LTLEDLLSFSYQVAKGMAFLASKN--CIHRDLAARNVLLTHGKIVKICDFGLA 188
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15222437 226 KDgPIGDKSHV---STRVmgTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:cd05055 189 RD-IMNDSNYVvkgNARL--PVKWMAPESIFNCVYTFESDVWSYGILLWEIFS 238
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
74-278 6.73e-18

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: 82.81  E-value: 6.73e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGwideksLTASrpgTGLVIAVKKL------NQDGWQGHQEWLA----EVNYLGQFSHRHLVKLIGYCLE 143
Cdd:cd06629   9 IGKGTYGRVYLA------MNAT---TGEMLAVKQVelpktsSDRADSRQKTVVDalksEIDTLKDLDHPNIVQYLGFEET 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 144 DEHRLLVYEFMPRGSLENHLFRRGLYFQPLSWKLRLKVAlgaaKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFG 223
Cdd:cd06629  80 EDYFSIFLEYVPGGSIGSCLRKYGKFEEDLVRFFTRQIL----DGLAYLHSKG--ILHRDLKADNILVDLEGICKISDFG 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15222437 224 LAKDGPIGDKSHVSTRVMGTHGYAAPEYLATGH--LTTKSDVYSFGVVLLELLSGRR 278
Cdd:cd06629 154 ISKKSDDIYGNNGATSMQGSVFWMAPEVIHSQGqgYSAKVDIWSLGCVVLEMLAGRR 210
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
102-277 7.33e-18

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: 82.79  E-value: 7.33e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 102 VIAVKKLNQDGWQGH-QEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEFMPRGSLEnHLFRRGLYFQPLSWKLRLK 180
Cdd:cd06610  28 KVAIKRIDLEKCQTSmDELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMPLLSGGSLL-DIMKSSYPRGGLDEAIIAT 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 181 VALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFG----LAKDGpiGDKSHVSTRVMGTHGYAAPEYLATGH 256
Cdd:cd06610 107 VLKEVLKGLEYLHSN--GQIHRDVKAGNILLGEDGSVKIADFGvsasLATGG--DRTRKVRKTFVGTPCWMAPEVMEQVR 182
                       170       180
                ....*....|....*....|..
gi 15222437 257 -LTTKSDVYSFGVVLLELLSGR 277
Cdd:cd06610 183 gYDFKADIWSFGITAIELATGA 204
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
73-275 7.83e-18

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: 82.78  E-value: 7.83e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKGWIdeksltaSRPGTGLVIAVKKLNQDGWQG-HQEWLAEVNYLGQFSHR-HLVKLIGYCledEHRLLV 150
Cdd:cd05047   2 VIGEGNFGQVLKARI-------KKDGLRMDAAIKRMKEYASKDdHRDFAGELEVLCKLGHHpNIINLLGAC---EHRGYL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 151 Y---EFMPRGSLENHLFR-RGLYFQP-----------LSWKLRLKVALGAAKGLAFLhsSETRVIYRDFKTSNILLDSEY 215
Cdd:cd05047  72 YlaiEYAPHGNLLDFLRKsRVLETDPafaianstastLSSQQLLHFAADVARGMDYL--SQKQFIHRDLAARNILVGENY 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15222437 216 NAKLSDFGLAKdgpiGDKSHVStRVMGTHG--YAAPEYLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:cd05047 150 VAKIADFGLSR----GQEVYVK-KTMGRLPvrWMAIESLNYSVYTTNSDVWSYGVLLWEIVS 206
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
74-277 8.51e-18

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


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 82.45  E-value: 8.51e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKG-WIDEKSltasrpgtglvIAVKKLnQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYE 152
Cdd:cd05068  16 LGSGQFGEVWEGlWNNTTP-----------VAVKTL-KPGTMDPEDFLREAQIMKKLRHPKLIQLYAVCTLEEPIYIITE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMPRGSLENHLFRRGLyfqplSWKLRLKVALGA--AKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAKdgpI 230
Cdd:cd05068  84 LMKHGSLLEYLQGKGR-----SLQLPQLIDMAAqvASGMAYLESQN--YIHRDLAARNVLVGENNICKVADFGLAR---V 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15222437 231 GDKSHVSTRVMGTH---GYAAPEYLATGHLTTKSDVYSFGVVLLELLS-GR 277
Cdd:cd05068 154 IKVEDEYEAREGAKfpiKWTAPEAANYNRFSIKSDVWSFGILLTEIVTyGR 204
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
73-277 8.93e-18

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: 83.42  E-value: 8.93e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGcvfkgwideKSLTASRPGTGLVIAVKKL-----NQDGwqgHQEW-LAEVNYLGQfSHRH--LVKLIGyCLED 144
Cdd:cd05570   2 VLGKGSFG---------KVMLAERKKTDELYAIKVLkkeviIEDD---DVECtMTEKRVLAL-ANRHpfLTGLHA-CFQT 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 145 EHRL-LVYEFMPRGSLENHLFRRGLYFQPLSWKLRLKVALGaakgLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFG 223
Cdd:cd05570  68 EDRLyFVMEYVNGGDLMFHIQRARRFTEERARFYAAEICLA----LQFLHERG--IIYRDLKLDNVLLDAEGHIKIADFG 141
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15222437 224 LAKDGPIGDKshvSTRVM-GTHGYAAPEYLaTGHLTTKS-DVYSFGVVLLELLSGR 277
Cdd:cd05570 142 MCKEGIWGGN---TTSTFcGTPDYIAPEIL-REQDYGFSvDWWALGVLLYEMLAGQ 193
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
74-353 9.13e-18

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: 83.24  E-value: 9.13e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGwiDEKSLTASRPGTgLVIAVKKLNQDGWQghQEWLAEVNYLGQFS----HRHLVKLIGYCLEDEHRLL 149
Cdd:cd05053  20 LGEGAFGQVVKA--EAVGLDNKPNEV-VTVAVKMLKDDATE--KDLSDLVSEMEMMKmigkHKNIINLLGACTQDGPLYV 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 150 VYEFMPRGSLENHLFRR---GLYF---------QPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNA 217
Cdd:cd05053  95 VVEYASKGNLREFLRARrppGEEAspddprvpeEQLTQKDLVSFAYQVARGMEYLASK--KCIHRDLAARNVLVTEDNVM 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 218 KLSDFGLAKDGPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSgrravdknrPSGernlvewaKP 297
Cdd:cd05053 173 KIADFGLARDIHHIDYYRKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFT---------LGG--------SP 235
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15222437 298 YL-VNKRKIFRVidnrLQDQYSMEEA--C--KVATLSLRCLTTEIKLRPNMSEVVSHLEHI 353
Cdd:cd05053 236 YPgIPVEELFKL----LKEGHRMEKPqnCtqELYMLMRDCWHEVPSQRPTFKQLVEDLDRI 292
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
68-276 9.40e-18

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: 83.50  E-value: 9.40e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  68 FRPDSVLGEGGFGcvfkgwideKSLTASRPGTGLVIAVKKLNQdgwqghQEWLA--EVNYL----------GQFSHRHLV 135
Cdd:cd05589   1 FRCIAVLGRGHFG---------KVLLAEYKPTGELFAIKALKK------GDIIArdEVESLmcekrifetvNSARHPFLV 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 136 KLIGyCLE-DEHRLLVYEFMPRGSLENHL----F--RRGLYFQPLswklrlkVALGaakgLAFLHssETRVIYRDFKTSN 208
Cdd:cd05589  66 NLFA-CFQtPEHVCFVMEYAAGGDLMMHIhedvFsePRAVFYAAC-------VVLG----LQFLH--EHKIVYRDLKLDN 131
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15222437 209 ILLDSEYNAKLSDFGLAKDGpIGDKSHVSTrVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd05589 132 LLLDTEGYVKIADFGLCKEG-MGFGDRTST-FCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVG 197
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
74-277 1.65e-17

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: 81.86  E-value: 1.65e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWIDEKSltasrpgtglVIAVKKLNQdGWQGHQEWLAEVNYLGQFSHRHLVKLIGyCLEDEHRLLVYEF 153
Cdd:cd05067  15 LGAGQFGEVWMGYYNGHT----------KVAIKSLKQ-GSMSPDAFLAEANLMKQLQHQRLVRLYA-VVTQEPIYIITEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 154 MPRGSLENHLFRRGLYFQPLSwKLrLKVALGAAKGLAFLHssETRVIYRDFKTSNILLDSEYNAKLSDFGLAKdgpIGDK 233
Cdd:cd05067  83 MENGSLVDFLKTPSGIKLTIN-KL-LDMAAQIAEGMAFIE--ERNYIHRDLRAANILVSDTLSCKIADFGLAR---LIED 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15222437 234 SHVSTRVMGTH--GYAAPEYLATGHLTTKSDVYSFGVVLLELLS-GR 277
Cdd:cd05067 156 NEYTAREGAKFpiKWTAPEAINYGTFTIKSDVWSFGILLTEIVThGR 202
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
67-276 2.05e-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: 82.10  E-value: 2.05e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGCVFKGwIDEksltasrPGTGLVIAVK-----KLNQDGWQGHQ--EWLAEVNYLGQFSHRHLVKLIG 139
Cdd:cd14096   2 NYRLINKIGEGAFSNVYKA-VPL-------RNTGKPVAIKvvrkaDLSSDNLKGSSraNILKEVQIMKRLSHPNIVKLLD 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 140 YCLEDEHRLLVYEFMPRGSLENHLFRRgLYFqplSWKLRLKVALGAAKGLAFLHssETRVIYRDFKTSNILLDS-EYN-- 216
Cdd:cd14096  74 FQESDEYYYIVLELADGGEIFHQIVRL-TYF---SEDLSRHVITQVASAVKYLH--EIGVVHRDIKPENLLFEPiPFIps 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 217 ------------------------------AKLSDFGLAKdgpIGDKSHVSTRVmGTHGYAAPEYLATGHLTTKSDVYSF 266
Cdd:cd14096 148 ivklrkadddetkvdegefipgvggggigiVKLADFGLSK---QVWDSNTKTPC-GTVGYTAPEVVKDERYSKKVDMWAL 223
                       250
                ....*....|
gi 15222437 267 GVVLLELLSG 276
Cdd:cd14096 224 GCVLYTLLCG 233
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
74-273 2.19e-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: 81.34  E-value: 2.19e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFkgwidekslTASRPGTGLVIAVKKLNQDGWQGHQEW---LAEVNYLGQFSHRHLVKLIGYCLEDEHRLLV 150
Cdd:cd06607   9 IGHGSFGAVY---------YARNKRTSEVVAIKKMSYSGKQSTEKWqdiIKEVKFLRQLRHPNTIEYKGCYLREHTAWLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 151 YEFMpRGS----LENHlfRRGLYFQPLSwklrlKVALGAAKGLAFLHSSETrvIYRDFKTSNILLDSEYNAKLSDFGLAk 226
Cdd:cd06607  80 MEYC-LGSasdiVEVH--KKPLQEVEIA-----AICHGALQGLAYLHSHNR--IHRDVKAGNILLTEPGTVKLADFGSA- 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15222437 227 dgpigdkSHVS--TRVMGTHGYAAPEY-LAT--GHLTTKSDVYSFGVVLLEL 273
Cdd:cd06607 149 -------SLVCpaNSFVGTPYWMAPEViLAMdeGQYDGKVDVWSLGITCIEL 193
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
73-277 2.66e-17

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: 82.35  E-value: 2.66e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGcvfkgwideKSLTASRPGTGLVIAVKKLNQDGWQGHQE---WLAEVNYLGQFSHRHLVKLIGYCLEDEHRL- 148
Cdd:cd05616   7 VLGKGSFG---------KVMLAERKGTDELYAVKILKKDVVIQDDDvecTMVEKRVLALSGKPPFLTQLHSCFQTMDRLy 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 LVYEFMPRGSLENHLFRRGLYFQPLSWKLRLKVALGaakgLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAKDG 228
Cdd:cd05616  78 FVMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIG----LFFLQSKG--IIYRDLKLDNVMLDSEGHIKIADFGMCKEN 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15222437 229 pIGDKshVSTRVM-GTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd05616 152 -IWDG--VTTKTFcGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQ 198
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
63-277 3.12e-17

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: 81.59  E-value: 3.12e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  63 SATRNFRPDSVLGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQ----DGWqgHQEWLAEVNYLGQFSHRHLVKLI 138
Cdd:cd07866   5 SKLRDYEILGKLGEGTFGEVYK---------ARQIKTGRVVALKKILMhnekDGF--PITALREIKILKKLKHPNVVPLI 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 139 GYCLE--DEH---RLLVYEFMP------RGSLENHLFRrglyFQPLSWKLRLKVALgaaKGLAFLHSSetRVIYRDFKTS 207
Cdd:cd07866  74 DMAVErpDKSkrkRGSVYMVTPymdhdlSGLLENPSVK----LTESQIKCYMLQLL---EGINYLHEN--HILHRDIKAA 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 208 NILLDSEYNAKLSDFGLAK--DGPI---GDKSHVSTR----VMGTHGYAAPEYLA-TGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd07866 145 NILIDNQGILKIADFGLARpyDGPPpnpKGGGGGGTRkytnLVVTRWYRPPELLLgERRYTTAVDIWGIGCVFAEMFTRR 224
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
72-276 3.46e-17

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: 81.68  E-value: 3.46e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  72 SVLGEGGFGCVFKgwidEKSLTASRPGTglVIAVKKL-------NQDGwQGHQEwlAEVNYLGQFSHRHLVKLIgYCLED 144
Cdd:cd05584   2 KVLGKGGYGKVFQ----VRKTTGSDKGK--IFAMKVLkkasivrNQKD-TAHTK--AERNILEAVKHPFIVDLH-YAFQT 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 145 EHRL-LVYEFMPRGSLENHLFRRGLYFQPLSwKLRLkvalgAAKGLAFLHSSETRVIYRDFKTSNILLDSEYNAKLSDFG 223
Cdd:cd05584  72 GGKLyLILEYLSGGELFMHLEREGIFMEDTA-CFYL-----AEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFG 145
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15222437 224 LAKDGpiGDKSHVSTRVMGTHGYAAPEYLA-TGHltTKS-DVYSFGVVLLELLSG 276
Cdd:cd05584 146 LCKES--IHDGTVTHTFCGTIEYMAPEILTrSGH--GKAvDWWSLGALMYDMLTG 196
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
73-277 3.83e-17

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: 81.53  E-value: 3.83e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGcvfkgwideKSLTASRPGTGLVIAVKKLNQDGWQGHQE---WLAEVNYLG-QFSHRHLVKLIGYCLEDEHRL 148
Cdd:cd05620   2 VLGKGSFG---------KVLLAELKGKGEYFAVKALKKDVVLIDDDvecTMVEKRVLAlAWENPFLTHLYCTFQTKEHLF 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 LVYEFMPRGSLENHLFRRG---LYfqplswklrlKVALGAAK---GLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDF 222
Cdd:cd05620  73 FVMEFLNGGDLMFHIQDKGrfdLY----------RATFYAAEivcGLQFLHSKG--IIYRDLKLDNVMLDRDGHIKIADF 140
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15222437 223 GLAKDGPIGDKShvSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd05620 141 GMCKENVFGDNR--ASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQ 193
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
68-349 4.30e-17

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: 80.89  E-value: 4.30e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  68 FRPDSVLGEGGFGCVFKGwIDEKsltasrpgTGLVIAVKKLNQDGWQGHQEWLA-EVNYLGQFSHRHLVKLIGYCLEDEH 146
Cdd:cd06641   6 FTKLEKIGKGSFGEVFKG-IDNR--------TQKVVAIKIIDLEEAEDEIEDIQqEITVLSQCDSPYVTKYYGSYLKDTK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 147 RLLVYEFMPRGSLENhLFRRGlyfqPLSWKLRLKVALGAAKGLAFLHSSETrvIYRDFKTSNILLDSEYNAKLSDFGLAk 226
Cdd:cd06641  77 LWIIMEYLGGGSALD-LLEPG----PLDETQIATILREILKGLDYLHSEKK--IHRDIKAANVLLSEHGEVKLADFGVA- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 227 dGPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVDKNRPSGERNLVEWAKPYLvnkrkif 306
Cdd:cd06641 149 -GQLTDTQIKRN*FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIPKNNPPT------- 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 15222437 307 rvidnrLQDQYS--MEEACKVatlslrCLTTEIKLRPNMSEVVSH 349
Cdd:cd06641 221 ------LEGNYSkpLKEFVEA------CLNKEPSFRPTAKELLKH 253
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
74-275 4.42e-17

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: 80.31  E-value: 4.42e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKG-WIDEKSltasrpgtglvIAVKKLnQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYE 152
Cdd:cd05113  12 LGTGQFGVVKYGkWRGQYD-----------VAIKMI-KEGSMSEDEFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMPRGSLENHLFRRGLYFQPLSWklrLKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAKdgPIGD 232
Cdd:cd05113  80 YMANGCLLNYLREMRKRFQTQQL---LEMCKDVCEAMEYLESKQ--FLHRDLAARNCLVNDQGVVKVSDFGLSR--YVLD 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15222437 233 KSHVSTrvMGTH---GYAAPEYLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:cd05113 153 DEYTSS--VGSKfpvRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYS 196
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
75-278 6.13e-17

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: 80.04  E-value: 6.13e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  75 GEGGFGCVFkgwidekslTASRPGTGLVIAVKKLN-QDG-WQGHQEWLAEVNYLGQFSHRHLVKLigYCLEdEHRLLVYE 152
Cdd:cd06626   9 GEGTFGKVY---------TAVNLDTGELMAMKEIRfQDNdPKTIKEIADEMKVLEGLDHPNLVRY--YGVE-VHREEVYI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FM---PRGSLEnHLFRRGLYFQPLSWKLRLKVALgaaKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAKDGP 229
Cdd:cd06626  77 FMeycQEGTLE-ELLRHGRILDEAVIRVYTLQLL---EGLAYLHEN--GIVHRDIKPANIFLDSNGLIKLGDFGSAVKLK 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15222437 230 IGDKSHVSTRV---MGTHGYAAPEYL----ATGHLTTkSDVYSFGVVLLELLSGRR 278
Cdd:cd06626 151 NNTTTMAPGEVnslVGTPAYMAPEVItgnkGEGHGRA-ADIWSLGCVVLEMATGKR 205
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
67-281 6.21e-17

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: 79.90  E-value: 6.21e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGCVFKGwideKSLTasrpgTGLVIAVKKLNQDGWQGH---QEWLAEVNYLGQFSHRHLVKLIGYCLE 143
Cdd:cd14186   2 DFKVLNLLGKGSFACVYRA----RSLH-----TGLEVAIKMIDKKAMQKAgmvQRVRNEVEIHCQLKHPSILELYNYFED 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 144 DEHRLLVYEFMPRGSLENHLFRRGlyfQPLSWKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFG 223
Cdd:cd14186  73 SNYVYLVLEMCHNGEMSRYLKNRK---KPFTEDEARHFMHQIVTGMLYLHSHG--ILHRDLTLSNLLLTRNMNIKIADFG 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15222437 224 LAKDGPIGDKSHVStrVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVD 281
Cdd:cd14186 148 LATQLKMPHEKHFT--MCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFD 203
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
73-277 7.28e-17

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: 80.33  E-value: 7.28e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKgwIDEKSltasrpgTGLVIAVKKLNQDGWQ---GHQEWLAEVNYLGQFSHRHLVKLiGYCLEDE-HRL 148
Cdd:cd05607   9 VLGKGGFGEVCA--VQVKN-------TGQMYACKKLDKKRLKkksGEKMALLEKEILEKVNSPFIVSL-AYAFETKtHLC 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 LVYEFMPRGSLENHLF---RRGLyfqplswKLRLKVALGAAKGLAFLHSSETRVIYRDFKTSNILLDSEYNAKLSDFGLA 225
Cdd:cd05607  79 LVMSLMNGGDLKYHIYnvgERGI-------EMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLA 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15222437 226 KDGPIGDKshvSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd05607 152 VEVKEGKP---ITQRAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGR 200
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
131-276 7.54e-17

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: 79.84  E-value: 7.54e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 131 HRHLVKLIGYCLEDEHR-------LLVYEFMPRgSLENHLfRRGLyfqplSWKLRLKVALGAAKGLAFLHSSEtrVIYRD 203
Cdd:cd13975  57 HERIVSLHGSVIDYSYGggssiavLLIMERLHR-DLYTGI-KAGL-----SLEERLQIALDVVEGIRFLHSQG--LVHRD 127
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15222437 204 FKTSNILLDSEYNAKLSDFGLAKdgpigDKSHVSTRVMGTHGYAAPEyLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd13975 128 IKLKNVLLDKKNRAKITDLGFCK-----PEAMMSGSIVGTPIHMAPE-LFSGKYDNSVDVYAFGILFWYLCAG 194
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
74-276 7.56e-17

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: 80.07  E-value: 7.56e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKgwideksltASRPGTGLVIAVKKL---NQDGWQGHQeWLAEVNYLGQF-SHRHLVKLIGYCLEDEHRLL 149
Cdd:cd07832   8 IGEGAHGIVFK---------AKDRETGETVALKKValrKLEGGIPNQ-ALREIKALQACqGHPYVVKLRDVFPHGTGFVL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 150 VYEFMPRgSLENHLfrrGLYFQPLS---WKLRLKVALgaaKGLAFLHssETRVIYRDFKTSNILLDSEYNAKLSDFGLAK 226
Cdd:cd07832  78 VFEYMLS-SLSEVL---RDEERPLTeaqVKRYMRMLL---KGVAYMH--ANRIMHRDLKPANLLISSTGVLKIADFGLAR 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15222437 227 DGPIGDKSHVSTRVmGTHGYAAPEYL-ATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd07832 149 LFSEEDPRLYSHQV-ATRWYRAPELLyGSRKYDEGVDLWAVGCIFAELLNG 198
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
73-277 8.10e-17

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: 80.51  E-value: 8.10e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGcvfkgwideKSLTASRPGTGLVIAVKKLNQD--------------------GWQghqewlaevnylgqfsHR 132
Cdd:cd05592   2 VLGKGSFG---------KVMLAELKGTNQYFAIKALKKDvvledddvectmierrvlalASQ----------------HP 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 133 HLVKLigYCL--EDEHRLLVYEFMPRGSLENHLFRRGlyfqplswKLRLKVA-LGAAK---GLAFLHSSEtrVIYRDFKT 206
Cdd:cd05592  57 FLTHL--FCTfqTESHLFFVMEYLNGGDLMFHIQQSG--------RFDEDRArFYGAEiicGLQFLHSRG--IIYRDLKL 124
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15222437 207 SNILLDSEYNAKLSDFGLAKDGPIGDKShvSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd05592 125 DNVLLDREGHIKIADFGMCKENIYGENK--ASTFCGTPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQ 193
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
60-277 8.67e-17

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: 80.48  E-value: 8.67e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  60 ELKSatRNFRPDSVLGEGGFGCVFKgwidekslTASRPgTGLVIAVKKLNQDGWQG-HQEWLAEVNYLGQFSHRHLVKLI 138
Cdd:cd06650   1 ELKD--DDFEKISELGAGNGGVVFK--------VSHKP-SGLVMARKLIHLEIKPAiRNQIIRELQVLHECNSPYIVGFY 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 139 GYCLEDEHRLLVYEFMPRGSLENHLFRRGlyfqPLSWKLRLKVALGAAKGLAFLHSSEtRVIYRDFKTSNILLDSEYNAK 218
Cdd:cd06650  70 GAFYSDGEISICMEHMDGGSLDQVLKKAG----RIPEQILGKVSIAVIKGLTYLREKH-KIMHRDVKPSNILVNSRGEIK 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15222437 219 LSDFGLAkdGPIGDKshVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd06650 145 LCDFGVS--GQLIDS--MANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGR 199
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
67-278 8.69e-17

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: 79.61  E-value: 8.69e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGCVfkgWIDEKSltasrpGTGLVIAVKKLNQ---DGWQGHQEWLAEVNYLGQFSHRHLVKLIgYCLE 143
Cdd:cd05578   1 HFQILRVIGKGSFGKV---CIVQKK------DTKKMFAMKYMNKqkcIEKDSVRNVLNELEILQELEHPFLVNLW-YSFQ 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 144 DEHRL-LVYEFMPRGSLENHLFRRGlYFQPLSWKLRLkVALGAAkgLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDF 222
Cdd:cd05578  71 DEEDMyMVVDLLLGGDLRYHLQQKV-KFSEETVKFYI-CEIVLA--LDYLHSK--NIIHRDIKPDNILLDEQGHVHITDF 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15222437 223 GLAKDGPigdKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRR 278
Cdd:cd05578 145 NIATKLT---DGTLATSTSGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKR 197
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
74-275 9.56e-17

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: 80.06  E-value: 9.56e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGwiDEKSLTASRPGTGLVIAVKKLNQDGWQGH-QEWLAEVNYLGQF-SHRHLVKLIGYCLEDEHRLLVY 151
Cdd:cd05098  21 LGEGCFGQVVLA--EAIGLDKDKPNRVTKVAVKMLKSDATEKDlSDLISEMEMMKMIgKHKNIINLLGACTQDGPLYVIV 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 152 EFMPRGSLENHLFRR---GLYF---------QPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKL 219
Cdd:cd05098  99 EYASKGNLREYLQARrppGMEYcynpshnpeEQLSSKDLVSCAYQVARGMEYLASK--KCIHRDLAARNVLVTEDNVMKI 176
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15222437 220 SDFGLAKdgpigDKSHVSTRVMGTHG-----YAAPEYLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:cd05098 177 ADFGLAR-----DIHHIDYYKKTTNGrlpvkWMAPEALFDRIYTHQSDVWSFGVLLWEIFT 232
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
66-273 1.12e-16

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: 80.08  E-value: 1.12e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  66 RNFRPDSV------LGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIG 139
Cdd:cd06644   6 RDLDPNEVweiigeLGDGAFGKVYK---------AKNKETGALAAAKVIETKSEEELEDYMVEIEILATCNHPYIVKLLG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 140 YCLEDEHRLLVYEFMPRGSLENHLFR--RGLyfQPLSWKLRLKVALGAakgLAFLHSseTRVIYRDFKTSNILLDSEYNA 217
Cdd:cd06644  77 AFYWDGKLWIMIEFCPGGAVDAIMLEldRGL--TEPQIQVICRQMLEA---LQYLHS--MKIIHRDLKAGNVLLTLDGDI 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15222437 218 KLSDFGL-AKDGPIGDKshvSTRVMGTHGYAAPEYLATGHLTT-----KSDVYSFGVVLLEL 273
Cdd:cd06644 150 KLADFGVsAKNVKTLQR---RDSFIGTPYWMAPEVVMCETMKDtpydyKADIWSLGITLIEM 208
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
67-280 1.15e-16

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: 79.86  E-value: 1.15e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQDGWQGHQEWLA--EVNYLGQFSHRHLVKLIGYCLED 144
Cdd:cd07860   1 NFQKVEKIGEGTYGVVYK---------ARNKLTGEVVALKKIRLDTETEGVPSTAirEISLLKELNHPNIVKLLDVIHTE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 145 EHRLLVYEFM-----------PRGSLENHLFRRGLyFQPLSwklrlkvalgaakGLAFLHSSetRVIYRDFKTSNILLDS 213
Cdd:cd07860  72 NKLYLVFEFLhqdlkkfmdasALTGIPLPLIKSYL-FQLLQ-------------GLAFCHSH--RVLHRDLKPQNLLINT 135
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15222437 214 EYNAKLSDFGLAKDGPIGDKSHVSTRVmgTHGYAAPE-YLATGHLTTKSDVYSFGVVLLELLSgRRAV 280
Cdd:cd07860 136 EGAIKLADFGLARAFGVPVRTYTHEVV--TLWYRAPEiLLGCKYYSTAVDIWSLGCIFAEMVT-RRAL 200
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
98-349 1.16e-16

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: 79.40  E-value: 1.16e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  98 GTGLVIAVKKLNQ-DGWQGHQEWLA-----EVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEFMPRGSLENHLFRRGlyfq 171
Cdd:cd06630  23 KTGTLMAVKQVSFcRNSSSEQEEVVeaireEIRMMARLNHPNIVRMLGATQHKSHFNIFVEWMAGGSVASLLSKYG---- 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 172 PLSWKLRLKVALGAAKGLAFLHssETRVIYRDFKTSNILLDSE-YNAKLSDFG----LAKDGPIGDKshVSTRVMGTHGY 246
Cdd:cd06630  99 AFSENVIINYTLQILRGLAYLH--DNQIIHRDLKGANLLVDSTgQRLRIADFGaaarLASKGTGAGE--FQGQLLGTIAF 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 247 AAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVDKNRPSGERNLvewakpylvnkrkIFRVIDNrlQDQYSMEEACKVA 326
Cdd:cd06630 175 MAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEKISNHLAL-------------IFKIASA--TTPPPIPEHLSPG 239
                       250       260
                ....*....|....*....|....*
gi 15222437 327 T--LSLRCLTTEIKLRPNMSEVVSH 349
Cdd:cd06630 240 LrdVTLRCLELQPEDRPPARELLKH 264
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
186-277 1.16e-16

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: 79.26  E-value: 1.16e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 186 AKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAK--------------DGPIGDKSHVSTRVMGTHGYAAPEY 251
Cdd:cd14010 104 VRGLHYIHSKG--IIYCDLKPSNILLDGNGTLKLSDFGLARregeilkelfgqfsDEGNVNKVSKKQAKRGTPYYMAPEL 181
                        90       100
                ....*....|....*....|....*.
gi 15222437 252 LATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd14010 182 FQGGVHSFASDLWALGCVLYEMFTGK 207
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
71-275 1.30e-16

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


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 79.66  E-value: 1.30e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  71 DSVLGEGGFGCVFKGWIdeksltaSRPGTGLVIAVKKLNQDGWQG-HQEWLAEVNYLGQFSHR-HLVKLIGYCLEDEHRL 148
Cdd:cd05089   7 EDVIGEGNFGQVIKAMI-------KKDGLKMNAAIKMLKEFASENdHRDFAGELEVLCKLGHHpNIINLLGACENRGYLY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 LVYEFMPRGSLENHLFR-RGLYFQP-----------LSWKLRLKVALGAAKGLAFLhsSETRVIYRDFKTSNILLDSEYN 216
Cdd:cd05089  80 IAIEYAPYGNLLDFLRKsRVLETDPafakehgtastLTSQQLLQFASDVAKGMQYL--SEKQFIHRDLAARNVLVGENLV 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15222437 217 AKLSDFGLAKdgpiGDKSHVStRVMGTHG--YAAPEYLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:cd05089 158 SKIADFGLSR----GEEVYVK-KTMGRLPvrWMAIESLNYSVYTTKSDVWSFGVLLWEIVS 213
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
72-277 1.34e-16

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: 79.50  E-value: 1.34e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  72 SVLGEGGFGCVFKGwiDEKSltasrpgTGLVIAVKKLNQDgwqgHQEW-----LAEVNYLGQF-SHRHLVKLIGYCLEDE 145
Cdd:cd07830   5 KQLGDGTFGSVYLA--RNKE-------TGELVAIKKMKKK----FYSWeecmnLREVKSLRKLnEHPNIVKLKEVFREND 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 146 HRLLVYEFMprgslENHLF-----RRGLYFQPLSWKLRLKVALgaaKGLAFLHSseTRVIYRDFKTSNILLDSEYNAKLS 220
Cdd:cd07830  72 ELYFVFEYM-----EGNLYqlmkdRKGKPFSESVIRSIIYQIL---QGLAHIHK--HGFFHRDLKPENLLVSGPEVVKIA 141
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15222437 221 DFGLAKDgpIGDK----SHVSTRvmgthGYAAPE-YLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd07830 142 DFGLARE--IRSRppytDYVSTR-----WYRAPEiLLRSTSYSSPVDIWALGCIMAELYTLR 196
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
62-277 1.39e-16

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


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 80.35  E-value: 1.39e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  62 KSATRNFRPDSVLGEGGFGCVFkgwidekslTASRPGTGLVIAVKKLNQDGWQGHQE---WLAEVNYLG-QFSHRHLVKL 137
Cdd:cd05619   1 KLTIEDFVLHKMLGKGSFGKVF---------LAELKGTNQFFAIKALKKDVVLMDDDvecTMVEKRVLSlAWEHPFLTHL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 138 IGYCLEDEHRLLVYEFMPRGSLENHLFRRGLYFQPLSWKLRLKVALGaakgLAFLHSSEtrVIYRDFKTSNILLDSEYNA 217
Cdd:cd05619  72 FCTFQTKENLFFVMEYLNGGDLMFHIQSCHKFDLPRATFYAAEIICG----LQFLHSKG--IVYRDLKLDNILLDKDGHI 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 218 KLSDFGLAKDGPIGDKShvSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd05619 146 KIADFGMCKENMLGDAK--TSTFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQ 203
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
74-276 1.72e-16

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: 78.64  E-value: 1.72e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVfkgwideksLTASRPGTGLVIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEF 153
Cdd:cd06648  15 IGEGSTGIV---------CIATDKSTGRQVAVKKMDLRKQQRRELLFNEVVIMRDYQHPNIVEMYSSYLVGDELWVVMEF 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 154 MPRGSLENHLFRRGLYFQPLSwklrlKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFG----LAKDGP 229
Cdd:cd06648  86 LEGGALTDIVTHTRMNEEQIA-----TVCRAVLKALSFLHSQ--GVIHRDIKSDSILLTSDGRVKLSDFGfcaqVSKEVP 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15222437 230 iGDKSHVstrvmGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd06648 159 -RRKSLV-----GTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDG 199
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
68-276 1.93e-16

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: 78.83  E-value: 1.93e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  68 FRPDSVLGEGGFGCVFKGwIDEKsltasrpgTGLVIAVKKLNQDGWQGHQEWLA-EVNYLGQFSHRHLVKLIGYCLEDEH 146
Cdd:cd06609   3 FTLLERIGKGSFGEVYKG-IDKR--------TNQVVAIKVIDLEEAEDEIEDIQqEIQFLSQCDSPYITKYYGSFLKGSK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 147 RLLVYEFMPRGSLENHLFRRGLYFQPLSWKLR--LKvalgaakGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGL 224
Cdd:cd06609  74 LWIIMEYCGGGSVLDLLKPGPLDETYIAFILRevLL-------GLEYLHSE--GKIHRDIKAANILLSEEGDVKLADFGV 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15222437 225 AkdgpiGDKSHVSTR---VMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd06609 145 S-----GQLTSTMSKrntFVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKG 194
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
67-275 1.94e-16

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: 78.53  E-value: 1.94e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGCVFKGWIDEksltasrpgTGLVIAVKKLNQDgwQGHQEWLAEVN-------YLGQFSHRHLVKLIG 139
Cdd:cd06653   3 NWRLGKLLGRGAFGEVYLCYDAD---------TGRELAVKQVPFD--PDSQETSKEVNaleceiqLLKNLRHDRIVQYYG 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 140 yCLED--EHRLLVY-EFMPRGSLENHLFRRGlyfqPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYN 216
Cdd:cd06653  72 -CLRDpeEKKLSIFvEYMPGGSVKDQLKAYG----ALTENVTRRYTRQILQGVSYLHSN--MIVHRDIKGANILRDSAGN 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 217 AKLSDFGLAKDGPIGDKSHVSTR-VMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:cd06653 145 VKLGDFGASKRIQTICMSGTGIKsVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLT 204
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
74-275 2.13e-16

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: 78.54  E-value: 2.13e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWIDEKSltasrpgtglVIAVKKLnQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEF 153
Cdd:cd05072  15 LGAGQFGEVWMGYYNNST----------KVAVKTL-KPGTMSVQAFLEEANLMKTLQHDKLVRLYAVVTKEEPIYIITEY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 154 MPRGSLENHLFRR--GLYFQPLSWKLRLKVAlgaaKGLAFLHssETRVIYRDFKTSNILLDSEYNAKLSDFGLAKdgPIG 231
Cdd:cd05072  84 MAKGSLLDFLKSDegGKVLLPKLIDFSAQIA----EGMAYIE--RKNYIHRDLRAANVLVSESLMCKIADFGLAR--VIE 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15222437 232 DKSHVSTRvmGTH---GYAAPEYLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:cd05072 156 DNEYTARE--GAKfpiKWTAPEAINFGSFTIKSDVWSFGILLYEIVT 200
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
74-275 2.16e-16

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: 79.24  E-value: 2.16e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGwiDEKSLTASRPGTGLVIAVKKLNQDGW-QGHQEWLAEVNYLGQFS-HRHLVKLIGYCLEDEHRLLVY 151
Cdd:cd05099  20 LGEGCFGQVVRA--EAYGIDKSRPDQTVTVAVKMLKDNATdKDLADLISEMELMKLIGkHKNIINLLGVCTQEGPLYVIV 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 152 EFMPRGSLENHLFRR------------GLYFQPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKL 219
Cdd:cd05099  98 EYAAKGNLREFLRARrppgpdytfditKVPEEQLSFKDLVSCAYQVARGMEYLESR--RCIHRDLAARNVLVTEDNVMKI 175
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15222437 220 SDFGLAKDGPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:cd05099 176 ADFGLARGVHDIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILMWEIFT 231
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
72-319 2.45e-16

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: 78.55  E-value: 2.45e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  72 SVLGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQDGWQGHQ-------EWLAEVNYLGQFS-HRHLVKLIGYCLE 143
Cdd:cd13993   6 SPIGEGAYGVVYL---------AVDLRTGRKYAIKCLYKSGPNSKDgndfqklPQLREIDLHRRVSrHPNIITLHDVFET 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 144 DEHRLLVYEFMPRGSLENHLFRRGLYfqPLSWKLRLKVALGAAKGLAFLHSsetRVIY-RDFKTSNILLD-SEYNAKLSD 221
Cdd:cd13993  77 EVAIYIVLEYCPNGDLFEAITENRIY--VGKTELIKNVFLQLIDAVKHCHS---LGIYhRDIKPENILLSqDEGTVKLCD 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 222 FGLAKDGPIgdKSHVSTrvmGTHGYAAPEYL------ATGHLTTKSDVYSFGVVLLELLSGR---RAVDKNRPSGERnlv 292
Cdd:cd13993 152 FGLATTEKI--SMDFGV---GSEFYMAPECFdevgrsLKGYPCAAGDIWSLGIILLNLTFGRnpwKIASESDPIFYD--- 223
                       250       260
                ....*....|....*....|....*..
gi 15222437 293 ewakpYLVNKRKIFRVIDNRLQDQYSM 319
Cdd:cd13993 224 -----YYLNSPNLFDVILPMSDDFYNL 245
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
67-277 2.48e-16

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: 78.55  E-value: 2.48e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGCVFKGWIDEksltasrpgTGLVIAVKKL--NQDGWQGHQEWLA---EVNYLGQFSHRHLVKLIGyC 141
Cdd:cd06652   3 NWRLGKLLGQGAFGRVYLCYDAD---------TGRELAVKQVqfDPESPETSKEVNAlecEIQLLKNLLHERIVQYYG-C 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 142 LED--EHRLLVY-EFMPRGSLENHLFRRGlyfqPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAK 218
Cdd:cd06652  73 LRDpqERTLSIFmEYMPGGSIKDQLKSYG----ALTENVTRKYTRQILEGVHYLHSN--MIVHRDIKGANILRDSVGNVK 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15222437 219 LSDFGLAKD------GPIGDKShvstrVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd06652 147 LGDFGASKRlqticlSGTGMKS-----VTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEK 206
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
68-293 2.54e-16

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: 78.88  E-value: 2.54e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  68 FRPDSVLGEGGFGCVfkgwideksLTASRPGTGLVIAVKKLNQD---GWQGHQEWLAEVNYLGQFSHRHLVKLiGYCLED 144
Cdd:cd05631   2 FRHYRVLGKGGFGEV---------CACQVRATGKMYACKKLEKKrikKRKGEAMALNEKRILEKVNSRFVVSL-AYAYET 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 145 EHRL-LVYEFMPRGSLENHLFRRGlyfQP-LSWKLRLKVALGAAKGLAFLHssETRVIYRDFKTSNILLDSEYNAKLSDF 222
Cdd:cd05631  72 KDALcLVLTIMNGGDLKFHIYNMG---NPgFDEQRAIFYAAELCCGLEDLQ--RERIVYRDLKPENILLDDRGHIRISDL 146
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15222437 223 GLAKDGPIGDKshVSTRVmGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVDKNRPSGERNLVE 293
Cdd:cd05631 147 GLAVQIPEGET--VRGRV-GTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKERVKREEVD 214
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
72-277 2.94e-16

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: 79.27  E-value: 2.94e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  72 SVLGEGGFGCVFkgwidekslTASRPGTGLVIAVKKLNQDGWQGH-QEWLAEVNYLGQFSHRHLVK----LIGYCLEDEH 146
Cdd:cd07849  11 SYIGEGAYGMVC---------SAVHKPTGQKVAIKKISPFEHQTYcLRTLREIKILLRFKHENIIGildiQRPPTFESFK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 147 RL-LVYEFMprgslENHLFRRgLYFQPLSWK---------LRlkvalgaakGLAFLHSSEtrVIYRDFKTSNILLDSEYN 216
Cdd:cd07849  82 DVyIVQELM-----ETDLYKL-IKTQHLSNDhiqyflyqiLR---------GLKYIHSAN--VLHRDLKPSNLLLNTNCD 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15222437 217 AKLSDFGLAKdgpIGDKSHVSTRVM----GTHGYAAPEYLATGHLTTKS-DVYSFGVVLLELLSGR 277
Cdd:cd07849 145 LKICDFGLAR---IADPEHDHTGFLteyvATRWYRAPEIMLNSKGYTKAiDIWSVGCILAEMLSNR 207
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
68-277 3.04e-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: 78.55  E-value: 3.04e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  68 FRPDSVLGEGGFGCVFKgwidekslTASRpGTGLVIAVKKLNQDGWQG-HQEWLA--EVNYLGQFSHRHLVKLiGYCLED 144
Cdd:cd05605   2 FRQYRVLGKGGFGEVCA--------CQVR-ATGKMYACKKLEKKRIKKrKGEAMAlnEKQILEKVNSRFVVSL-AYAYET 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 145 EHRL-LVYEFMPRGSLENHLFRRGlyfQP-LSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDF 222
Cdd:cd05605  72 KDALcLVLTIMNGGDLKFHIYNMG---NPgFEEERAVFYAAEITCGLEHLHSE--RIVYRDLKPENILLDDHGHVRISDL 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15222437 223 GLAKDGPIGDKshVSTRVmGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd05605 147 GLAVEIPEGET--IRGRV-GTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQ 198
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
74-275 3.10e-16

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: 79.29  E-value: 3.10e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGwiDEKSLTASRPGTGLVIAVKKLNQDGW-QGHQEWLAEVNYLGQF-SHRHLVKLIGYCLEDEHRLLVY 151
Cdd:cd05100  20 LGEGCFGQVVMA--EAIGIDKDKPNKPVTVAVKMLKDDATdKDLSDLVSEMEMMKMIgKHKNIINLLGACTQDGPLYVLV 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 152 EFMPRGSLENHLFRR---GLYF---------QPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKL 219
Cdd:cd05100  98 EYASKGNLREYLRARrppGMDYsfdtcklpeEQLTFKDLVSCAYQVARGMEYLASQ--KCIHRDLAARNVLVTEDNVMKI 175
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15222437 220 SDFGLAKDGPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:cd05100 176 ADFGLARDVHNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFT 231
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
74-277 3.13e-16

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: 78.25  E-value: 3.13e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEF 153
Cdd:cd06611  13 LGDGAFGKVYK---------AQHKETGLFAAAKIIQIESEEELEDFMVEIDILSECKHPNIVGLYEAYFYENKLWILIEF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 154 MPRGSLENHLFR--RGL---YFQPLSWKLrlkvalgaAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAKDG 228
Cdd:cd06611  84 CDGGALDSIMLEleRGLtepQIRYVCRQM--------LEALNFLHSH--KVIHRDLKAGNILLTLDGDVKLADFGVSAKN 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15222437 229 PIGDKSHVStrVMGTHGYAAPEYLATGHLTT-----KSDVYSFGVVLLELLSGR 277
Cdd:cd06611 154 KSTLQKRDT--FIGTPYWMAPEVVACETFKDnpydyKADIWSLGITLIELAQME 205
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
73-276 3.32e-16

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


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 78.86  E-value: 3.32e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGcvfkgwideKSLTASRPGTGLVIAVKKLNQDGWQGHQEW---LAEVN-YLGQFSHRHLVKLiGYCLEDEHRL 148
Cdd:cd05603   2 VIGKGSFG---------KVLLAKRKCDGKFYAVKVLQKKTILKKKEQnhiMAERNvLLKNLKHPFLVGL-HYSFQTSEKL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 -LVYEFMPRGSLENHLFRRGLYFQPlswKLRLKVAlGAAKGLAFLHSseTRVIYRDFKTSNILLDSEYNAKLSDFGLAKD 227
Cdd:cd05603  72 yFVLDYVNGGELFFHLQRERCFLEP---RARFYAA-EVASAIGYLHS--LNIIYRDLKPENILLDCQGHVVLTDFGLCKE 145
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15222437 228 GPigDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd05603 146 GM--EPEETTSTFCGTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYG 192
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
77-276 3.33e-16

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: 78.03  E-value: 3.33e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  77 GGFGCVFkgwidekslTASRPGTGLVIAVKKLNQDGWQGH---QEWLAEVNYLGQFSHRHLVKLIgYCLEDEHRL-LVYE 152
Cdd:cd05579   4 GAYGRVY---------LAKKKSTGDLYAIKVIKKRDMIRKnqvDSVLAERNILSQAQNPFVVKLY-YSFQGKKNLyLVME 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMPRG----------SLENHLFRrgLYFQPLswklrlkvalgaAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDF 222
Cdd:cd05579  74 YLPGGdlysllenvgALDEDVAR--IYIAEI------------VLALEYLHSH--GIIHRDLKPDNILIDANGHLKLTDF 137
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15222437 223 GLAKDGPIGDKSHVS-------------TRVMGTHGYAAPE-YLATGHlTTKSDVYSFGVVLLELLSG 276
Cdd:cd05579 138 GLSKVGLVRRQIKLSiqkksngapekedRRIVGTPDYLAPEiLLGQGH-GKTVDWWSLGVILYEFLVG 204
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
68-272 3.45e-16

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: 78.23  E-value: 3.45e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  68 FRPDSVLGEGGFGCVFKgwidekslTASRPGTGLVIAVKKL--NQDGWQGHQEWLAEVNYLGQFS---HRHLVKLIGYCL 142
Cdd:cd14052   2 FANVELIGSGEFSQVYK--------VSERVPTGKVYAVKKLkpNYAGAKDRLRRLEEVSILRELTldgHDNIVQLIDSWE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 143 EDEHRLLVYEFMPRGSLENHLFRRGLYF---QPLSWKLRLKVALGaakgLAFLHSSEtrVIYRDFKTSNILLDSEYNAKL 219
Cdd:cd14052  74 YHGHLYIQTELCENGSLDVFLSELGLLGrldEFRVWKILVELSLG----LRFIHDHH--FVHLDLKPANVLITFEGTLKI 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15222437 220 SDFGLAKDGPIGDkshvSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLE 272
Cdd:cd14052 148 GDFGMATVWPLIR----GIEREGDREYIAPEILSEHMYDKPADIFSLGLILLE 196
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
73-275 3.61e-16

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: 78.14  E-value: 3.61e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKG-WIDEKSltasrpGTGLVIAVKKLNQD-GWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLlV 150
Cdd:cd05109  14 VLGSGAFGTVYKGiWIPDGE------NVKIPVAIKVLRENtSPKANKEILDEAYVMAGVGSPYVCRLLGICLTSTVQL-V 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 151 YEFMPRGSLENHLF----RRGLYFQpLSWKLRLkvalgaAKGLAFLHssETRVIYRDFKTSNILLDSEYNAKLSDFGLAK 226
Cdd:cd05109  87 TQLMPYGCLLDYVRenkdRIGSQDL-LNWCVQI------AKGMSYLE--EVRLVHRDLAARNVLVKSPNHVKITDFGLAR 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15222437 227 DGPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:cd05109 158 LLDIDETEYHADGGKVPIKWMALESILHRRFTHQSDVWSYGVTVWELMT 206
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
73-350 3.72e-16

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: 78.30  E-value: 3.72e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVfkgwIDEKSLTASRPGTGLVIAVKKLNQDGWQG-HQEWLAEVNYLGQFSHrHL--VKLIGYCLEDEHRLL 149
Cdd:cd05054  14 PLGRGAFGKV----IQASAFGIDKSATCRTVAVKMLKEGATASeHKALMTELKILIHIGH-HLnvVNLLGACTKPGGPLM 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 150 V-YEFMPRGSLENHLFRR----------------------GLYFQPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKT 206
Cdd:cd05054  89 ViVEFCKFGNLSNYLRSKreefvpyrdkgardveeeedddELYKEPLTLEDLICYSFQVARGMEFLASR--KCIHRDLAA 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 207 SNILLdSEYN-AKLSDFGLAKDgPIGDKSHV---STRVmgTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLS-Grravd 281
Cdd:cd05054 167 RNILL-SENNvVKICDFGLARD-IYKDPDYVrkgDARL--PLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSlG----- 237
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15222437 282 knrpsgernlvewAKPYL-VNKRKIFRvidNRLQDQYSMEE----ACKVATLSLRCLTTEIKLRPNMSEVVSHL 350
Cdd:cd05054 238 -------------ASPYPgVQMDEEFC---RRLKEGTRMRApeytTPEIYQIMLDCWHGEPKERPTFSELVEKL 295
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
73-281 4.25e-16

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: 78.89  E-value: 4.25e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGcvfkgwideKSLTASRPGTGLVIAVKKLNQDGWQGHQE---WLAEVNYLGQFSHRHLVKLIGYCLEDEHRL- 148
Cdd:cd05615  17 VLGKGSFG---------KVMLAERKGSDELYAIKILKKDVVIQDDDvecTMVEKRVLALQDKPPFLTQLHSCFQTVDRLy 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 LVYEFMPRGSLENHLFRRGLYFQPLSWKLRLKVALGaakgLAFLHssETRVIYRDFKTSNILLDSEYNAKLSDFGLAKDG 228
Cdd:cd05615  88 FVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISVG----LFFLH--KKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEH 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15222437 229 PIgdkSHVSTRVM-GTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVD 281
Cdd:cd05615 162 MV---EGVTTRTFcGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFD 212
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
68-273 5.04e-16

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: 77.35  E-value: 5.04e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  68 FRPDSVLGEGGFGCVFKgwidEKSLTasrpgTGLVIAVKKLNQ--DGWQGHQEWLAEVNYLGQFS-HRHLVKLIgYCLED 144
Cdd:cd14050   3 FTILSKLGEGSFGEVFK----VRSRE-----DGKLYAVKRSRSrfRGEKDRKRKLEEVERHEKLGeHPNCVRFI-KAWEE 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 145 EHRLLVYEFMPRGSLENHLFRrglyFQPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGL 224
Cdd:cd14050  73 KGILYIQTELCDTSLQQYCEE----THSLPESEVWNILLDLLKGLKHLHDH--GLIHLDIKPANIFLSKDGVCKLGDFGL 146
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15222437 225 AKDGPIGDKSHVSTrvmGTHGYAAPEYLaTGHLTTKSDVYSFGVVLLEL 273
Cdd:cd14050 147 VVELDKEDIHDAQE---GDPRYMAPELL-QGSFTKAADIFSLGITILEL 191
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
74-275 6.73e-16

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: 77.36  E-value: 6.73e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWIDEKSLTASRpgtglVIAVKKLNQ-DGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYE 152
Cdd:cd05090  13 LGECAFGKIYKGHLYLPGMDHAQ-----LVAIKTLKDyNNPQQWNEFQQEASLMTELHHPNIVCLLGVVTQEQPVCMLFE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMPRGSLENHLFRR-------------GLYFQPLSWKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKL 219
Cdd:cd05090  88 FMNQGDLHEFLIMRsphsdvgcssdedGTVKSSLDHGDFLHIAIQIAAGMEYLSSHF--FVHKDLAARNILVGEQLHVKI 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15222437 220 SDFGLAKDGPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:cd05090 166 SDLGLSREIYSSDYYRVQNKSLLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFS 221
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
73-281 7.07e-16

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: 77.38  E-value: 7.07e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKGWIDEKsltasrpgtglVIAVKKL---NQDGWQGHQEWLAEVNylgqFSHRHLVKLI-----GYCLED 144
Cdd:cd14140   2 IKARGRFGCVWKAQLMNE-----------YVAVKIFpiqDKQSWQSEREIFSTPG----MKHENLLQFIaaekrGSNLEM 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 145 EHrLLVYEFMPRGSLENHLfrRGlyfQPLSWKLRLKVALGAAKGLAFLHSSETR---------VIYRDFKTSNILLDSEY 215
Cdd:cd14140  67 EL-WLITAFHDKGSLTDYL--KG---NIVSWNELCHIAETMARGLSYLHEDVPRckgeghkpaIAHRDFKSKNVLLKNDL 140
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15222437 216 NAKLSDFGLA----KDGPIGDkSHVStrvMGTHGYAAPEYLaTGHLT------TKSDVYSFGVVLLELLSGRRAVD 281
Cdd:cd14140 141 TAVLADFGLAvrfePGKPPGD-THGQ---VGTRRYMAPEVL-EGAINfqrdsfLRIDMYAMGLVLWELVSRCKAAD 211
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
67-277 7.34e-16

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: 77.01  E-value: 7.34e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQDG-WQGHQEW-------LAEVNYLGQFS-HRHLVKL 137
Cdd:cd14093   4 KYEPKEILGRGVSSTVRR---------CIEKETGQEFAVKIIDITGeKSSENEAeelreatRREIEILRQVSgHPNIIEL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 138 IGYCLEDEHRLLVYEFMPRGSLENHLFRRglyfQPLSWKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNA 217
Cdd:cd14093  75 HDVFESPTFIFLVFELCRKGELFDYLTEV----VTLSEKKTRRIMRQLFEAVEFLHSLN--IVHRDLKPENILLDDNLNV 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15222437 218 KLSDFGLAKDGPIGDKshvSTRVMGTHGYAAPEYL-------ATGHlTTKSDVYSFGVVLLELLSGR 277
Cdd:cd14093 149 KISDFGFATRLDEGEK---LRELCGTPGYLAPEVLkcsmydnAPGY-GKEVDMWACGVIMYTLLAGC 211
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
73-276 7.77e-16

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: 78.08  E-value: 7.77e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGcvfkgwideKSLTASRPGTGLVIAVKKLNQDGWQGHQEW---LAEVN-YLGQFSHRHLVKLiGYCLEDEHRL 148
Cdd:cd05604   3 VIGKGSFG---------KVLLAKRKRDGKYYAVKVLQKKVILNRKEQkhiMAERNvLLKNVKHPFLVGL-HYSFQTTDKL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 -LVYEFMPRGSLENHLFRRGLYFQPlswKLRLKVAlGAAKGLAFLHSseTRVIYRDFKTSNILLDSEYNAKLSDFGLAKD 227
Cdd:cd05604  73 yFVLDFVNGGELFFHLQRERSFPEP---RARFYAA-EIASALGYLHS--INIVYRDLKPENILLDSQGHIVLTDFGLCKE 146
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15222437 228 GPigDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd05604 147 GI--SNSDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYG 193
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
72-306 8.11e-16

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


Pssm-ID: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 77.14  E-value: 8.11e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  72 SVLGEGGFGCVFKGWIDEKSltASRPGTGLVIAVKKLNQDGWQGHQEWLA-EVNYLGQFSHRHLVKLIGYCLEDEHRLLV 150
Cdd:cd14076   7 RTLGEGEFGKVKLGWPLPKA--NHRSGVQVAIKLIRRDTQQENCQTSKIMrEINILKGLTHPNIVRLLDVLKTKKYIGIV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 151 YEFMPRGSLENHLFRRglyfQPLSWKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPI 230
Cdd:cd14076  85 LEFVSGGELFDYILAR----RRLKDSVACRLFAQLISGVAYLHKKG--VVHRDLKLENLLLDKNRNLVITDFGFANTFDH 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 231 GDKSHVSTRVmGTHGYAAPEY--LATGHLTTKSDVYSFGVVLLELLSGRRAVDKN--RPSGErNLVEWAKpYLVNKRKIF 306
Cdd:cd14076 159 FNGDLMSTSC-GSPCYAAPELvvSDSMYAGRKADIWSCGVILYAMLAGYLPFDDDphNPNGD-NVPRLYR-YICNTPLIF 235
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
122-349 1.14e-15

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: 76.24  E-value: 1.14e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 122 EVNYLGQFSHRHLVKLIGYCLE-----DEHRL-LVYEFMPRGSLENHLFRRGlyFQPL----SWKLRLkvalgaAKGLAF 191
Cdd:cd14012  48 ELESLKKLRHPNLVSYLAFSIErrgrsDGWKVyLLTEYAPGGSLSELLDSVG--SVPLdtarRWTLQL------LEALEY 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 192 LHSSEtrVIYRDFKTSNILLDS---EYNAKLSDFGLAKdgPIGD-KSHVSTRVMGTHGYAAPEyLATGHL--TTKSDVYS 265
Cdd:cd14012 120 LHRNG--VVHKSLHAGNVLLDRdagTGIVKLTDYSLGK--TLLDmCSRGSLDEFKQTYWLPPE-LAQGSKspTRKTDVWD 194
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 266 FGVVLLELLSGRRAVDKnrpsgernlVEWAKPYLVNKrkifrVIDNRLQDqysmeeackvatLSLRCLTTEIKLRPNMSE 345
Cdd:cd14012 195 LGLLFLQMLFGLDVLEK---------YTSPNPVLVSL-----DLSASLQD------------FLSKCLSLDPKKRPTALE 248

                ....
gi 15222437 346 VVSH 349
Cdd:cd14012 249 LLPH 252
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
74-275 1.31e-15

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: 76.98  E-value: 1.31e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGwiDEKSLTASRPGTGLVIAVKKLNQDGWQGH-QEWLAEVNYLGQFS-HRHLVKLIGYCLEDEHRLLVY 151
Cdd:cd05101  32 LGEGCFGQVVMA--EAVGIDKDKPKEAVTVAVKMLKDDATEKDlSDLVSEMEMMKMIGkHKNIINLLGACTQDGPLYVIV 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 152 EFMPRGSLENHLFRR---GLYF---------QPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKL 219
Cdd:cd05101 110 EYASKGNLREYLRARrppGMEYsydinrvpeEQMTFKDLVSCTYQLARGMEYLASQ--KCIHRDLAARNVLVTENNVMKI 187
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15222437 220 SDFGLAKDGPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:cd05101 188 ADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFT 243
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
74-276 1.47e-15

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: 76.24  E-value: 1.47e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGwIDEKsltasrpgTGLVIAVKKLNQDGWQGHQEWLA-EVNYLGQFSHRHLVKLIGYCLEDEHRLLVYE 152
Cdd:cd06640  12 IGKGSFGEVFKG-IDNR--------TQQVVAIKIIDLEEAEDEIEDIQqEITVLSQCDSPYVTKYYGSYLKGTKLWIIME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMPRGSLENhLFRRGLyFQPLSWKLRLKVALgaaKGLAFLHSSETrvIYRDFKTSNILLDSEYNAKLSDFGLAkdGPIGD 232
Cdd:cd06640  83 YLGGGSALD-LLRAGP-FDEFQIATMLKEIL---KGLDYLHSEKK--IHRDIKAANVLLSEQGDVKLADFGVA--GQLTD 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 15222437 233 KSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd06640 154 TQIKRNTFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKG 197
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
74-297 1.51e-15

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: 76.33  E-value: 1.51e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKgWIDEKsltasrpgTGLVIAVKKLNQ--DGWQGHQE-WLAEVNYLGQFSHRHLVKL------IGYCLED 144
Cdd:cd13989   1 LGSGGFGYVTL-WKHQD--------TGEYVAIKKCRQelSPSDKNRErWCLEVQIMKKLNHPNVVSArdvppeLEKLSPN 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 145 EHRLLVYEFMPRGSLENHLFR----RGLYFQPLSWKLRlkvalGAAKGLAFLHssETRVIYRDFKTSNILLDSEYNA--- 217
Cdd:cd13989  72 DLPLLAMEYCSGGDLRKVLNQpencCGLKESEVRTLLS-----DISSAISYLH--ENRIIHRDLKPENIVLQQGGGRviy 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 218 KLSDFGLAKDGpigDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVDKNRPSGERN-LVEWAK 296
Cdd:cd13989 145 KLIDLGYAKEL---DQGSLCTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPFLPNWQPVQWHgKVKQKK 221

                .
gi 15222437 297 P 297
Cdd:cd13989 222 P 222
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
74-276 1.65e-15

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: 75.88  E-value: 1.65e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGcvfkgwideKSLTASRPGTGLVIAVKKLNQDGWqGHQ--EWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVY 151
Cdd:cd14078  11 IGSGGFA---------KVKLATHILTGEKVAIKIMDKKAL-GDDlpRVKTEIEALKNLSHQHICRLYHVIETDNKIFMVL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 152 EFMPRGSLENHLFR---------RGLYFQPLSwklrlkvalgaakGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDF 222
Cdd:cd14078  81 EYCPGGELFDYIVAkdrlsedeaRVFFRQIVS-------------AVAYVHSQG--YAHRDLKPENLLLDEDQNLKLIDF 145
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15222437 223 GLAKDGPIGDKSHVSTrVMGTHGYAAPEYLATG-HLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14078 146 GLCAKPKGGMDHHLET-CCGSPAYAAPELIQGKpYIGSEADVWSMGVLLYALLCG 199
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
131-277 1.98e-15

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: 75.67  E-value: 1.98e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 131 HRHLVKLIGyCLEDEHR---LLVYEFMPRGSLENhlFRRGLYFQPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTS 207
Cdd:cd14008  63 HPNIVRLYE-VIDDPESdklYLVLEYCEGGPVME--LDSGDRVPPLPEETARKYFRDLVLGLEYLHEN--GIVHRDIKPE 137
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15222437 208 NILLDSEYNAKLSDFGLAKDGPIGDKSHVSTrvMGTHGYAAPEyLATGHLTTKS----DVYSFGVVLLELLSGR 277
Cdd:cd14008 138 NLLLTADGTVKISDFGVSEMFEDGNDTLQKT--AGTPAFLAPE-LCDGDSKTYSgkaaDIWALGVTLYCLVFGR 208
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
39-355 2.21e-15

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: 76.63  E-value: 2.21e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  39 PSPRTEGEiLQSPNLKSFSFAElkSATRNFRPDSVLGEGGFGCVFkgwidekslTASRPGTGLVIAVKKLNQDGWQGHQE 118
Cdd:cd06635   1 PSTSRAGS-LKDPDIAELFFKE--DPEKLFSDLREIGHGSFGAVY---------FARDVRTSEVVAIKKMSYSGKQSNEK 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 119 W---LAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEFMpRGSLENHLfrrGLYFQPLSWKLRLKVALGAAKGLAFLHSS 195
Cdd:cd06635  69 WqdiIKEVKFLQRIKHPNSIEYKGCYLREHTAWLVMEYC-LGSASDLL---EVHKKPLQEIEIAAITHGALQGLAYLHSH 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 196 EtrVIYRDFKTSNILLDSEYNAKLSDFGLAKdgpigdKSHVSTRVMGTHGYAAPEYLAT---GHLTTKSDVYSFGVVLLE 272
Cdd:cd06635 145 N--MIHRDIKAGNILLTEPGQVKLADFGSAS------IASPANSFVGTPYWMAPEVILAmdeGQYDGKVDVWSLGITCIE 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 273 LLSGRRAV-DKNRPSGERNLVEWAKPYLVNKR--KIFR-VIDNRL----QDQYSMEEACK-VATLSLRCLTTEIKLRPNM 343
Cdd:cd06635 217 LAERKPPLfNMNAMSALYHIAQNESPTLQSNEwsDYFRnFVDSCLqkipQDRPTSEELLKhMFVLRERPETVLIDLIQRT 296
                       330
                ....*....|..
gi 15222437 344 SEVVSHLEHIQS 355
Cdd:cd06635 297 KDAVRELDNLQY 308
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
74-275 2.27e-15

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: 75.75  E-value: 2.27e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWIDEKSltasrpgTGLVIAVKKLNQDGWQG-HQEWLAEVNYLGQFSHRHLVKLIGYClEDEHRLLVYE 152
Cdd:cd05115  12 LGSGNFGCVKKGVYKMRK-------KQIDVAIKVLKQGNEKAvRDEMMREAQIMHQLDNPYIVRMIGVC-EAEALMLVME 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMPRGSLenHLFRRGLYFQ-PLSWKLRL--KVALGaakgLAFLHssETRVIYRDFKTSNILLDSEYNAKLSDFGLAKdgP 229
Cdd:cd05115  84 MASGGPL--NKFLSGKKDEiTVSNVVELmhQVSMG----MKYLE--EKNFVHRDLAARNVLLVNQHYAKISDFGLSK--A 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15222437 230 IG-DKSHVSTRVMGTH--GYAAPEYLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:cd05115 154 LGaDDSYYKARSAGKWplKWYAPECINFRKFSSRSDVWSYGVTMWEAFS 202
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
74-349 2.27e-15

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: 75.86  E-value: 2.27e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGwIDEKSLTasrpgtglVIAVKKLNQDGWQGHQEWLA-EVNYLGQFSHRHLVKLIGYCLEDEHRLLVYE 152
Cdd:cd06642  12 IGKGSFGEVYKG-IDNRTKE--------VVAIKIIDLEEAEDEIEDIQqEITVLSQCDSPYITRYYGSYLKGTKLWIIME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMPRGSLENhLFRRGlyfqPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAkdGPIGD 232
Cdd:cd06642  83 YLGGGSALD-LLKPG----PLEETYIATILREILKGLDYLHSE--RKIHRDIKAANVLLSEQGDVKLADFGVA--GQLTD 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 233 KSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVDKNRPsgernlvewakpylvnKRKIFRVIDNR 312
Cdd:cd06642 154 TQIKRNTFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDLHP----------------MRVLFLIPKNS 217
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 15222437 313 ---LQDQYSMEEACKVATlslrCLTTEIKLRPNMSEVVSH 349
Cdd:cd06642 218 pptLEGQHSKPFKEFVEA----CLNKDPRFRPTAKELLKH 253
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
63-349 2.31e-15

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: 75.89  E-value: 2.31e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  63 SATRNFRPDSVLGEGGFGCVFKGW-IDeksltasrpgTGLVIAVKKL--NQDGWQGHQEWLA---EVNYLGQFSHRHLVK 136
Cdd:cd06651   4 SAPINWRRGKLLGQGAFGRVYLCYdVD----------TGRELAAKQVqfDPESPETSKEVSAlecEIQLLKNLQHERIVQ 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 137 LIGyCLED--EHRLLVY-EFMPRGSLENHLFRRGLYFQPLSWKLRLKVAlgaaKGLAFLHSSetRVIYRDFKTSNILLDS 213
Cdd:cd06651  74 YYG-CLRDraEKTLTIFmEYMPGGSVKDQLKAYGALTESVTRKYTRQIL----EGMSYLHSN--MIVHRDIKGANILRDS 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 214 EYNAKLSDFGLAKDGPIGDKSHVSTR-VMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSgrravdkNRPSgernlv 292
Cdd:cd06651 147 AGNVKLGDFGASKRLQTICMSGTGIRsVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLT-------EKPP------ 213
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15222437 293 eWAKPYLVnkRKIFRVIDNRLQDQYSmEEACKVATLSLRCLTTEIKLRPNMSEVVSH 349
Cdd:cd06651 214 -WAEYEAM--AAIFKIATQPTNPQLP-SHISEHARDFLGCIFVEARHRPSAEELLRH 266
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
73-276 2.41e-15

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


Pssm-ID: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 76.20  E-value: 2.41e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGcvfkgwideKSLTASRPGTGLVIAVKKLNQDGWQGHQEW---LAEVNYL-GQFSHRHLVKLiGYCLEDEHRL 148
Cdd:cd05575   2 VIGKGSFG---------KVLLARHKAEGKLYAVKVLQKKAILKRNEVkhiMAERNVLlKNVKHPFLVGL-HYSFQTKDKL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 -LVYEFMPRGSLENHLfRRGLYFQPLSWKLrlkVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAKD 227
Cdd:cd05575  72 yFVLDYVNGGELFFHL-QRERHFPEPRARF---YAAEIASALGYLHSLN--IIYRDLKPENILLDSQGHVVLTDFGLCKE 145
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15222437 228 GpIGDKSHVSTrVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd05575 146 G-IEPSDTTST-FCGTPEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYG 192
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
188-277 2.80e-15

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: 75.03  E-value: 2.80e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 188 GLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPIGD--KSHVSTRVMGTHGYAAPEYL-ATGHLTTKSDVY 264
Cdd:cd14162 112 GVEYCHSK--GVVHRDLKCENLLLDKNNNLKITDFGFARGVMKTKdgKPKLSETYCGSYAYASPEILrGIPYDPFLSDIW 189
                        90
                ....*....|...
gi 15222437 265 SFGVVLLELLSGR 277
Cdd:cd14162 190 SMGVVLYTMVYGR 202
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
73-277 2.82e-15

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


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 76.24  E-value: 2.82e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKGwiDEKSltasrpgTGLVIAVKKLNQDGWQGHQE---WLAEVNYLGQFSHRHLVKLiGYCLEDEHRL- 148
Cdd:cd05571   2 VLGKGTFGKVILC--REKA-------TGELYAIKILKKEVIIAKDEvahTLTENRVLQNTRHPFLTSL-KYSFQTNDRLc 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 LVYEFMPRGSLENHLFRRGLYFQPlswKLRLkvaLGAAKGLA--FLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAK 226
Cdd:cd05571  72 FVMEYVNGGELFFHLSRERVFSED---RTRF---YGAEIVLAlgYLHSQG--IVYRDLKLENLLLDKDGHIKITDFGLCK 143
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15222437 227 DGpIGDKSHVSTrVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd05571 144 EE-ISYGATTKT-FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGR 192
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
74-276 3.24e-15

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: 75.48  E-value: 3.24e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKG-WIDEksltasrpgtglvIAVKKLNQDGW--QGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEhRLLV 150
Cdd:cd14151  16 IGSGSFGTVYKGkWHGD-------------VAVKMLNVTAPtpQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQ-LAIV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 151 YEFMPRGSLENHLFRRGLYFQplsWKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPI 230
Cdd:cd14151  82 TQWCEGSSLYHHLHIIETKFE---MIKLIDIARQTAQGMDYLHAKS--IIHRDLKSNNIFLHEDLTVKIGDFGLATVKSR 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15222437 231 GDKSHVSTRVMGTHGYAAPEYLA---TGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14151 157 WSGSHQFEQLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTG 205
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
74-277 3.67e-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: 3.67e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGwideKSLTasrpgTGLVIAVKK--LNQDGWQGHQEWLAEVNYLGQFSHRHLVKLigYC-LEDEHRL-L 149
Cdd:cd07835   7 IGEGTYGVVYKA----RDKL-----TGEIVALKKirLETEDEGVPSTAIREISLLKELNHPNIVRL--LDvVHSENKLyL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 150 VYEFM-----------PRGSLENHLFRRGLYfQPLswklrlkvalgaaKGLAFLHSSetRVIYRDFKTSNILLDSEYNAK 218
Cdd:cd07835  76 VFEFLdldlkkymdssPLTGLDPPLIKSYLY-QLL-------------QGIAFCHSH--RVLHRDLKPQNLLIDTEGALK 139
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 219 LSDFGLAKdgPIGDKSHVSTRVMGTHGYAAPE-YLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd07835 140 LADFGLAR--AFGVPVRTYTHEVVTLWYRAPEiLLGSKHYSTPVDIWSVGCIFAEMVTRR 197
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
74-278 3.92e-15

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: 74.57  E-value: 3.92e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKG-WideksltasrPGTGLViAVKKLnQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGyCLEDEHRLLVYE 152
Cdd:cd14203   3 LGQGCFGEVWMGtW----------NGTTKV-AIKTL-KPGTMSPEAFLEEAQIMKKLRHDKLVQLYA-VVSEEPIYIVTE 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMPRGSLENhlFRRGLYFQPLSWKLRLKVALGAAKGLAFLHssETRVIYRDFKTSNILLDSEYNAKLSDFGLAKdgPIGD 232
Cdd:cd14203  70 FMSKGSLLD--FLKDGEGKYLKLPQLVDMAAQIASGMAYIE--RMNYIHRDLRAANILVGDNLVCKIADFGLAR--LIED 143
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15222437 233 KSHvsTRVMGTH---GYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRR 278
Cdd:cd14203 144 NEY--TARQGAKfpiKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGR 190
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
73-276 4.17e-15

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: 75.03  E-value: 4.17e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFkgWIDEKSltasrpgTGLVIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYE 152
Cdd:cd14166  10 VLGSGAFSEVY--LVKQRS-------TGKLYALKCIKKSPLSRDSSLENEIAVLKRIKHENIVTLEDIYESTTHYYLVMQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMPRGSLENHLFRRGLYFQPLSwKLRLKVALGAAKglaFLHssETRVIYRDFKTSNIL-LDSEYNAKL--SDFGLAKdgp 229
Cdd:cd14166  81 LVSGGELFDRILERGVYTEKDA-SRVINQVLSAVK---YLH--ENGIVHRDLKPENLLyLTPDENSKImiTDFGLSK--- 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15222437 230 IGDKSHVSTrVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14166 152 MEQNGIMST-ACGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCG 197
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
73-276 4.65e-15

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


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 75.51  E-value: 4.65e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFkgwideksLTASRPG--TGLVIAVKKLNQ------DGWQGHQE--WLAEVNylgqfsHRHLVKLiGYCL 142
Cdd:cd05582   2 VLGQGSFGKVF--------LVRKITGpdAGTLYAMKVLKKatlkvrDRVRTKMErdILADVN------HPFIVKL-HYAF 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 143 EDEHRL-LVYEFMPRGSLENHLFRRgLYFQPLSWKLRL-KVALGaakgLAFLHSseTRVIYRDFKTSNILLDSEYNAKLS 220
Cdd:cd05582  67 QTEGKLyLILDFLRGGDLFTRLSKE-VMFTEEDVKFYLaELALA----LDHLHS--LGIIYRDLKPENILLDEDGHIKLT 139
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15222437 221 DFGLAKDGPIGDKSHVStrVMGTHGYAAPEYLA-TGHlTTKSDVYSFGVVLLELLSG 276
Cdd:cd05582 140 DFGLSKESIDHEKKAYS--FCGTVEYMAPEVVNrRGH-TQSADWWSFGVLMFEMLTG 193
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
73-277 4.74e-15

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


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 75.43  E-value: 4.74e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFkgWIDEKSltasrpgTGLVIAVKKLNQDGWQGHQE---WLAEVNYLGQFSHRHLVKLiGYCLEDEHRL- 148
Cdd:cd05595   2 LLGKGTFGKVI--LVREKA-------TGRYYAMKILRKEVIIAKDEvahTVTESRVLQNTRHPFLTAL-KYAFQTHDRLc 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 LVYEFMPRGSLENHLFRRGLYFQPlswKLRLkvaLGA--AKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAK 226
Cdd:cd05595  72 FVMEYANGGELFFHLSRERVFTED---RARF---YGAeiVSALEYLHSRD--VVYRDIKLENLMLDKDGHIKITDFGLCK 143
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15222437 227 DGpIGDKSHVSTrVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd05595 144 EG-ITDGATMKT-FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGR 192
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
73-277 5.64e-15

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: 74.69  E-value: 5.64e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKG-WIDEksltasrpgtglvIAVKKLNQDGWQghQEWLA----EVNYLGQFSHRHLVKLIGYCLEDEHR 147
Cdd:cd14063   7 VIGKGRFGRVHRGrWHGD-------------VAIKLLNIDYLN--EEQLEafkeEVAAYKNTRHDNLVLFMGACMDPPHL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 148 LLVYEFMPRGSLENHLFRRGLYFqPLSWKLrlKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDseyNAK--LSDFGLA 225
Cdd:cd14063  72 AIVTSLCKGRTLYSLIHERKEKF-DFNKTV--QIAQQICQGMGYLHAKG--IIHKDLKSKNIFLE---NGRvvITDFGLF 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15222437 226 KDGPIGDKSHVSTRVMGTHG---YAAPE-------YLATGHL---TTKSDVYSFGVVLLELLSGR 277
Cdd:cd14063 144 SLSGLLQPGRREDTLVIPNGwlcYLAPEiiralspDLDFEESlpfTKASDVYAFGTVWYELLAGR 208
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
74-281 5.72e-15

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: 74.61  E-value: 5.72e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGcvfkgwideKSLTASRPGTGLVIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEF 153
Cdd:cd14221   1 LGKGCFG---------QAIKVTHRETGEVMVMKELIRFDEETQRTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEY 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 154 MPRGSLENHLFRRGLYFqplSWKLRLKVALGAAKGLAFLHSseTRVIYRDFKTSNILLDSEYNAKLSDFGLA------KD 227
Cdd:cd14221  72 IKGGTLRGIIKSMDSHY---PWSQRVSFAKDIASGMAYLHS--MNIIHRDLNSHNCLVRENKSVVVADFGLArlmvdeKT 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 228 GPIGDKSHVST------RVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLsGRRAVD 281
Cdd:cd14221 147 QPEGLRSLKKPdrkkryTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEII-GRVNAD 205
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
73-276 6.06e-15

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: 6.06e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGcvfkgwideKSLTASRPGTGLVIAVKKLNQDGWQGHQE---WLAEVNYLG-QFSHRHLVKLIgYCLEDEHRL 148
Cdd:cd05590   2 VLGKGSFG---------KVMLARLKESGRLYAVKVLKKDVILQDDDvecTMTEKRILSlARNHPFLTQLY-CCFQTPDRL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 L-VYEFMPRGSLENHLFRRGLYFQPlswKLRLKVAlGAAKGLAFLHssETRVIYRDFKTSNILLDSEYNAKLSDFGLAKD 227
Cdd:cd05590  72 FfVMEFVNGGDLMFHIQKSRRFDEA---RARFYAA-EITSALMFLH--DKGIIYRDLKLDNVLLDHEGHCKLADFGMCKE 145
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15222437 228 GpIGDKSHVSTrVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd05590 146 G-IFNGKTTST-FCGTPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCG 192
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
68-293 6.76e-15

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: 75.01  E-value: 6.76e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  68 FRPDSVLGEGGFGCVfkgwideksLTASRPGTGLVIAVKKLNQD---GWQGHQEWLAEVNYLGQFSHRHLVKLiGYCLED 144
Cdd:cd05632   4 FRQYRVLGKGGFGEV---------CACQVRATGKMYACKRLEKKrikKRKGESMALNEKQILEKVNSQFVVNL-AYAYET 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 145 EHRL-LVYEFMPRGSLENHLFRRGlyfQPLSWKLRlkVALGAAK---GLAFLHSSETrvIYRDFKTSNILLDSEYNAKLS 220
Cdd:cd05632  74 KDALcLVLTIMNGGDLKFHIYNMG---NPGFEEER--ALFYAAEilcGLEDLHRENT--VYRDLKPENILLDDYGHIRIS 146
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15222437 221 DFGLAKDGPIGDKshVSTRVmGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVDKNRPSGERNLVE 293
Cdd:cd05632 147 DLGLAVKIPEGES--IRGRV-GTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKREEVD 216
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
73-277 7.03e-15

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: 74.84  E-value: 7.03e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGcvfkgwideKSLTASRPGTGLVIAVKKLNQDGWQGHQE---WLAEVNYLGQFSHRHLVKLIGYCLEDEHRLL 149
Cdd:cd05591   2 VLGKGSFG---------KVMLAERKGTDEVYAIKVLKKDVILQDDDvdcTMTEKRILALAAKHPFLTALHSCFQTKDRLF 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 150 -VYEFMPRGSLENHLFRRGLYFQPLSWKLRLKVALGaakgLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAKDG 228
Cdd:cd05591  73 fVMEYVNGGDLMFQIQRARKFDEPRARFYAAEVTLA----LMFLHRHG--VIYRDLKLDNILLDAEGHCKLADFGMCKEG 146
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15222437 229 PIGDKShvSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd05591 147 ILNGKT--TTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQ 193
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
73-276 7.58e-15

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: 73.98  E-value: 7.58e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKGwIDEKsltasrpgTGLVIAVKKLNQDGWQGH---QEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLL 149
Cdd:cd14663   7 TLGEGTFAKVKFA-RNTK--------TGESVAIKIIDKEQVAREgmvEQIKREIAIMKLLRHPNIVELHEVMATKTKIFF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 150 VYEFMPRGSLENHLFRRGL--------YFQPLswklrlkvalgaAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSD 221
Cdd:cd14663  78 VMELVTGGELFSKIAKNGRlkedkarkYFQQL------------IDAVDYCHSRG--VFHRDLKPENLLLDEDGNLKISD 143
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15222437 222 FGL-AKDGPIGDKSHVSTRVmGTHGYAAPEYLAT-GHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14663 144 FGLsALSEQFRQDGLLHTTC-GTPNYVAPEVLARrGYDGAKADIWSCGVILFVLLAG 199
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
68-293 7.59e-15

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: 74.28  E-value: 7.59e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  68 FRPDSVLGEGGFGCVFKGWIDEKSltasrpgtGLVIAVKKLNQDGWQGHQEWLA-EVNYLGQFSHRHLVKLIGYCLEDEH 146
Cdd:cd14202   4 FSRKDLIGHGAFAVVFKGRHKEKH--------DLEVAVKCINKKNLAKSQTLLGkEIKILKELKHENIVALYDFQEIANS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 147 RLLVYEFMPRGSLENHLFRRGLYFQPlSWKLRLKVALGAAKglaFLHSSEtrVIYRDFKTSNILLD---------SEYNA 217
Cdd:cd14202  76 VYLVMEYCNGGDLADYLHTMRTLSED-TIRLFLQQIAGAMK---MLHSKG--IIHRDLKPQNILLSysggrksnpNNIRI 149
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15222437 218 KLSDFGLAKdgpIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVDKNRPSGERNLVE 293
Cdd:cd14202 150 KIADFGFAR---YLQNNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQDLRLFYE 222
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
74-277 7.80e-15

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: 73.80  E-value: 7.80e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVfkgwidekSLTASRPgTGLVIAVKKLN-----QDGWQGH----QEWLAEVNylgqfsHRHLVKLIGYCLED 144
Cdd:cd05572   1 LGVGGFGRV--------ELVQLKS-KGRTFALKCVKkrhivQTRQQEHifseKEILEECN------SPFIVKLYRTFKDK 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 145 EHRLLVYEFMPRGSLENHLFRRGLYFqplSWKLRLKVALgAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGL 224
Cdd:cd05572  66 KYLYMLMEYCLGGELWTILRDRGLFD---EYTARFYTAC-VVLAFEYLHSRG--IIYRDLKPENLLLDSNGYVKLVDFGF 139
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15222437 225 AKDgpIGDKSHVSTRVmGTHGYAAPE-YLATGHlTTKSDVYSFGVVLLELLSGR 277
Cdd:cd05572 140 AKK--LGSGRKTWTFC-GTPEYVAPEiILNKGY-DFSVDYWSLGILLYELLTGR 189
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
74-275 8.02e-15

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: 73.74  E-value: 8.02e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKG-WideksltasrpGTGLVIAVKKLNQdGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYE 152
Cdd:cd05114  12 LGSGLFGVVRLGkW-----------RAQYKVAIKAIRE-GAMSEEDFIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMPRGSLENHLFRRGLYFQPlswKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAKdGPIGD 232
Cdd:cd05114  80 FMENGCLLNYLRQRRGKLSR---DMLLSMCQDVCEGMEYLERNN--FIHRDLAARNCLVNDTGVVKVSDFGMTR-YVLDD 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 15222437 233 KSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:cd05114 154 QYTSSSGAKFPVKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFT 196
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
73-276 8.82e-15

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: 74.01  E-value: 8.82e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQDGW---QGHQEWLAEVNYLGQFSHRHLVKLI---GYCLEDEH 146
Cdd:cd05606   1 IIGRGGFGEVYG---------CRKADTGKMYAMKCLDKKRIkmkQGETLALNERIMLSLVSTGGDCPFIvcmTYAFQTPD 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 147 RL-LVYEFMPRGSLENHLFRRGLYFQPlswklrlKVALGAAK---GLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDF 222
Cdd:cd05606  72 KLcFILDLMNGGDLHYHLSQHGVFSEA-------EMRFYAAEvilGLEHMHNR--FIVYRDLKPANILLDEHGHVRISDL 142
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15222437 223 GLAKDGPiGDKSHVStrvMGTHGYAAPEYLATG-HLTTKSDVYSFGVVLLELLSG 276
Cdd:cd05606 143 GLACDFS-KKKPHAS---VGTHGYMAPEVLQKGvAYDSSADWFSLGCMLYKLLKG 193
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
66-277 9.07e-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: 73.46  E-value: 9.07e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  66 RNFRPDSVLGEGGFGCVfKGWIDEKsltasrpgTGLVIAVKKLNQDGWQG---HQEWLAEVNYLGQFSHRHLVKLigY-C 141
Cdd:cd14079   2 GNYILGKTLGVGSFGKV-KLAEHEL--------TGHKVAVKILNRQKIKSldmEEKIRREIQILKLFRHPHIIRL--YeV 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 142 LEDEHRL-LVYEFMPRGSLENHLFRRG---------LYFQPLSwklrlkvalgaakGLAFLHSSetRVIYRDFKTSNILL 211
Cdd:cd14079  71 IETPTDIfMVMEYVSGGELFDYIVQKGrlsedearrFFQQIIS-------------GVEYCHRH--MVVHRDLKPENLLL 135
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15222437 212 DSEYNAKLSDFGLA---KDGPIGDKShvstrvMGTHGYAAPEYLaTGHLTTKS--DVYSFGVVLLELLSGR 277
Cdd:cd14079 136 DSNMNVKIADFGLSnimRDGEFLKTS------CGSPNYAAPEVI-SGKLYAGPevDVWSCGVILYALLCGS 199
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
67-278 9.36e-15

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: 73.95  E-value: 9.36e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGCVFKGwideksltaSRPGTGLViAVKKLnQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGyCLEDEH 146
Cdd:cd05071  10 SLRLEVKLGQGCFGEVWMG---------TWNGTTRV-AIKTL-KPGTMSPEAFLQEAQVMKKLRHEKLVQLYA-VVSEEP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 147 RLLVYEFMPRGSLENhlFRRGLYFQPLSWKLRLKVALGAAKGLAFLHssETRVIYRDFKTSNILLDSEYNAKLSDFGLAK 226
Cdd:cd05071  78 IYIVTEYMSKGSLLD--FLKGEMGKYLRLPQLVDMAAQIASGMAYVE--RMNYVHRDLRAANILVGENLVCKVADFGLAR 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15222437 227 dgPIGDKSHVSTRvmGTH---GYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRR 278
Cdd:cd05071 154 --LIEDNEYTARQ--GAKfpiKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGR 204
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
74-273 1.04e-14

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: 73.69  E-value: 1.04e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKgwIDEKSltasrpGTGLVIAVKKLN----------QDGWQGHQEWLAEVNYLG-QFSHRHLVKLIGYCL 142
Cdd:cd08528   8 LGSGAFGCVYK--VRKKS------NGQTLLALKEINmtnpafgrteQERDKSVGDIISEVNIIKeQLRHPNIVRYYKTFL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 143 EDEHRLLVYEFM---PRGSLENHLFRRGLYF-QPLSWKLRLKVALGaakgLAFLHSsETRVIYRDFKTSNILLDSEYNAK 218
Cdd:cd08528  80 ENDRLYIVMELIegaPLGEHFSSLKEKNEHFtEDRIWNIFVQMVLA----LRYLHK-EKQIVHRDLKPNNIMLGEDDKVT 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15222437 219 LSDFGLAKDGpiGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLEL 273
Cdd:cd08528 155 ITDFGLAKQK--GPESSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQM 207
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
67-276 1.10e-14

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: 73.52  E-value: 1.10e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRpdSVLGEGGFGCVfkgwideksLTASRPGTGLVIAVKKLNQDGWQGHQEWLA-EVNYLGQFSHRHLVKLIGYCLEDE 145
Cdd:cd14167   6 DFR--EVLGTGAFSEV---------VLAEEKRTQKLVAIKCIAKKALEGKETSIEnEIAVLHKIKHPNIVALDDIYESGG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 146 HRLLVYEFMPRGSLENHLFRRGLYFQPLSWKLRLKVaLGAAKglaFLHssETRVIYRDFKTSNIL---LDSEYNAKLSDF 222
Cdd:cd14167  75 HLYLIMQLVSGGELFDRIVEKGFYTERDASKLIFQI-LDAVK---YLH--DMGIVHRDLKPENLLyysLDEDSKIMISDF 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15222437 223 GLAKdgpIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14167 149 GLSK---IEGSGSVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCG 199
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
67-349 1.12e-14

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: 74.39  E-value: 1.12e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGCVFKgwidekslTASRPgTGLVIAVKKLNQDGWQG-HQEWLAEVNYLGQFSHRHLVKLIGYCLEDE 145
Cdd:cd06615   2 DFEKLGELGAGNGGVVTK--------VLHRP-SGLIMARKLIHLEIKPAiRNQIIRELKVLHECNSPYIVGFYGAFYSDG 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 146 HRLLVYEFMPRGSLENHLFRRGlyfqPLSWKLRLKVALGAAKGLAFLHSsETRVIYRDFKTSNILLDSEYNAKLSDFGLA 225
Cdd:cd06615  73 EISICMEHMDGGSLDQVLKKAG----RIPENILGKISIAVLRGLTYLRE-KHKIMHRDVKPSNILVNSRGEIKLCDFGVS 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 226 kdGPIGDkSHVSTRVmGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAV-------------DKNRPSGERNLV 292
Cdd:cd06615 148 --GQLID-SMANSFV-GTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGRYPIpppdakeleamfgRPVSEGEAKESH 223
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15222437 293 EWAKPYLVNKRK---IFRVIDN-------RLQDQYSMEEACKVATlslRCLTTEIKLRPNMSEVVSH 349
Cdd:cd06615 224 RPVSGHPPDSPRpmaIFELLDYivnepppKLPSGAFSDEFQDFVD---KCLKKNPKERADLKELTKH 287
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
74-350 1.14e-14

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They 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. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. In the case of Jak2, the presumed pseudokinase (repeat 1) domain exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. 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 serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270633 [Multi-domain]  Cd Length: 259  Bit Score: 73.28  E-value: 1.14e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWIDEKSLTASRpgtgLVIAVKK-LNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHrLLVYE 152
Cdd:cd05037   7 LGQGTFTNIYDGILREVGDGRVQ----EVEVLLKvLDSDHRDISESFFETASLMSQISHKHLVKLYGVCVADEN-IMVQE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMPRGSLENHLFRRGLYFqPLSWKlrLKVALGAAKGLAFLHssETRVIYRDFKTSNILL----DSEYN--AKLSDFGLAK 226
Cdd:cd05037  82 YVRYGPLDKYLRRMGNNV-PLSWK--LQVAKQLASALHYLE--DKKLIHGNVRGRNILLaregLDGYPpfIKLSDPGVPI 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 227 dgPIGDKSHVSTRVmgthGYAAPEYL--ATGHLTTKSDVYSFGVVLLELLSGrravdknrpsGERNLvewaKPYLVNKRK 304
Cdd:cd05037 157 --TVLSREERVDRI----PWIAPECLrnLQANLTIAADKWSFGTTLWEICSG----------GEEPL----SALSSQEKL 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 15222437 305 IFRvidnRLQDQYSMEEACKVATLSLRCLTTEIKLRPNMSEVVSHL 350
Cdd:cd05037 217 QFY----EDQHQLPAPDCAELAELIMQCWTYEPTKRPSFRAILRDL 258
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
73-275 1.23e-14

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: 73.88  E-value: 1.23e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKGWIdeksltaSRPGTGLVIAVKKLNQDGWQG-HQEWLAEVNYLGQFS-HRHLVKLIGYCledEHRLLV 150
Cdd:cd05088  14 VIGEGNFGQVLKARI-------KKDGLRMDAAIKRMKEYASKDdHRDFAGELEVLCKLGhHPNIINLLGAC---EHRGYL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 151 Y---EFMPRGSLENHLFR-RGLYFQP-----------LSWKLRLKVALGAAKGLAFLhsSETRVIYRDFKTSNILLDSEY 215
Cdd:cd05088  84 YlaiEYAPHGNLLDFLRKsRVLETDPafaianstastLSSQQLLHFAADVARGMDYL--SQKQFIHRDLAARNILVGENY 161
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15222437 216 NAKLSDFGLAKdgpiGDKSHVStRVMGTHG--YAAPEYLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:cd05088 162 VAKIADFGLSR----GQEVYVK-KTMGRLPvrWMAIESLNYSVYTTNSDVWSYGVLLWEIVS 218
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
72-276 1.25e-14

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


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 74.63  E-value: 1.25e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  72 SVLGEGGFGCVFkgwidekslTASRPGTGLVIAVKKLN-QDGWQGHQE--WLAEVNYLGQFSHRHLVKLIgYCLEDEHRL 148
Cdd:cd05573   7 KVIGRGAFGEVW---------LVRDKDTGQVYAMKILRkSDMLKREQIahVRAERDILADADSPWIVRLH-YAFQDEDHL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 -LVYEFMPRGSLENHLFRRG--------LYFQPLSwklrlkVALGAAKGLAFLHssetrviyRDFKTSNILLDSEYNAKL 219
Cdd:cd05573  77 yLVMEYMPGGDLMNLLIKYDvfpeetarFYIAELV------LALDSLHKLGFIH--------RDIKPDNILLDADGHIKL 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 220 SDFGLAKDGPIGDKS---------------------------HVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLE 272
Cdd:cd05573 143 ADFGLCTKMNKSGDResylndsvntlfqdnvlarrrphkqrrVRAYSAVGTPDYIAPEVLRGTGYGPECDWWSLGVILYE 222

                ....
gi 15222437 273 LLSG 276
Cdd:cd05573 223 MLYG 226
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
131-281 1.25e-14

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: 73.64  E-value: 1.25e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 131 HRHLVKLIGYCLEDEHRLLVYEFMPRGSLENHLFRRGlyfqPLSWKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNIL 210
Cdd:cd14077  72 HPHICRLRDFLRTPNHYYMLFEYVDGGQLLDYIISHG----KLKEKQARKFARQIASALDYLHRNS--IVHRDLKIENIL 145
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15222437 211 LDSEYNAKLSDFGLAKdgpIGDKSHVSTRVMGTHGYAAPEYL-ATGHLTTKSDVYSFGVVLLELLSGRRAVD 281
Cdd:cd14077 146 ISKSGNIKIIDFGLSN---LYDPRRLLRTFCGSLYFAAPELLqAQPYTGPEVDVWSFGVVLYVLVCGKVPFD 214
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
67-278 1.26e-14

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: 73.02  E-value: 1.26e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGCVFKGwIDEKSLTASRPGTGLViAVKKLNQdgwQGH-QEWLAEVNYLGQFSHRHLVKLIGYCLEDE 145
Cdd:cd14019   2 KYRIIEKIGEGTFSSVYKA-EDKLHDLYDRNKGRLV-ALKHIYP---TSSpSRILNELECLERLGGSNNVSGLITAFRNE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 146 -HRLLVYEFMPRGSLenHLFRRGLYFQPLSWKLRlkvALgaAKGLAFLHSSEtrVIYRDFKTSNILLDSEyNAK--LSDF 222
Cdd:cd14019  77 dQVVAVLPYIEHDDF--RDFYRKMSLTDIRIYLR---NL--FKALKHVHSFG--IIHRDVKPGNFLYNRE-TGKgvLVDF 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15222437 223 GLAKDGPiGDKSHVSTRVmGTHGYAAPEYL-ATGHLTTKSDVYSFGVVLLELLSGRR 278
Cdd:cd14019 147 GLAQREE-DRPEQRAPRA-GTRGFRAPEVLfKCPHQTTAIDIWSAGVILLSILSGRF 201
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
74-273 1.59e-14

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: 73.52  E-value: 1.59e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEF 153
Cdd:cd06643  13 LGDGAFGKVYK---------AQNKETGILAAAKVIDTKSEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILIEF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 154 MPRGSLENHLFRRGlyfQPLSWKLRLKVALGAAKGLAFLHssETRVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPIGDK 233
Cdd:cd06643  84 CAGGAVDAVMLELE---RPLTEPQIRVVCKQTLEALVYLH--ENKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTRTLQ 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 15222437 234 SHVStrVMGTHGYAAPEYLATGH-----LTTKSDVYSFGVVLLEL 273
Cdd:cd06643 159 RRDS--FIGTPYWMAPEVVMCETskdrpYDYKADVWSLGVTLIEM 201
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
74-349 1.70e-14

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: 72.68  E-value: 1.70e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVfKGWIDEKSLTAsrpgtglvIAVKKLNQ-------DGWQGHQEwlaEVNYLGQFSHRHLVKLIGYcLEDEH 146
Cdd:cd14119   1 LGEGSYGKV-KEVLDTETLCR--------RAVKILKKrklrripNGEANVKR---EIQILRRLNHRNVIKLVDV-LYNEE 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 147 RLLVYEFMP--RGSLENHLFRRGLYFQPLSWKLRLKVALgaAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGL 224
Cdd:cd14119  68 KQKLYMVMEycVGGLQEMLDSAPDKRLPIWQAHGYFVQL--IDGLEYLHSQ--GIIHKDIKPGNLLLTTDGTLKISDFGV 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 225 AKDGPIGDKSHVSTRVMGTHGYAAPEyLATGHLT---TKSDVYSFGVVLLELLSGRravdknrpsgernlvewakpYLVN 301
Cdd:cd14119 144 AEALDLFAEDDTCTTSQGSPAFQPPE-IANGQDSfsgFKVDIWSAGVTLYNMTTGK--------------------YPFE 202
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 15222437 302 KRKIFRVIDNRLQDQYSMEEACKVATLSL--RCLTTEIKLRPNMSEVVSH 349
Cdd:cd14119 203 GDNIYKLFENIGKGEYTIPDDVDPDLQDLlrGMLEKDPEKRFTIEQIRQH 252
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
74-276 1.71e-14

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: 73.10  E-value: 1.71e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGwideKSLTASRPgtglvIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCL---EDEHRL-- 148
Cdd:cd13986   8 LGEGGFSFVYLV----EDLSTGRL-----YALKKILCHSKEDVKEAMREIENYRLFNHPNILRLLDSQIvkeAGGKKEvy 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 LVYEFMPRGSLENHLFRRGLYFQPLSWKLRLKVALGAAKGLAFLHSSETR-VIYRDFKTSNILLDSEYNAKLSDFGLAKD 227
Cdd:cd13986  79 LLLPYYKRGSLQDEIERRLVKGTFFPEDRILHIFLGICRGLKAMHEPELVpYAHRDIKPGNVLLSEDDEPILMDLGSMNP 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15222437 228 GPIgdksHVSTRVM-----------GTHGYAAPEYLA--TGH-LTTKSDVYSFGVVLLELLSG 276
Cdd:cd13986 159 ARI----EIEGRREalalqdwaaehCTMPYRAPELFDvkSHCtIDEKTDIWSLGCTLYALMYG 217
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
71-277 1.96e-14

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: 72.75  E-value: 1.96e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  71 DSVLGEGGFGCVFKGWIDEKSLTA---SRPGTGLVIAvkklnqdgwqghqeWLAEVNYLGQFSHRHLVKLiGYCLEDEHR 147
Cdd:cd05073  16 EKKLGAGQFGEVWMATYNKHTKVAvktMKPGSMSVEA--------------FLAEANVMKTLQHDKLVKL-HAVVTKEPI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 148 LLVYEFMPRGSLENHLFRRGLYFQPLSwKLrLKVALGAAKGLAFLHssETRVIYRDFKTSNILLDSEYNAKLSDFGLAKd 227
Cdd:cd05073  81 YIITEFMAKGSLLDFLKSDEGSKQPLP-KL-IDFSAQIAEGMAFIE--QRNYIHRDLRAANILVSASLVCKIADFGLAR- 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15222437 228 gPIGDKSHVSTRvmGTH---GYAAPEYLATGHLTTKSDVYSFGVVLLELLS-GR 277
Cdd:cd05073 156 -VIEDNEYTARE--GAKfpiKWTAPEAINFGSFTIKSDVWSFGILLMEIVTyGR 206
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
67-277 2.01e-14

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: 73.28  E-value: 2.01e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGCVFKGwideksltASRPgTGLVIAVKKLNQDGWQGH-QEWLAEVNYLGQFSHRHLVKLIGYCLEDE 145
Cdd:cd07836   1 NFKQLEKLGEGTYATVYKG--------RNRT-TGEIVALKEIHLDAEEGTpSTAIREISLMKELKHENIVRLHDVIHTEN 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 146 HRLLVYEFMP---RGSLENHLFRRGL------YFQplsWKLrlkvalgaAKGLAFLHssETRVIYRDFKTSNILLDSEYN 216
Cdd:cd07836  72 KLMLVFEYMDkdlKKYMDTHGVRGALdpntvkSFT---YQL--------LKGIAFCH--ENRVLHRDLKPQNLLINKRGE 138
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15222437 217 AKLSDFGLAKDGPIGDKSHVSTRVmgTHGYAAPEYL-ATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd07836 139 LKLADFGLARAFGIPVNTFSNEVV--TLWYRAPDVLlGSRTYSTSIDIWSVGCIMAEMITGR 198
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
73-275 2.31e-14

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


Pssm-ID: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 73.18  E-value: 2.31e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKGwidekSLTASRPGTGLVIAVKKL---NQDGWQGHQEWLAEVNylgqFSHRHLVKLIGyclEDEHRL- 148
Cdd:cd14055   2 LVGKGRFAEVWKA-----KLKQNASGQYETVAVKIFpyeEYASWKNEKDIFTDAS----LKHENILQFLT---AEERGVg 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 ------LVYEFMPRGSLENHLFRRglyfqPLSWKLRLKVALGAAKGLAFLHSSETR-------VIYRDFKTSNILLDSEY 215
Cdd:cd14055  70 ldrqywLITAYHENGSLQDYLTRH-----ILSWEDLCKMAGSLARGLAHLHSDRTPcgrpkipIAHRDLKSSNILVKNDG 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15222437 216 NAKLSDFGLA-KDGPIGDKSHV--STRVmGTHGYAAPEYL-ATGHLT-----TKSDVYSFGVVLLELLS 275
Cdd:cd14055 145 TCVLADFGLAlRLDPSLSVDELanSGQV-GTARYMAPEALeSRVNLEdlesfKQIDVYSMALVLWEMAS 212
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
74-349 2.35e-14

Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase Kinases 3 and 6; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK3 and MKK6 are dual-specificity PKs that phosphorylate and activate their downstream target, p38 MAPK, on specific threonine and tyrosine residues. MKK3/6 play roles in the regulation of cell cycle progression, cytokine- and stress-induced apoptosis, oncogenic transformation, and adult tissue regeneration. In addition, MKK6 plays a critical role in osteoclast survival in inflammatory disease while MKK3 is associated with tumor invasion, progression, and poor patient survival in glioma. The MKK3/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 72.84  E-value: 2.35e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKgwidekslTASRPgTGLVIAVKKLNqdgwqghqewlAEVNYLGQfsHRHLVKLiGYCLEDEHRLLVYEF 153
Cdd:cd06617   9 LGRGAYGVVDK--------MRHVP-TGTIMAVKRIR-----------ATVNSQEQ--KRLLMDL-DISMRSVDCPYTVTF 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 154 MprGSLenhlFRRG---------------LYFQPLSWKLRL------KVALGAAKGLAFLHSsETRVIYRDFKTSNILLD 212
Cdd:cd06617  66 Y--GAL----FREGdvwicmevmdtsldkFYKKVYDKGLTIpedilgKIAVSIVKALEYLHS-KLSVIHRDVKPSNVLIN 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 213 SEYNAKLSDFGLAkdGPIGDkSHVSTRVMGTHGYAAPEY----LATGHLTTKSDVYSFGVVLLELLSGRRAVDKNRPSGE 288
Cdd:cd06617 139 RNGQVKLCDFGIS--GYLVD-SVAKTIDAGCKPYMAPERinpeLNQKGYDVKSDVWSLGITMIELATGRFPYDSWKTPFQ 215
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15222437 289 --RNLVEWAKPYLVNKRkiFRVidnRLQDQYSmeeackvatlslRCLTTEIKLRPNMSEVVSH 349
Cdd:cd06617 216 qlKQVVEEPSPQLPAEK--FSP---EFQDFVN------------KCLKKNYKERPNYPELLQH 261
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
68-277 2.58e-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: 73.33  E-value: 2.58e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  68 FRPDSVLGEGGFGCVFKGwIDEKsltasrpgTGLVIAVKKLN------QDGwqghQEWLAEVNYLGQFSHRHLVKLI--- 138
Cdd:cd07834   2 YELLKPIGSGAYGVVCSA-YDKR--------TGRKVAIKKISnvfddlIDA----KRILREIKILRHLKHENIIGLLdil 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 139 ----GYCLEDEHrlLVYEFMP---------RGSLENHLFRRGLYfQPLswklrlkvalgaaKGLAFLHSSEtrVIYRDFK 205
Cdd:cd07834  69 rppsPEEFNDVY--IVTELMEtdlhkviksPQPLTDDHIQYFLY-QIL-------------RGLKYLHSAG--VIHRDLK 130
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15222437 206 TSNILLDSEYNAKLSDFGLAK-DGPIGDKS----HVSTRvmgthGYAAPEYLATGHLTTKS-DVYSFGVVLLELLSGR 277
Cdd:cd07834 131 PSNILVNSNCDLKICDFGLARgVDPDEDKGflteYVVTR-----WYRAPELLLSSKKYTKAiDIWSVGCIFAELLTRK 203
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
180-349 3.00e-14

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: 72.78  E-value: 3.00e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 180 KVALGAAKGLAFLhSSETRVIYRDFKTSNILLDSEYNAKLSDFGLAkdGPIGDkSHVSTRVMGTHGYAAPEYLATGHLT- 258
Cdd:cd06616 113 KIAVATVKALNYL-KEELKIIHRDVKPSNILLDRNGNIKLCDFGIS--GQLVD-SIAKTRDAGCRPYMAPERIDPSASRd 188
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 259 ---TKSDVYSFGVVLLELLSGRRAVDKNRPSGE--RNLVEWAKPYLvnkrkifrviDNRLQDQYSMEEACKVATlslrCL 333
Cdd:cd06616 189 gydVRSDVWSLGITLYEVATGKFPYPKWNSVFDqlTQVVKGDPPIL----------SNSEEREFSPSFVNFVNL----CL 254
                       170
                ....*....|....*.
gi 15222437 334 TTEIKLRPNMSEVVSH 349
Cdd:cd06616 255 IKDESKRPKYKELLKH 270
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
68-276 3.68e-14

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: 72.12  E-value: 3.68e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  68 FRPDSVLGEGGFGCVFKGWIDEksltasrpgTGLVIAVKKLNQDGWQGH-QEWLAEVNYLGQFSH---RHLVKLIGYCLE 143
Cdd:cd06917   3 YRRLELVGRGSYGAVYRGYHVK---------TGRVVALKVLNLDTDDDDvSDIQKEVALLSQLKLgqpKNIIKYYGSYLK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 144 DEHRLLVYEFMPRGSLENhLFRRGlyfqPLSWKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFG 223
Cdd:cd06917  74 GPSLWIIMDYCEGGSIRT-LMRAG----PIAERYIAVIMREVLVALKFIHKDG--IIHRDIKAANILVTNTGNVKLCDFG 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15222437 224 LAKDGPIGdKSHVSTRVmGTHGYAAPEYLATGHL-TTKSDVYSFGVVLLELLSG 276
Cdd:cd06917 147 VAASLNQN-SSKRSTFV-GTPYWMAPEVITEGKYyDTKADIWSLGITTYEMATG 198
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
73-270 3.92e-14

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: 71.98  E-value: 3.92e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQDGWQGHQEWLAEVNYLGQFS-HRHLVKLIGY-CLEDEHR--- 147
Cdd:cd13985   7 QLGEGGFSYVYL---------AHDVNTGRRYALKRMYFNDEEQLRVAIKEIEIMKRLCgHPNIVQYYDSaILSSEGRkev 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 148 LLVYEFMPrGSLENHLFRRglYFQPLSWKLRLKVALGAAKGLAFLHSSETRVIYRDFKTSNILLDSEYNAKLSDFGLA-- 225
Cdd:cd13985  78 LLLMEYCP-GSLVDILEKS--PPSPLSEEEVLRIFYQICQAVGHLHSQSPPIIHRDIKIENILFSNTGRFKLCDFGSAtt 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15222437 226 KDGPIGDKSHVST-----RVMGTHGYAAPEYL---ATGHLTTKSDVYSFGVVL 270
Cdd:cd13985 155 EHYPLERAEEVNIieeeiQKNTTPMYRAPEMIdlySKKPIGEKADIWALGCLL 207
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
74-277 3.93e-14

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: 72.45  E-value: 3.93e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGwideKSLTasrpgTGLVIAVKKL----NQDGWQGHQewLAEVNYLGQFSHRHLVKLIGYCLEDEHRLL 149
Cdd:cd07861   8 IGEGTYGVVYKG----RNKK-----TGQIVAMKKIrlesEEEGVPSTA--IREISLLKELQHPNIVCLEDVLMQENRLYL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 150 VYEFMPRgSLENHL--FRRGLYFQPLSWKLRLKVALgaaKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAKd 227
Cdd:cd07861  77 VFEFLSM-DLKKYLdsLPKGKYMDAELVKSYLYQIL---QGILFCHSR--RVLHRDLKPQNLLIDNKGVIKLADFGLAR- 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15222437 228 gPIGDKSHVSTRVMGTHGYAAPEYL-ATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd07861 150 -AFGIPVRVYTHEVVTLWYRAPEVLlGSPRYSTPVDIWSIGTIFAEMATKK 199
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
68-275 4.09e-14

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


Pssm-ID: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 72.10  E-value: 4.09e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  68 FRPDSVLGEGGFGCVFKG-WIDEKSLTASrpgtGLVIAVKklnqDGWQGHQ--EWLAEVNYLGQFSHRHLVKLIGYCLED 144
Cdd:cd05043   8 VTLSDLLQEGTFGRIFHGiLRDEKGKEEE----VLVKTVK----DHASEIQvtMLLQESSLLYGLSHQNLLPILHVCIED 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 145 -EHRLLVYEFMPRGSLENHLFRRGL----YFQPLSWKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKL 219
Cdd:cd05043  80 gEKPMVLYPYMNWGNLKLFLQQCRLseanNPQALSTQQLVHMALQIACGMSYLHRRG--VIHKDIAARNCVIDDELQVKI 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15222437 220 SDFGLAKD------GPIGDKSHVSTRVMgthgyaAPEYLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:cd05043 158 TDNALSRDlfpmdyHCLGDNENRPIKWM------SLESLVNKEYSSASDVWSFGVLLWELMT 213
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
60-277 4.21e-14

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: 72.77  E-value: 4.21e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  60 ELKSatRNFRPDSVLGEGGFGCVFKgwidekslTASRPgTGLVIAVKKLNQDGWQG-HQEWLAEVNYLGQFSHRHLVKLI 138
Cdd:cd06649   1 ELKD--DDFERISELGAGNGGVVTK--------VQHKP-SGLIMARKLIHLEIKPAiRNQIIRELQVLHECNSPYIVGFY 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 139 GYCLEDEHRLLVYEFMPRGSLENHLFRRglyfQPLSWKLRLKVALGAAKGLAFLHSSEtRVIYRDFKTSNILLDSEYNAK 218
Cdd:cd06649  70 GAFYSDGEISICMEHMDGGSLDQVLKEA----KRIPEEILGKVSIAVLRGLAYLREKH-QIMHRDVKPSNILVNSRGEIK 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15222437 219 LSDFGLAkdGPIGDKshVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd06649 145 LCDFGVS--GQLIDS--MANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGR 199
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
73-276 6.36e-14

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: 71.56  E-value: 6.36e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKGwIDEKsltasrpgTGLVIAVKKLNQDgWQGHQEWLAEVNYLGQFS-HRHLVKLIGYCLEDEHRL--- 148
Cdd:cd06608  13 VIGEGTYGKVYKA-RHKK--------TGQLAAIKIMDII-EDEEEEIKLEINILRKFSnHPNIATFYGAFIKKDPPGgdd 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 ---LVYEFMPRGS---LENHLFRRGlyfQPLSWKLRLKVALGAAKGLAFLHssETRVIYRDFKTSNILLDSEYNAKLSDF 222
Cdd:cd06608  83 qlwLVMEYCGGGSvtdLVKGLRKKG---KRLKEEWIAYILRETLRGLAYLH--ENKVIHRDIKGQNILLTEEAEVKLVDF 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15222437 223 GLAKDgpigDKSHVSTR--VMGTHGYAAPEYLA-----TGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd06608 158 GVSAQ----LDSTLGRRntFIGTPYWMAPEVIAcdqqpDASYDARCDVWSLGITAIELADG 214
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
72-281 6.36e-14

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


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 71.53  E-value: 6.36e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  72 SVLGEGGFGCVFKG-WIDEKsltasrpgtglvIAVKKLN---QDGWqgHQEwlAEVNYLGQFSHRHLVKLIGYCLEDEHR 147
Cdd:cd14056   1 KTIGKGRYGEVWLGkYRGEK------------VAVKIFSsrdEDSW--FRE--TEIYQTVMLRHENILGFIAADIKSTGS 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 148 ----LLVYEFMPRGSLENHLFRrglyfQPLSWKLRLKVALGAAKGLAFLHS------SETRVIYRDFKTSNILLDSEYNA 217
Cdd:cd14056  65 wtqlWLITEYHEHGSLYDYLQR-----NTLDTEEALRLAYSAASGLAHLHTeivgtqGKPAIAHRDLKSKNILVKRDGTC 139
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15222437 218 KLSDFGLA-------KDGPIGDKSHVstrvmGTHGYAAPEYLaTGHLTTKS-------DVYSFGVVLLELLsgRRAVD 281
Cdd:cd14056 140 CIADLGLAvrydsdtNTIDIPPNPRV-----GTKRYMAPEVL-DDSINPKSfesfkmaDIYSFGLVLWEIA--RRCEI 209
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
74-276 7.17e-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: 71.20  E-value: 7.17e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKG-WIDEksltasrpgtgLVIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYcLEDEHRLLVYE 152
Cdd:cd14150   8 IGTGSFGTVFRGkWHGD-----------VAVKILKVTEPTPEQLQAFKNEMQVLRKTRHVNILLFMGF-MTRPNFAIITQ 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMPRGSLENHLFRRGLYFQPLSwklRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPIGD 232
Cdd:cd14150  76 WCEGSSLYRHLHVTETRFDTMQ---LIDVARQTAQGMDYLHAKN--IIHRDLKSNNIFLHEGLTVKIGDFGLATVKTRWS 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15222437 233 KSHVSTRVMGTHGYAAPEYL---ATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14150 151 GSQQVEQPSGSILWMAPEVIrmqDTNPYSFQSDVYAYGVVLYELMSG 197
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
74-296 7.81e-14

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: 70.82  E-value: 7.81e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGcvfkgwideKSLTASRPGTGLVIAVKKLNQDGWQgHQEWLAEVNYLGQFS-HRHLVKLIGYCLE-DEHRLLVY 151
Cdd:cd13987   1 LGEGTYG---------KVLLAVHKGSGTKMALKFVPKPSTK-LKDFLREYNISLELSvHPHIIKTYDVAFEtEDYYVFAQ 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 152 EFMPRGSL-ENHLFRRGLyfqPLSWKLRLKVALGAAkgLAFLHSSetRVIYRDFKTSNILL-DSEYN-AKLSDFGLAKdg 228
Cdd:cd13987  71 EYAPYGDLfSIIPPQVGL---PEERVKRCAAQLASA--LDFMHSK--NLVHRDIKPENVLLfDKDCRrVKLCDFGLTR-- 141
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15222437 229 PIGdkSHVStRVMGTHGYAAPEYLATGH-----LTTKSDVYSFGVVLLELLSG----RRAVDKNRPSgeRNLVEWAK 296
Cdd:cd13987 142 RVG--STVK-RVSGTIPYTAPEVCEAKKnegfvVDPSIDVWAFGVLLFCCLTGnfpwEKADSDDQFY--EEFVRWQK 213
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
67-349 7.86e-14

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


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 70.73  E-value: 7.86e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGCVFKGwideksltaSRPGTGLVIAVK---KLNQDGW---QGHQEWLAEVNYL---GQFSHRHLVKL 137
Cdd:cd14005   1 QYEVGDLLGKGGFGTVYSG---------VRIRDGLPVAVKfvpKSRVTEWamiNGPVPVPLEIALLlkaSKPGVPGVIRL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 138 IGYCLEDEHRLLVYEFmPRGS--LENHLFRRGLYFQPLSWKLRLKVALgaakglAFLHSSETRVIYRDFKTSNILLDSE- 214
Cdd:cd14005  72 LDWYERPDGFLLIMER-PEPCqdLFDFITERGALSENLARIIFRQVVE------AVRHCHQRGVLHRDIKDENLLINLRt 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 215 YNAKLSDFG---LAKDGPIGDKShvstrvmGTHGYAAPEYLATG-HLTTKSDVYSFGVVLLELLSGRravdknrpsgern 290
Cdd:cd14005 145 GEVKLIDFGcgaLLKDSVYTDFD-------GTRVYSPPEWIRHGrYHGRPATVWSLGILLYDMLCGD------------- 204
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15222437 291 lvewaKPYlVNKRKIfrvIDNRLQDQYSMEEACKvaTLSLRCLTTEIKLRPNMSEVVSH 349
Cdd:cd14005 205 -----IPF-ENDEQI---LRGNVLFRPRLSKECC--DLISRCLQFDPSKRPSLEQILSH 252
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
74-277 8.05e-14

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: 71.63  E-value: 8.05e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQDgwqghQE-------WLAEVNYLGQFSHRHLVKL--------- 137
Cdd:cd07845  15 IGEGTYGIVYR---------ARDTTSGEIVALKKVRMD-----NErdgipisSLREITLLLNLRHPNIVELkevvvgkhl 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 138 ------IGYCLEDEHRLLvyEFMPRGSLENHLfrRGLYFQPLswklrlkvalgaaKGLAFLHssETRVIYRDFKTSNILL 211
Cdd:cd07845  81 dsiflvMEYCEQDLASLL--DNMPTPFSESQV--KCLMLQLL-------------RGLQYLH--ENFIIHRDLKVSNLLL 141
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15222437 212 DSEYNAKLSDFGLAKdgPIGDKSHVSTRVMGTHGYAAPEYL--ATGHlTTKSDVYSFGVVLLELLSGR 277
Cdd:cd07845 142 TDKGCLKIADFGLAR--TYGLPAKPMTPKVVTLWYRAPELLlgCTTY-TTAIDMWAVGCILAELLAHK 206
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
73-277 8.20e-14

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: 71.06  E-value: 8.20e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQD-GWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVY 151
Cdd:cd06619   8 ILGHGNGGTVYK---------AYHLLTRRILAVKVIPLDiTVELQKQIMSELEILYKCDSPYIIGFYGAFFVENRISICT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 152 EFMPRGSLEnhLFRRglyfqpLSWKLRLKVALGAAKGLAFLHSseTRVIYRDFKTSNILLDSEYNAKLSDFGLAKDGpig 231
Cdd:cd06619  79 EFMDGGSLD--VYRK------IPEHVLGRIAVAVVKGLTYLWS--LKILHRDVKPSNMLVNTRGQVKLCDFGVSTQL--- 145
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15222437 232 dKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd06619 146 -VNSIAKTYVGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGR 190
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
72-276 8.45e-14

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: 71.27  E-value: 8.45e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  72 SVLGEGGFGCVFKGWidEKSltasrpgTGLVIAVKKLNQDGWQGHQEWLA--------EVNYLGQFSHRHLVKLIGYCLE 143
Cdd:cd14084  12 RTLGSGACGEVKLAY--DKS-------TCKKVAIKIINKRKFTIGSRREInkprnietEIEILKKLSHPCIIKIEDFFDA 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 144 DEHRLLVYEFMPRGSLENHLFRRGLYFQPLSwKLRLKVALGAAKglaFLHSSEtrVIYRDFKTSNILLDS---EYNAKLS 220
Cdd:cd14084  83 EDDYYIVLELMEGGELFDRVVSNKRLKEAIC-KLYFYQMLLAVK---YLHSNG--IIHRDLKPENVLLSSqeeECLIKIT 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15222437 221 DFGLAKDgpIGDKSHVSTRVmGTHGYAAPEYLATGHL---TTKSDVYSFGVVLLELLSG 276
Cdd:cd14084 157 DFGLSKI--LGETSLMKTLC-GTPTYLAPEVLRSFGTegyTRAVDCWSLGVILFICLSG 212
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
66-285 8.64e-14

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: 71.28  E-value: 8.64e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  66 RNFRPDSVLGEGGFGCVfkgwideksLTASRPGTGLVIAVKKLNQDGWQGHQE---WLAEVNYLGQFSHRHLVKLIgYCL 142
Cdd:cd14209   1 DDFDRIKTLGTGSFGRV---------MLVRHKETGNYYAMKILDKQKVVKLKQvehTLNEKRILQAINFPFLVKLE-YSF 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 143 EDEHRL-LVYEFMPRGSLENHLFRRGLYFQPLSWKLRLKVALGaakgLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSD 221
Cdd:cd14209  71 KDNSNLyMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLA----FEYLHSLD--LIYRDLKPENLLIDQQGYIKVTD 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15222437 222 FGLAKdgpigdksHVSTRVM---GTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVDKNRP 285
Cdd:cd14209 145 FGFAK--------RVKGRTWtlcGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQP 203
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
156-349 9.13e-14

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: 70.97  E-value: 9.13e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 156 RGSLENHLFRRglYFQPLSwklrlkvalgaakgLAFLHSSETRVIYRDFKTSNILLDSEYNAKLSDFGLAK----DGpiG 231
Cdd:cd14165  96 RGALPEDVARK--MFHQLS--------------SAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKrclrDE--N 157
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 232 DKSHVSTRVMGTHGYAAPEYLaTGHL--TTKSDVYSFGVVLLELLSGRRAVDKNrpsgernlvewakpylvNKRKIFRV- 308
Cdd:cd14165 158 GRIVLSKTFCGSAAYAAPEVL-QGIPydPRIYDIWSLGVILYIMVCGSMPYDDS-----------------NVKKMLKIq 219
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 15222437 309 IDNRLQDQYSMEEACKVATLSLRCLTTEIKLRPNMSEVVSH 349
Cdd:cd14165 220 KEHRVRFPRSKNLTSECKDLIYRLLQPDVSQRLCIDEVLSH 260
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
67-278 9.96e-14

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: 70.87  E-value: 9.96e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGCVFKG-WideksltasrPGTGLViAVKKLnQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGyCLEDE 145
Cdd:cd05069  13 SLRLDVKLGQGCFGEVWMGtW----------NGTTKV-AIKTL-KPGTMMPEAFLQEAQIMKKLRHDKLVPLYA-VVSEE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 146 HRLLVYEFMPRGSLENHLFR-RGLYfqpLSWKLRLKVALGAAKGLAFLHssETRVIYRDFKTSNILLDSEYNAKLSDFGL 224
Cdd:cd05069  80 PIYIVTEFMGKGSLLDFLKEgDGKY---LKLPQLVDMAAQIADGMAYIE--RMNYIHRDLRAANILVGDNLVCKIADFGL 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15222437 225 AKdgPIGDKSHVSTRvmGTH---GYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRR 278
Cdd:cd05069 155 AR--LIEDNEYTARQ--GAKfpiKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGR 207
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
134-290 1.09e-13

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: 70.89  E-value: 1.09e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 134 LVKLiGYCLEDEHRL-LVYEFMPRGSLENHLFRRGlYFQPLSWKLrlkvaLGAAKGLAFLHSSETRVIYRDFKTSNILLD 212
Cdd:cd05583  61 LVTL-HYAFQTDAKLhLILDYVNGGELFTHLYQRE-HFTESEVRI-----YIGEIVLALEHLHKLGIIYRDIKLENILLD 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 213 SEYNAKLSDFGLAKDGpIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKS--DVYSFGVVLLELLSGRR--AVDknrpsGE 288
Cdd:cd05583 134 SEGHVVLTDFGLSKEF-LPGENDRAYSFCGTIEYMAPEVVRGGSDGHDKavDWWSLGVLTYELLTGASpfTVD-----GE 207

                ..
gi 15222437 289 RN 290
Cdd:cd05583 208 RN 209
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
72-278 1.33e-13

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: 70.43  E-value: 1.33e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  72 SVLGEGGFGCVFKGWidekSLTASRpgtglVIAVK--KLNQDgWQGHQEW------LAEVNYLGQFSHRHLVKLIGYCLE 143
Cdd:cd13990   6 NLLGKGGFSEVYKAF----DLVEQR-----YVACKihQLNKD-WSEEKKQnyikhaLREYEIHKSLDHPRIVKLYDVFEI 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 144 DEHRLL-VYEFMPRGSLENHLFRRGLyfqpLSWKLRLKVALGAAKGLAFLHSSETRVIYRDFKTSNILLDSEY---NAKL 219
Cdd:cd13990  76 DTDSFCtVLEYCDGNDLDFYLKQHKS----IPEREARSIIMQVVSALKYLNEIKPPIIHYDLKPGNILLHSGNvsgEIKI 151
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 220 SDFGLAKdgpIGDKSHVSTRVM-------GTHGYAAPEYLATG----HLTTKSDVYSFGVVLLELLSGRR 278
Cdd:cd13990 152 TDFGLSK---IMDDESYNSDGMeltsqgaGTYWYLPPECFVVGktppKISSKVDVWSVGVIFYQMLYGRK 218
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
74-275 1.58e-13

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


Pssm-ID: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 70.43  E-value: 1.58e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGwidekSLTASRPGTGL-VIAVKKLnQDGWQG--HQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLV 150
Cdd:cd05091  14 LGEDRFGKVYKG-----HLFGTAPGEQTqAVAIKTL-KDKAEGplREEFRHEAMLRSRLQHPNIVCLLGVVTKEQPMSMI 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 151 YEFMPRGSLENHLFRRGLY---------------FQPLSWklrLKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEY 215
Cdd:cd05091  88 FSYCSHGDLHEFLVMRSPHsdvgstdddktvkstLEPADF---LHIVTQIAAGMEYLSSHH--VVHKDLATRNVLVFDKL 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 216 NAKLSDFGLAKDGPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:cd05091 163 NVKISDLGLFREVYAADYYKLMGNSLLPIRWMSPEAIMYGKFSIDSDIWSYGVVLWEVFS 222
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
73-293 1.62e-13

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: 70.42  E-value: 1.62e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKGwideksltASRPGTGLVIAVKKLNQDGWQGHQEWLA-EVNYLGQFSHRHLVKLIGYCLEDEHRLLVY 151
Cdd:cd14201  13 LVGHGAFAVVFKG--------RHRKKTDWEVAIKSINKKNLSKSQILLGkEIKILKELQHENIVALYDVQEMPNSVFLVM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 152 EFMPRGSLENHLFRRGLYFQPlswklRLKVALGA-AKGLAFLHSSEtrVIYRDFKTSNILLD---------SEYNAKLSD 221
Cdd:cd14201  85 EYCNGGDLADYLQAKGTLSED-----TIRVFLQQiAAAMRILHSKG--IIHRDLKPQNILLSyasrkkssvSGIRIKIAD 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15222437 222 FGLAKdgpIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVDKNRPSGERNLVE 293
Cdd:cd14201 158 FGFAR---YLQSNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQDLRMFYE 226
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
74-349 1.68e-13

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: 70.52  E-value: 1.68e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFkgwidekslTASRPGTGLVIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEF 153
Cdd:cd06655  27 IGQGASGTVF---------TAIDVATGQEVAIKQINLQKQPKKELIINEILVMKELKNPNIVNFLDSFLVGDELFVVMEY 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 154 MPRGSLENHLFRRGLYFQPLSwklrlKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGL-AKDGPigD 232
Cdd:cd06655  98 LAGGSLTDVVTETCMDEAQIA-----AVCRECLQALEFLHANQ--VIHRDIKSDNVLLGMDGSVKLTDFGFcAQITP--E 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 233 KSHVSTRVmGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVDKNRPSGERNLVEW-AKPYLVNKRKIFRVIDN 311
Cdd:cd06655 169 QSKRSTMV-GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATnGTPELQNPEKLSPIFRD 247
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 15222437 312 RLQdqysmeeackvatlslRCLTTEIKLRPNMSEVVSH 349
Cdd:cd06655 248 FLN----------------RCLEMDVEKRGSAKELLQH 269
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
74-273 1.76e-13

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: 70.82  E-value: 1.76e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFkgwidekslTASRPGTGLVIAVKKLNQDGWQGHQEW---LAEVNYLGQFSHRHLVKLIGYCLEDEHRLLV 150
Cdd:cd06634  23 IGHGSFGAVY---------FARDVRNNEVVAIKKMSYSGKQSNEKWqdiIKEVKFLQKLRHPNTIEYRGCYLREHTAWLV 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 151 YEFMpRGSLENHLfrrGLYFQPLSWKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAK-DGP 229
Cdd:cd06634  94 MEYC-LGSASDLL---EVHKKPLQEVEIAAITHGALQGLAYLHSHN--MIHRDVKAGNILLTEPGLVKLGDFGSASiMAP 167
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15222437 230 igdkshvSTRVMGTHGYAAPEYLAT---GHLTTKSDVYSFGVVLLEL 273
Cdd:cd06634 168 -------ANSFVGTPYWMAPEVILAmdeGQYDGKVDVWSLGITCIEL 207
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
141-281 1.82e-13

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: 70.91  E-value: 1.82e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 141 CLEDEHRL-LVYEFMPRGSLENHLFRRGLYFQPLSWKLRLKVALGaakgLAFLHssETRVIYRDFKTSNILLDSEYNAKL 219
Cdd:cd05588  64 CFQTESRLfFVIEFVNGGDLMFHMQRQRRLPEEHARFYSAEISLA----LNFLH--EKGIIYRDLKLDNVLLDSEGHIKL 137
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15222437 220 SDFGLAKDGpIGDKSHVSTrVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVD 281
Cdd:cd05588 138 TDYGMCKEG-LRPGDTTST-FCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPFD 197
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
67-277 1.91e-13

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: 69.59  E-value: 1.91e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGCVFkgwidekslTASRPGTGLVIAVKKLNQDGWQGHQEWLA---EVNYLGQFSHRHLVKLIGYCLE 143
Cdd:cd14081   2 PYRLGKTLGKGQTGLVK---------LAKHCVTGQKVAIKIVNKEKLSKESVLMKverEIAIMKLIEHPNVLKLYDVYEN 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 144 DEHRLLVYEFMPRGSLENHLFRRGlyfqPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFG 223
Cdd:cd14081  73 KKYLYLVLEYVSGGELFDYLVKKG----RLTEKEARKFFRQIISALDYCHSH--SICHRDLKPENLLLDEKNNIKIADFG 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15222437 224 LAKDGPIGDKSHVSTrvmGTHGYAAPEYLATGHLT-TKSDVYSFGVVLLELLSGR 277
Cdd:cd14081 147 MASLQPEGSLLETSC---GSPHYACPEVIKGEKYDgRKADIWSCGVILYALLVGA 198
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
122-276 1.91e-13

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: 70.16  E-value: 1.91e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 122 EVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEFMPRGSLENHLFRRGLYfqplSWKLRLKVALGAAKGLAFLHSSEtrVIY 201
Cdd:cd05612  51 EKRVLKEVSHPFIIRLFWTEHDQRFLYMLMEYVPGGELFSYLRNSGRF----SNSTGLFYASEIVCALEYLHSKE--IVY 124
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15222437 202 RDFKTSNILLDSEYNAKLSDFGLAKDgpIGDKSHVstrVMGTHGYAAPEYLA-TGHlTTKSDVYSFGVVLLELLSG 276
Cdd:cd05612 125 RDLKPENILLDKEGHIKLTDFGFAKK--LRDRTWT---LCGTPEYLAPEVIQsKGH-NKAVDWWALGILIYEMLVG 194
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
67-276 2.03e-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: 2.03e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGcvfkgwideKSLTASRPGTGLVIAVKKLN--QDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLED 144
Cdd:cd14072   1 NYRLLKTIGKGNFA---------KVKLARHVLTGREVAIKIIDktQLNPSSLQKLFREVRIMKILNHPNIVKLFEVIETE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 145 EHRLLVYEFMPRGSLENHLFRRGlyfqplswklRLKVALGAAK------GLAFLHSSetRVIYRDFKTSNILLDSEYNAK 218
Cdd:cd14072  72 KTLYLVMEYASGGEVFDYLVAHG----------RMKEKEARAKfrqivsAVQYCHQK--RIVHRDLKAENLLLDADMNIK 139
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15222437 219 LSDFGLAKDGPIGDKSHVstrVMGTHGYAAPE-YLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14072 140 IADFGFSNEFTPGNKLDT---FCGSPPYAAPElFQGKKYDGPEVDVWSLGVILYTLVSG 195
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
74-349 2.06e-13

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: 69.96  E-value: 2.06e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFkgwidekslTASRPGTGLVIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEF 153
Cdd:cd06647  15 IGQGASGTVY---------TAIDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 154 MPRGSLENHLFRRGLYFQPLSwklrlKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGL-AKDGPigD 232
Cdd:cd06647  86 LAGGSLTDVVTETCMDEGQIA-----AVCRECLQALEFLHSNQ--VIHRDIKSDNILLGMDGSVKLTDFGFcAQITP--E 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 233 KSHVSTRVmGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVDKNRPSGERNLVEW-AKPYLVNKRKIFRVIDN 311
Cdd:cd06647 157 QSKRSTMV-GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATnGTPELQNPEKLSAIFRD 235
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 15222437 312 RLQdqysmeeackvatlslRCLTTEIKLRPNMSEVVSH 349
Cdd:cd06647 236 FLN----------------RCLEMDVEKRGSAKELLQH 257
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
67-283 2.23e-13

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


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 69.60  E-value: 2.23e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGCVF--KGWIDEKSLtasrpgtglVIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLED 144
Cdd:cd08225   1 RYEIIKKIGEGSFGKIYlaKAKSDSEHC---------VIKEIDLTKMPVKEKEASKKEVILLAKMKHPNIVTFFASFQEN 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 145 EHRLLVYEFMPRGSLENHLFR-RGLYF---QPLSWKLRLKValgaakGLAFLHssETRVIYRDFKTSNILLDSE-YNAKL 219
Cdd:cd08225  72 GRLFIVMEYCDGGDLMKRINRqRGVLFsedQILSWFVQISL------GLKHIH--DRKILHRDIKSQNIFLSKNgMVAKL 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15222437 220 SDFGLAKDgpIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVDKN 283
Cdd:cd08225 144 GDFGIARQ--LNDSMELAYTCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGN 205
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
73-276 2.30e-13

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: 69.71  E-value: 2.30e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQDGWQGHQEWLA-EVNYLGQFSHRHLVKLIGYCLEDEHRLLVY 151
Cdd:cd14083  10 VLGTGAFSEVVL---------AEDKATGKLVAIKCIDKKALKGKEDSLEnEIAVLRKIKHPNIVQLLDIYESKSHLYLVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 152 EFMPRGSLENHLFRRGLYFQPLSWKLRLKVaLGAAKglaFLHSSEtrVIYRDFKTSNIL-LDSEYNAKL--SDFGLAKdg 228
Cdd:cd14083  81 ELVTGGELFDRIVEKGSYTEKDASHLIRQV-LEAVD---YLHSLG--IVHRDLKPENLLyYSPDEDSKImiSDFGLSK-- 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15222437 229 pIGDKSHVSTrVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14083 153 -MEDSGVMST-ACGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCG 198
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
72-276 2.33e-13

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: 70.06  E-value: 2.33e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  72 SVLGEGGFGCVFKG-WIDEksltasrpgtgLVIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDeHRLLV 150
Cdd:cd14149  18 TRIGSGSFGTVYKGkWHGD-----------VAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMTKD-NLAIV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 151 YEFMPRGSLENHLFRRGLYFQPLSWklrLKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPI 230
Cdd:cd14149  86 TQWCEGSSLYKHLHVQETKFQMFQL---IDIARQTAQGMDYLHAKN--IIHRDMKSNNIFLHEGLTVKIGDFGLATVKSR 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15222437 231 GDKSHVSTRVMGTHGYAAPEYLA---TGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14149 161 WSGSQQVEQPTGSILWMAPEVIRmqdNNPFSFQSDVYSYGIVLYELMTG 209
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
67-277 2.41e-13

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: 69.60  E-value: 2.41e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGCVFkgwidekslTASRPGTGLVIAVK-----KLNQDGWQgHQeWLAEVNYLGQFSHRHLVKLIGYC 141
Cdd:cd14116   6 DFEIGRPLGKGKFGNVY---------LAREKQSKFILALKvlfkaQLEKAGVE-HQ-LRREVEIQSHLRHPNILRLYGYF 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 142 LEDEHRLLVYEFMPRGSLENHLFRRGLYFQPLSWKLRLKVAlgaaKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSD 221
Cdd:cd14116  75 HDATRVYLILEYAPLGTVYRELQKLSKFDEQRTATYITELA----NALSYCHSK--RVIHRDIKPENLLLGSAGELKIAD 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15222437 222 FGLAKDGPigdkSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd14116 149 FGWSVHAP----SSRRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGK 200
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
74-276 2.44e-13

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 70.62  E-value: 2.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437   74 LGEGGFGCVfkgwideksLTASRPGTGLVIAVKKLNQD---GWQGHQEWLAEVNYLGQFSHRHLVKLigYC-LEDEHRL- 148
Cdd:PTZ00263  26 LGTGSFGRV---------RIAKHKGTGEYYAIKCLKKReilKMKQVQHVAQEKSILMELSHPFIVNM--MCsFQDENRVy 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  149 LVYEFMPRGSLENHLFRRGLYFQPLSWKLRLKVALGaakgLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAKDG 228
Cdd:PTZ00263  95 FLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLA----FEYLHSKD--IIYRDLKPENLLLDNKGHVKVTDFGFAKKV 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 15222437  229 PigDKSHVstrVMGTHGYAAPEYLAT-GHlTTKSDVYSFGVVLLELLSG 276
Cdd:PTZ00263 169 P--DRTFT---LCGTPEYLAPEVIQSkGH-GKAVDWWTMGVLLYEFIAG 211
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
74-276 2.45e-13

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: 70.09  E-value: 2.45e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWIDEksltasrpgTGLVIAVKKL--NQDGWQGHQEWLAEVNYLGQFSHRHLVKLIgYCLEDEHRL-LV 150
Cdd:cd07847   9 IGEGSYGVVFKCRNRE---------TGQIVAIKKFveSEDDPVIKKIALREIRMLKQLKHPNLVNLI-EVFRRKRKLhLV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 151 YEFM-----------PRGsLENHLFRRGLYfQPLswklrlkvalgaaKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKL 219
Cdd:cd07847  79 FEYCdhtvlneleknPRG-VPEHLIKKIIW-QTL-------------QAVNFCHKH--NCIHRDVKPENILITKQGQIKL 141
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15222437 220 SDFGLAK--DGPIGDKS-HVSTRvmgthGYAAPEYLaTGHLT--TKSDVYSFGVVLLELLSG 276
Cdd:cd07847 142 CDFGFARilTGPGDDYTdYVATR-----WYRAPELL-VGDTQygPPVDVWAIGCVFAELLTG 197
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
63-276 2.52e-13

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: 69.56  E-value: 2.52e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  63 SATRNFRPDSVLGEGGFGCVFkgwidekslTASRPGTGLVIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGyCL 142
Cdd:cd14190   1 SSTFSIHSKEVLGGGKFGKVH---------TCTEKRTGLKLAAKVINKQNSKDKEMVLLEIQVMNQLNHRNLIQLYE-AI 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 143 EDEHRL-LVYEFMPRGSLENHLFRRGLYFQPLSWKLRLKvalGAAKGLAFLHssETRVIYRDFKTSNILL--DSEYNAKL 219
Cdd:cd14190  71 ETPNEIvLFMEYVEGGELFERIVDEDYHLTEVDAMVFVR---QICEGIQFMH--QMRVLHLDLKPENILCvnRTGHQVKI 145
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15222437 220 SDFGLAKDGPIGDKSHVStrvMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14190 146 IDFGLARRYNPREKLKVN---FGTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSG 199
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
74-279 2.68e-13

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: 70.00  E-value: 2.68e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKgwideksltASRPGTGLVIAVKK----LNQDGWQghQEWLAEVNYLGQ---FSHRHLVKLIGYCL--ED 144
Cdd:cd07838   7 IGEGAYGTVYK---------ARDLQDGRFVALKKvrvpLSEEGIP--LSTIREIALLKQlesFEHPNVVRLLDVCHgpRT 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 145 EHRL---LVYEFMP---RGSLENHLfRRGL---YFQPLSWKLrlkvalgaAKGLAFLHSSetRVIYRDFKTSNILLDSEY 215
Cdd:cd07838  76 DRELkltLVFEHVDqdlATYLDKCP-KPGLppeTIKDLMRQL--------LRGLDFLHSH--RIVHRDLKPQNILVTSDG 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15222437 216 NAKLSDFGLAKdgpIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSgRRA 279
Cdd:cd07838 145 QVKLADFGLAR---IYSFEMALTSVVVTLWYRAPEVLLQSSYATPVDMWSVGCIFAELFN-RRP 204
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
74-277 2.71e-13

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 69.85  E-value: 2.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437   74 LGEGGFGCVFKgwideksltASRPGTGLVIAVKK--LNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVY 151
Cdd:PLN00009  10 IGEGTYGVVYK---------ARDRVTNETIALKKirLEQEDEGVPSTAIREISLLKEMQHGNIVRLQDVVHSEKRLYLVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  152 EFM-----------PRGSLENHLFRRGLYfQPLSwklrlkvalgaakGLAFLHSSetRVIYRDFKTSNILLDSEYNA-KL 219
Cdd:PLN00009  81 EYLdldlkkhmdssPDFAKNPRLIKTYLY-QILR-------------GIAYCHSH--RVLHRDLKPQNLLIDRRTNAlKL 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15222437  220 SDFGLAKdgPIGDKSHVSTRVMGTHGYAAPE-YLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:PLN00009 145 ADFGLAR--AFGIPVRTFTHEVVTLWYRAPEiLLGSRHYSTPVDIWSVGCIFAEMVNQK 201
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
67-276 2.83e-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: 70.33  E-value: 2.83e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGCVFkgwIDEKsltASRPGTGLVIAVKKLNQDGW------QGHQEwlAEVNYLGQFSHRHLVKLIGY 140
Cdd:cd05614   1 NFELLKVLGTGAYGKVF---LVRK---VSGHDANKLYAMKVLRKAALvqkaktVEHTR--TERNVLEHVRQSPFLVTLHY 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 141 CLEDEHRL-LVYEFMPRGSLENHLFRRGlYFQplswKLRLKVALGAAKgLAFLHSSETRVIYRDFKTSNILLDSEYNAKL 219
Cdd:cd05614  73 AFQTDAKLhLILDYVSGGELFTHLYQRD-HFS----EDEVRFYSGEII-LALEHLHKLGIVYRDIKLENILLDSEGHVVL 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15222437 220 SDFGLAKDGPIGDKSHVSTrVMGTHGYAAPEYL--ATGHlTTKSDVYSFGVVLLELLSG 276
Cdd:cd05614 147 TDFGLSKEFLTEEKERTYS-FCGTIEYMAPEIIrgKSGH-GKAVDWWSLGILMFELLTG 203
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
74-278 2.86e-13

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


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 69.99  E-value: 2.86e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKgWIDEKsltasrpgTGLVIAVKKLNQD-GWQGHQEWLAEVNYLGQFSHRHLVKL------IGYCLEDEH 146
Cdd:cd14038   2 LGTGGFGNVLR-WINQE--------TGEQVAIKQCRQElSPKNRERWCLEIQIMKRLNHPNVVAArdvpegLQKLAPNDL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 147 RLLVYEFMPRGSLENHLFRR----GLYFQPLswklrLKVALGAAKGLAFLHssETRVIYRDFKTSNILL---DSEYNAKL 219
Cdd:cd14038  73 PLLAMEYCQGGDLRKYLNQFenccGLREGAI-----LTLLSDISSALRYLH--ENRIIHRDLKPENIVLqqgEQRLIHKI 145
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15222437 220 SDFGLAKDGpigDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRR 278
Cdd:cd14038 146 IDLGYAKEL---DQGSLCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFR 201
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
74-277 3.15e-13

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: 69.24  E-value: 3.15e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWideksltaSRPGTGLVIAVK-----KLNQdgwQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRL 148
Cdd:cd14121   3 LGSGTYATVYKAY--------RKSGAREVVAVKcvsksSLNK---ASTENLLTEIELLKKLKHPHIVELKDFQWDEEHIY 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 LVYEFMPRGSLENHL-FRRGLyfqPLSWKLRLKVALgaAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNA--KLSDFGLA 225
Cdd:cd14121  72 LIMEYCSGGDLSRFIrSRRTL---PESTVRRFLQQL--ASALQFLREHN--ISHMDLKPQNLLLSSRYNPvlKLADFGFA 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15222437 226 KDGPIGDKSHVstrVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd14121 145 QHLKPNDEAHS---LRGSPLYMAPEMILKKKYDARVDLWSVGVILYECLFGR 193
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
62-277 3.32e-13

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: 70.44  E-value: 3.32e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  62 KSATRNFRPDSVLGEGGFGcvfkgwideKSLTASRPGTGLVIAVKKLNQDGWQGHQE---WLAEVNYLGQFSHRHLVKLi 138
Cdd:cd05594  21 KVTMNDFEYLKLLGKGTFG---------KVILVKEKATGRYYAMKILKKEVIVAKDEvahTLTENRVLQNSRHPFLTAL- 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 139 GYCLEDEHRL-LVYEFMPRGSLENHLFRRGLYFQPlswKLRLKVAlGAAKGLAFLHSsETRVIYRDFKTSNILLDSEYNA 217
Cdd:cd05594  91 KYSFQTHDRLcFVMEYANGGELFFHLSRERVFSED---RARFYGA-EIVSALDYLHS-EKNVVYRDLKLENLMLDKDGHI 165
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 218 KLSDFGLAKDGpIGDKSHVSTrVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd05594 166 KITDFGLCKEG-IKDGATMKT-FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGR 223
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
73-276 3.47e-13

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: 69.37  E-value: 3.47e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKgwideksltASRPGTGLVIAVKKL--NQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLV 150
Cdd:cd07846   8 LVGEGSYGMVMK---------CRHKETGQIVAIKKFleSEDDKMVKKIAMREIKMLKQLRHENLVNLIEVFRRKKRWYLV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 151 YEFMPRGSLEN-HLFRRGLYFQPLSwklrlKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAKDgp 229
Cdd:cd07846  79 FEFVDHTVLDDlEKYPNGLDESRVR-----KYLFQILRGIDFCHSHN--IIHRDIKPENILVSQSGVVKLCDFGFART-- 149
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15222437 230 IGDKSHVSTRVMGTHGYAAPEYLATGHLTTKS-DVYSFGVVLLELLSG 276
Cdd:cd07846 150 LAAPGEVYTDYVATRWYRAPELLVGDTKYGKAvDVWAVGCLVTEMLTG 197
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
67-350 4.03e-13

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: 69.06  E-value: 4.03e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGCVFKGwideKSLTASRpgtglVIAVK--KLNqdgwqgHQEWLAEVNYLGQFSHRHLVKLIGyCLED 144
Cdd:cd14047   7 DFKEIELIGSGGFGQVFKA----KHRIDGK-----TYAIKrvKLN------NEKAEREVKALAKLDHPNIVRYNG-CWDG 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 145 E--------------HRLLVY---EFMPRGSLENHLFRRGlyFQPLSWKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTS 207
Cdd:cd14047  71 FdydpetsssnssrsKTKCLFiqmEFCEKGTLESWIEKRN--GEKLDKVLALEIFEQITKGVEYIHSKK--LIHRDLKPS 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 208 NILLDSEYNAKLSDFGL--AKDGPIGdkshvSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLsgrravdknrp 285
Cdd:cd14047 147 NIFLVDTGKVKIGDFGLvtSLKNDGK-----RTKSKGTLSYMSPEQISSQDYGKEVDIYALGLILFELL----------- 210
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15222437 286 sgernlveWAKPYLVNKRKIF-RVIDNRLQDQYSMEEACKVATLSlRCLTTEIKLRPNMSEVVSHL 350
Cdd:cd14047 211 --------HVCDSAFEKSKFWtDLRNGILPDIFDKRYKIEKTIIK-KMLSKKPEDRPNASEILRTL 267
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
73-277 4.43e-13

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


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 69.72  E-value: 4.43e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGcvfkgwideKSLTASRPGTGLVIAVKKLNQDGWQGHQE---WLAEVNYLGQFSHRHLVKLiGYCLEDEHRL- 148
Cdd:cd05593  22 LLGKGTFG---------KVILVREKASGKYYAMKILKKEVIIAKDEvahTLTESRVLKNTRHPFLTSL-KYSFQTKDRLc 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 LVYEFMPRGSLENHLFRRGLYFQPlswKLRLKVAlGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAKDG 228
Cdd:cd05593  92 FVMEYVNGGELFFHLSRERVFSED---RTRFYGA-EIVSALDYLHSG--KIVYRDLKLENLMLDKDGHIKITDFGLCKEG 165
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15222437 229 pIGDKSHVSTrVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd05593 166 -ITDAATMKT-FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGR 212
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
76-277 4.57e-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: 69.18  E-value: 4.57e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  76 EGGFGCVFKGwiDEKSltasrpgTGLVIAVKKLNQDGwqgHQE-----WLAEVNYLGQFSHRHLVKL----IGYCLEDEH 146
Cdd:cd07843  15 EGTYGVVYRA--RDKK-------TGEIVALKKLKMEK---EKEgfpitSLREINILLKLQHPNIVTVkevvVGSNLDKIY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 147 rlLVYEFMP---RGSLENH--LFRRG----LYFQPLSwklrlkvalgaakGLAFLHssETRVIYRDFKTSNILLDSEYNA 217
Cdd:cd07843  83 --MVMEYVEhdlKSLMETMkqPFLQSevkcLMLQLLS-------------GVAHLH--DNWILHRDLKTSNLLLNNRGIL 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15222437 218 KLSDFGLAKdgPIGDKSHVSTRVMGTHGYAAPE-YLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd07843 146 KICDFGLAR--EYGSPLKPYTQLVVTLWYRAPElLLGAKEYSTAIDMWSVGCIFAELLTKK 204
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
74-273 4.87e-13

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: 68.49  E-value: 4.87e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEF 153
Cdd:cd06613   8 IGSGTYGDVYK---------ARNIATGELAAVKVIKLEPGDDFEIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVMEY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 154 MPRGSLENHLFRRGlyfqPLSWKLRLKVALGAAKGLAFLHssETRVIYRDFKTSNILLDSEYNAKLSDFGLAkdGPIGDK 233
Cdd:cd06613  79 CGGGSLQDIYQVTG----PLSELQIAYVCRETLKGLAYLH--STGKIHRDIKGANILLTEDGDVKLADFGVS--AQLTAT 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 15222437 234 SHVSTRVMGTHGYAAPEYLA---TGHLTTKSDVYSFGVVLLEL 273
Cdd:cd06613 151 IAKRKSFIGTPYWMAPEVAAverKGGYDGKCDIWALGITAIEL 193
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
68-276 5.17e-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: 69.71  E-value: 5.17e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  68 FRPDSVLGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQDGW---QGHQEWLAEVNYLGQFSHRH--LVKLIGYCL 142
Cdd:cd05633   7 FSVHRIIGRGGFGEVYG---------CRKADTGKMYAMKCLDKKRIkmkQGETLALNERIMLSLVSTGDcpFIVCMTYAF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 143 EDEHRL-LVYEFMPRGSLENHLFRRGLYFQPlswKLRLkVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSD 221
Cdd:cd05633  78 HTPDKLcFILDLMNGGDLHYHLSQHGVFSEK---EMRF-YATEIILGLEHMHNR--FVVYRDLKPANILLDEHGHVRISD 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15222437 222 FGLAKDGPiGDKSHVStrvMGTHGYAAPEYLATG-HLTTKSDVYSFGVVLLELLSG 276
Cdd:cd05633 152 LGLACDFS-KKKPHAS---VGTHGYMAPEVLQKGtAYDSSADWFSLGCMLFKLLRG 203
PK_GC-C cd14044
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain ...
102-355 6.01e-13

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-C binds and is activated by the intestinal hormones, guanylin (GN) and uroguanylin (UGN), which are secreted after salty meals to inhibit sodium absorption and induce the secretion of chloride, bicarbonate, and water. GN and UGN are also present in the kidney, where they induce increased salt and water secretion. This prevents the development of hypernatremia and hypervolemia after ingestion of high amounts of salt. 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 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-C 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: 270946 [Multi-domain]  Cd Length: 271  Bit Score: 68.76  E-value: 6.01e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 102 VIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEFMPRGSLENHLFRRGLYFQP--LSWKLRL 179
Cdd:cd14044  33 VVILKDLKNNEGNFTEKQKIELNKLLQIDYYNLTKFYGTVKLDTMIFGVIEYCERGSLRDVLNDKISYPDGtfMDWEFKI 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 180 KVALGAAKGLAFLHSSETRVIYRdFKTSNILLDSEYNAKLSDFGLakdgpigdKSHVSTRvmgTHGYAAPEYLATGHLTT 259
Cdd:cd14044 113 SVMYDIAKGMSYLHSSKTEVHGR-LKSTNCVVDSRMVVKITDFGC--------NSILPPS---KDLWTAPEHLRQAGTSQ 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 260 KSDVYSFGVVLLELLSgRRAVDKNRPSGERnlvewakpylvnKRKIFRVIDNR--------LQDQYSMEEACKVATLSLR 331
Cdd:cd14044 181 KGDVYSYGIIAQEIIL-RKETFYTAACSDR------------KEKIYRVQNPKgmkpfrpdLNLESAGEREREVYGLVKN 247
                       250       260
                ....*....|....*....|....
gi 15222437 332 CLTTEIKLRPNMSEVVSHLEHIQS 355
Cdd:cd14044 248 CWEEDPEKRPDFKKIENTLAKIFS 271
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
67-274 6.40e-13

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: 68.75  E-value: 6.40e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGCVFKgwideksltASRPGTGLVIAVKKL---NQDgwQGHQEWLAEVNYLGQFSHRHLVKLIGYCLE 143
Cdd:cd14048   7 DFEPIQCLGRGGFGVVFE---------AKNKVDDCNYAVKRIrlpNNE--LAREKVLREVRALAKLDHPGIVRYFNAWLE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 144 ----------DEHRL-LVYEFMPRGSLENHLFRR-GLYFQPLSWKLRLKVALgaAKGLAFLHSSEtrVIYRDFKTSNILL 211
Cdd:cd14048  76 rppegwqekmDEVYLyIQMQLCRKENLKDWMNRRcTMESRELFVCLNIFKQI--ASAVEYLHSKG--LIHRDLKPSNVFF 151
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15222437 212 DSEYNAKLSDFGLAKDGPIGDK----------SHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELL 274
Cdd:cd14048 152 SLDDVVKVGDFGLVTAMDQGEPeqtvltpmpaYAKHTGQVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELI 224
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
73-276 6.42e-13

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: 68.27  E-value: 6.42e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQDGWQGHQEWLA----EVNYLGQFSHRHLVKLIGYCLEDEHRL 148
Cdd:cd14098   7 RLGSGTFAEVKK---------AVEVETGKMRAIKQIVKRKVAGNDKNLQlfqrEINILKSLEHPGIVRLIDWYEDDQHIY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 LVYEFMPRGSLENHLFRRGLYFQPLSWKLRLKValgaAKGLAFLHSSEtrVIYRDFKTSNILL--DSEYNAKLSDFGLAK 226
Cdd:cd14098  78 LVMEYVEGGDLMDFIMAWGAIPEQHARELTKQI----LEAMAYTHSMG--ITHRDLKPENILItqDDPVIVKISDFGLAK 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15222437 227 dgPIGDKSHVSTRVmGTHGYAAPEYLAT------GHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14098 152 --VIHTGTFLVTFC-GTMAYLAPEILMSkeqnlqGGYSNLVDMWSVGCLVYVMLTG 204
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
73-276 7.83e-13

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: 68.89  E-value: 7.83e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGcvfkgwideKSLTASRPGTGLVIAVKKLNQDGWQGHQE---WLAEVN-YLGQFSHRHLVKLiGYCLEDEHRL 148
Cdd:cd05602  14 VIGKGSFG---------KVLLARHKSDEKFYAVKVLQKKAILKKKEekhIMSERNvLLKNVKHPFLVGL-HFSFQTTDKL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 -LVYEFMPRGSLENHLFRRGLYFQPlswKLRLKVAlGAAKGLAFLHSseTRVIYRDFKTSNILLDSEYNAKLSDFGLAKD 227
Cdd:cd05602  84 yFVLDYINGGELFYHLQRERCFLEP---RARFYAA-EIASALGYLHS--LNIVYRDLKPENILLDSQGHIVLTDFGLCKE 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15222437 228 GpIGDKSHVSTrVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd05602 158 N-IEPNGTTST-FCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYG 204
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
141-281 8.74e-13

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: 68.89  E-value: 8.74e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 141 CLEDEHRL-LVYEFMPRGSLENHLFRRglyfQPLSWKLRLKVALGAAKGLAFLHssETRVIYRDFKTSNILLDSEYNAKL 219
Cdd:cd05617  84 CFQTTSRLfLVIEYVNGGDLMFHMQRQ----RKLPEEHARFYAAEICIALNFLH--ERGIIYRDLKLDNVLLDADGHIKL 157
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15222437 220 SDFGLAKDGpIGDKSHVSTrVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVD 281
Cdd:cd05617 158 TDYGMCKEG-LGPGDTTST-FCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFD 217
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
74-293 9.35e-13

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: 67.78  E-value: 9.35e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWIDEKsltasrpgTGLVIAVKKLNQDGWQGHQEWLA-EVNYLGQFSHRHLVKLIGYCLEDEHRLLVYE 152
Cdd:cd14120   1 IGHGAFAVVFKGRHRKK--------PDLPVAIKCITKKNLSKSQNLLGkEIKILKELSHENVVALLDCQETSSSVYLVME 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMPRGSLENHLFRRGlyfqPLS---WKLRLKVALGAAKGLaflhsSETRVIYRDFKTSNILLD---------SEYNAKLS 220
Cdd:cd14120  73 YCNGGDLADYLQAKG----TLSedtIRVFLQQIAAAMKAL-----HSKGIVHRDLKPQNILLShnsgrkpspNDIRLKIA 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15222437 221 DFGLAKdgpigdksHVSTRVM-----GTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVDKNRPSGERNLVE 293
Cdd:cd14120 144 DFGFAR--------FLQDGMMaatlcGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQAQTPQELKAFYE 213
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
74-276 9.91e-13

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: 68.14  E-value: 9.91e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVfkgwideksLTASRPGTGLVIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEF 153
Cdd:cd06658  30 IGEGSTGIV---------CIATEKHTGKQVAVKKMDLRKQQRRELLFNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEF 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 154 MPRGSLENHLFRRGLYFQPLSwklrlKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAKDgpIGDK 233
Cdd:cd06658 101 LEGGALTDIVTHTRMNEEQIA-----TVCLSVLRALSYLHNQG--VIHRDIKSDSILLTSDGRIKLSDFGFCAQ--VSKE 171
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 15222437 234 SHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd06658 172 VPKRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDG 214
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
74-277 1.01e-12

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: 67.65  E-value: 1.01e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFG-CVFKGWIDEKSLTASR--PGTGLVIAVKKlnqdgwqghQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLV 150
Cdd:cd14187  15 LGKGGFAkCYEITDADTKEVFAGKivPKSLLLKPHQK---------EKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 151 YEFMPRGSL-ENHLFRRGLYFQPLSWKLRLKVAlgaakGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAKDgp 229
Cdd:cd14187  86 LELCRRRSLlELHKRRKALTEPEARYYLRQIIL-----GCQYLHRN--RVIHRDLKLGNLFLNDDMEVKIGDFGLATK-- 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15222437 230 IGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd14187 157 VEYDGERKKTLCGTPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGK 204
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
66-274 1.02e-12

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: 67.92  E-value: 1.02e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  66 RNFRPDSVLGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQDGWQGH--QEWLAEVNYLGQFSHRHLVKLIGYCLE 143
Cdd:cd14049   6 NEFEEIARLGKGGYGKVYK---------VRNKLDGQYYAIKKILIKKVTKRdcMKVLREVKVLAGLQHPNIVGYHTAWME 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 144 DEHrLLVYEFMP--RGSLENHL-----------FRRGLY-FQPLSWKLRLKVALgaAKGLAFLHSSEtrVIYRDFKTSNI 209
Cdd:cd14049  77 HVQ-LMLYIQMQlcELSLWDWIvernkrpceeeFKSAPYtPVDVDVTTKILQQL--LEGVTYIHSMG--IVHRDLKPRNI 151
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15222437 210 LLD-SEYNAKLSDFGLA-------------KDGPIGdkSHVSTRVmGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELL 274
Cdd:cd14049 152 FLHgSDIHVRIGDFGLAcpdilqdgndsttMSRLNG--LTHTSGV-GTCLYAAPEQLEGSHYDFKSDMYSIGVILLELF 227
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
122-276 1.31e-12

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: 67.69  E-value: 1.31e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 122 EVNYLGQFS-HRHLVKLIGYCLEDEHRLLVYEFMPRGSLENHLFRRglyfQPLSWKLRLKVALGAAKGLAFLHSSEtrVI 200
Cdd:cd14181  65 EIHILRQVSgHPSIITLIDSYESSTFIFLVFDLMRRGELFDYLTEK----VTLSEKETRSIMRSLLEAVSYLHANN--IV 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 201 YRDFKTSNILLDSEYNAKLSDFGLAKDGPIGDKSHvstRVMGTHGYAAPEYLATGHLTT------KSDVYSFGVVLLELL 274
Cdd:cd14181 139 HRDLKPENILLDDQLHIKLSDFGFSCHLEPGEKLR---ELCGTPGYLAPEILKCSMDEThpgygkEVDLWACGVILFTLL 215

                ..
gi 15222437 275 SG 276
Cdd:cd14181 216 AG 217
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
67-276 1.39e-12

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: 68.15  E-value: 1.39e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQDGW---QGHQEWLAEVNYLGQFSHRH--LVKLIGYC 141
Cdd:cd14223   1 DFSVHRIIGRGGFGEVYG---------CRKADTGKMYAMKCLDKKRIkmkQGETLALNERIMLSLVSTGDcpFIVCMSYA 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 142 LEDEHRL-LVYEFMPRGSLENHLFRRGLYFQPLSWKLRLKVALGAAkglaflHSSETRVIYRDFKTSNILLDSEYNAKLS 220
Cdd:cd14223  72 FHTPDKLsFILDLMNGGDLHYHLSQHGVFSEAEMRFYAAEIILGLE------HMHSRFVVYRDLKPANILLDEFGHVRIS 145
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15222437 221 DFGLAKDGPiGDKSHVStrvMGTHGYAAPEYLATG-HLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14223 146 DLGLACDFS-KKKPHAS---VGTHGYMAPEVLQKGvAYDSSADWFSLGCMLFKLLRG 198
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
73-349 1.44e-12

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: 67.34  E-value: 1.44e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFkgwiDEKSLTASRPGTGLVIAVKKLNQDgwqgHQEWL--AEVNYLGQFSHRHLVKLIGYCLEDEHRLLV 150
Cdd:cd14188   8 VLGKGGFAKCY----EMTDLTTNKVYAAKIIPHSRVSKP----HQREKidKEIELHRILHHKHVVQFYHYFEDKENIYIL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 151 YEFMPRGSLENHLFRRGLYFQP-LSWKLRLKVAlgaakGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGL-AKDG 228
Cdd:cd14188  80 LEYCSRRSMAHILKARKVLTEPeVRYYLRQIVS-----GLKYLHEQE--ILHRDLKLGNFFINENMELKVGDFGLaARLE 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 229 PIGDKSHVstrVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGrravdknRPSGERnlvewakpylVNKRKIFRV 308
Cdd:cd14188 153 PLEHRRRT---ICGTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLG-------RPPFET----------TNLKETYRC 212
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 15222437 309 IDnrlQDQYSMEEACKVATLSL--RCLTTEIKLRPNMSEVVSH 349
Cdd:cd14188 213 IR---EARYSLPSSLLAPAKHLiaSMLSKNPEDRPSLDEIIRH 252
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
74-278 1.46e-12

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: 67.40  E-value: 1.46e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWIDEKSltasrpgtglVIAVKKLnQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGyCLEDEHRLLVYEF 153
Cdd:cd05070  17 LGNGQFGEVWMGTWNGNT----------KVAIKTL-KPGTMSPESFLEEAQIMKKLKHDKLVQLYA-VVSEEPIYIVTEY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 154 MPRGSLenHLFRRGLYFQPLSWKLRLKVALGAAKGLAFLHssETRVIYRDFKTSNILLDSEYNAKLSDFGLAKdgPIGDK 233
Cdd:cd05070  85 MSKGSL--LDFLKDGEGRALKLPNLVDMAAQVAAGMAYIE--RMNYIHRDLRSANILVGNGLICKIADFGLAR--LIEDN 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15222437 234 SHVSTRvmGTH---GYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRR 278
Cdd:cd05070 159 EYTARQ--GAKfpiKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGR 204
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
68-274 1.48e-12

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: 67.68  E-value: 1.48e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  68 FRPDSVLGEGGFGCVFKgwideksltASRPGTGLVIAVKKL----NQDGWQ-GHQEWLAEVNYLGQFSHRHLVKLIGYC- 141
Cdd:cd07863   2 YEPVAEIGVGAYGTVYK---------ARDPHSGHFVALKSVrvqtNEDGLPlSTVREVALLKRLEAFDHPNIVRLMDVCa 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 142 ---LEDEHRL-LVYEFMPRgSLENHLFRR---GLYFQPLswKLRLKVALgaaKGLAFLHSSetRVIYRDFKTSNILLDSE 214
Cdd:cd07863  73 tsrTDRETKVtLVFEHVDQ-DLRTYLDKVpppGLPAETI--KDLMRQFL---RGLDFLHAN--CIVHRDLKPENILVTSG 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 215 YNAKLSDFGLAKdgpIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELL 274
Cdd:cd07863 145 GQVKLADFGLAR---IYSCQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMF 201
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
74-280 1.65e-12

Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin receptor-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR1, also called Activin receptor-Like Kinase 2 (ALK2), and ALK1 act as receptors for bone morphogenetic proteins (BMPs) and they activate SMAD1/5/8. ACVR1 is widely expressed while ALK1 is limited mainly to endothelial cells. The specificity of BMP binding to type I receptors is affected by type II receptors. ACVR1 binds BMP6/7/9/10 and can also bind anti-Mullerian hormone (AMH) in the presence of AMHR2. ALK1 binds BMP9/10 as well as TGFbeta in endothelial cells. A missense mutation in the GS domain of ACVR1 causes fibrodysplasia ossificans progressiva, a complex and disabling disease characterized by congenital skeletal malformations and extraskeletal bone formation. ACVR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like ACVR1 and ALK1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The ACVR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 67.47  E-value: 1.65e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKG-WIDEKsltasrpgtglvIAVKKLNQdgwQGHQEWLAEVNYLGQFSHRHlVKLIGYCLED------EH 146
Cdd:cd14142  13 IGKGRYGEVWRGqWQGES------------VAVKIFSS---RDEKSWFRETEIYNTVLLRH-ENILGFIASDmtsrnsCT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 147 RL-LVYEFMPRGSLENHLFRrglyfQPLSWKLRLKVALGAAKGLAFLHS------SETRVIYRDFKTSNILLDSEYNAKL 219
Cdd:cd14142  77 QLwLITHYHENGSLYDYLQR-----TTLDHQEMLRLALSAASGLVHLHTeifgtqGKPAIAHRDLKSKNILVKSNGQCCI 151
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15222437 220 SDFGLA----KDGPIGDKSHvSTRVmGTHGYAAPEYLATGHLTT------KSDVYSFGVVLLELlsGRRAV 280
Cdd:cd14142 152 ADLGLAvthsQETNQLDVGN-NPRV-GTKRYMAPEVLDETINTDcfesykRVDIYAFGLVLWEV--ARRCV 218
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
141-281 1.75e-12

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: 68.14  E-value: 1.75e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 141 CLEDEHRLL-VYEFMPRGSLENHLFRRGLYFQPLSWKLRLKVALGaakgLAFLHssETRVIYRDFKTSNILLDSEYNAKL 219
Cdd:cd05618  89 CFQTESRLFfVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLA----LNYLH--ERGIIYRDLKLDNVLLDSEGHIKL 162
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15222437 220 SDFGLAKDGpIGDKSHVSTrVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVD 281
Cdd:cd05618 163 TDYGMCKEG-LRPGDTTST-FCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFD 222
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
72-349 1.94e-12

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: 66.64  E-value: 1.94e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  72 SVLGEGGFGCVfkgwideksLTASRPGTGLVIAVK-----KLNQDGWQGHQEwLAEV-------NYLGQFSHRHLVKLIG 139
Cdd:cd14004   6 KEMGEGAYGQV---------NLAIYKSKGKEVVIKfifkeRILVDTWVRDRK-LGTVpleihilDTLNKRSHPNIVKLLD 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 140 YCLEDEHRLLVyefMPRGSLENHLFRRgLYFQP-LSWKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAK 218
Cdd:cd14004  76 FFEDDEFYYLV---MEKHGSGMDLFDF-IERKPnMDEKEAKYIFRQVADAVKHLHDQG--IVHRDIKDENVILDGNGTIK 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 219 LSDFGLA---KDGPIgdkshvSTRVmGTHGYAAPEYLA-TGHLTTKSDVYSFGVVLLELLSGRravdknrpsgernlvew 294
Cdd:cd14004 150 LIDFGSAayiKSGPF------DTFV-GTIDYAAPEVLRgNPYGGKEQDIWALGVLLYTLVFKE----------------- 205
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15222437 295 aKPYLvnkrKIFRVIDNRLQDQYSMEEACkvATLSLRCLTTEIKLRPNMSEVVSH 349
Cdd:cd14004 206 -NPFY----NIEEILEADLRIPYAVSEDL--IDLISRMLNRDVGDRPTIEELLTD 253
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
67-276 1.97e-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: 67.64  E-value: 1.97e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGCVfkgWIDEKSLTasrpgtGLVIAVKKL--------NQdgwQGHQEwlAEVNYLGQFSHRHLVKLI 138
Cdd:cd05599   2 DFEPLKVIGRGAFGEV---RLVRKKDT------GHVYAMKKLrksemlekEQ---VAHVR--AERDILAEADNPWVVKLY 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 139 gYCLEDEHRL-LVYEFMPRGSLENHLFRRGLyfqpLSWKL------RLKVALGAAKGLAFLHssetrviyRDFKTSNILL 211
Cdd:cd05599  68 -YSFQDEENLyLIMEFLPGGDMMTLLMKKDT----LTEEEtrfyiaETVLAIESIHKLGYIH--------RDIKPDNLLL 134
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15222437 212 DSEYNAKLSDFGLAKdgPIgDKSHVSTRVMGTHGYAAPE-YLATGHlTTKSDVYSFGVVLLELLSG 276
Cdd:cd05599 135 DARGHIKLSDFGLCT--GL-KKSHLAYSTVGTPDYIAPEvFLQKGY-GKECDWWSLGVIMYEMLIG 196
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
172-277 2.08e-12

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 68.67  E-value: 2.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  172 PLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAKdgpigdksHVST-------RVMGTH 244
Cdd:NF033483 103 PLSPEEAVEIMIQILSALEHAHRN--GIVHRDIKPQNILITKDGRVKVTDFGIAR--------ALSSttmtqtnSVLGTV 172
                         90       100       110
                 ....*....|....*....|....*....|...
gi 15222437  245 GYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:NF033483 173 HYLSPEQARGGTVDARSDIYSLGIVLYEMLTGR 205
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
67-276 2.43e-12

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: 66.48  E-value: 2.43e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGCVFKgwIDEKSltasrpgTGLVIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEH 146
Cdd:cd14193   5 NVNKEEILGGGRFGQVHK--CEEKS-------SGLKLAAKIIKARSQKEKEEVKNEIEVMNQLNHANLIQLYDAFESRND 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 147 RLLVYEFMPRGSLENHLFRRGLYFQPLSWKLRLKVALgaaKGLAFLHssETRVIYRDFKTSNILLDSE--YNAKLSDFGL 224
Cdd:cd14193  76 IVLVMEYVDGGELFDRIIDENYNLTELDTILFIKQIC---EGIQYMH--QMYILHLDLKPENILCVSReaNQVKIIDFGL 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15222437 225 AKDGPIGDKSHVStrvMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14193 151 ARRYKPREKLRVN---FGTPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSG 199
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
74-349 2.74e-12

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: 66.93  E-value: 2.74e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVfkgwideksLTASRPGTGLVIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEF 153
Cdd:cd06659  29 IGEGSTGVV---------CIAREKHSGRQVAVKMMDLRKQQRRELLFNEVVIMRDYQHPNVVEMYKSYLVGEELWVLMEY 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 154 MPRGSLENHLFRRGLYFQPLSwklrlKVALGAAKGLAFLHSseTRVIYRDFKTSNILLDSEYNAKLSDFG----LAKDGP 229
Cdd:cd06659 100 LQGGALTDIVSQTRLNEEQIA-----TVCEAVLQALAYLHS--QGVIHRDIKSDSILLTLDGRVKLSDFGfcaqISKDVP 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 230 iGDKSHVstrvmGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVDKNRP-SGERNLVEWAKPYLVNKRKIFRV 308
Cdd:cd06659 173 -KRKSLV-----GTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPvQAMKRLRDSPPPKLKNSHKASPV 246
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 15222437 309 IDNRLQdqysmeeackvatlslRCLTTEIKLRPNMSEVVSH 349
Cdd:cd06659 247 LRDFLE----------------RMLVRDPQERATAQELLDH 271
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
73-281 2.77e-12

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


Pssm-ID: 271043 [Multi-domain]  Cd Length: 290  Bit Score: 66.99  E-value: 2.77e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKGWIDEKSltasrpgtglvIAVKKLN-QDGWQGHQEWlaEVNYLGQFSHRHLVKLIGYCLE----DEHR 147
Cdd:cd14141   2 IKARGRFGCVWKAQLLNEY-----------VAVKIFPiQDKLSWQNEY--EIYSLPGMKHENILQFIGAEKRgtnlDVDL 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 148 LLVYEFMPRGSLENHLfrrglYFQPLSWKLRLKVALGAAKGLAFLHSS--------ETRVIYRDFKTSNILLDSEYNAKL 219
Cdd:cd14141  69 WLITAFHEKGSLTDYL-----KANVVSWNELCHIAQTMARGLAYLHEDipglkdghKPAIAHRDIKSKNVLLKNNLTACI 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15222437 220 SDFGLAKDGPIGDKSHVSTRVMGTHGYAAPEYLaTGHLT------TKSDVYSFGVVLLELLSGRRAVD 281
Cdd:cd14141 144 ADFGLALKFEAGKSAGDTHGQVGTRRYMAPEVL-EGAINfqrdafLRIDMYAMGLVLWELASRCTASD 210
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
121-276 2.81e-12

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


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 66.19  E-value: 2.81e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 121 AEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEFMPRGSLENHLFRRGlyfqPLSWKLRLKVALGAAKGLAFLHSSetRVI 200
Cdd:cd13995  45 SDVEIQACFRHENIAELYGALLWEETVHLFMEAGEGGSVLEKLESCG----PMREFEIIWVTKHVLKGLDFLHSK--NII 118
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15222437 201 YRDFKTSNILLDSEyNAKLSDFGLAKDgpIGDKSHVSTRVMGTHGYAAPEY-LATGHlTTKSDVYSFGVVLLELLSG 276
Cdd:cd13995 119 HHDIKPSNIVFMST-KAVLVDFGLSVQ--MTEDVYVPKDLRGTEIYMSPEViLCRGH-NTKADIYSLGATIIHMQTG 191
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
72-276 3.06e-12

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: 66.42  E-value: 3.06e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  72 SVLGEGGFGCVFKGWIDEksltasrpgTGLVIAVKKLNQD--GWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLL 149
Cdd:cd14097   7 RKLGQGSFGVVIEATHKE---------TQTKWAIKKINREkaGSSAVKLLEREVDILKHVNHAHIIHLEEVFETPKRMYL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 150 VYEFMPRGSLENHLFRRGLYfqplSWKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDS-------EYNAKLSDF 222
Cdd:cd14097  78 VMELCEDGELKELLLRKGFF----SENETRHIIQSLASAVAYLHKND--IVHRDLKLENILVKSsiidnndKLNIKVTDF 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15222437 223 GLAKDGPIGDKSHVsTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14097 152 GLSVQKYGLGEDML-QETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCG 204
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
74-349 3.14e-12

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: 66.67  E-value: 3.14e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFkgwidekslTASRPGTGLVIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEF 153
Cdd:cd06654  28 IGQGASGTVY---------TAMDVATGQEVAIRQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 154 MPRGSLENHLFRRGLYFQPLSwklrlKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGL-AKDGPigD 232
Cdd:cd06654  99 LAGGSLTDVVTETCMDEGQIA-----AVCRECLQALEFLHSNQ--VIHRDIKSDNILLGMDGSVKLTDFGFcAQITP--E 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 233 KSHVSTRVmGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVDKNRPSGERNLVEW-AKPYLVNKRKIFRVIDN 311
Cdd:cd06654 170 QSKRSTMV-GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATnGTPELQNPEKLSAIFRD 248
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 15222437 312 RLQdqysmeeackvatlslRCLTTEIKLRPNMSEVVSH 349
Cdd:cd06654 249 FLN----------------RCLEMDVEKRGSAKELLQH 270
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
74-349 3.20e-12

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: 66.29  E-value: 3.20e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFkgWIDEKSLTASRPGTGLV-IAVKKLNQDGWQGHqewLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYE 152
Cdd:cd08222   8 LGSGNFGTVY--LVSDLKATADEELKVLKeISVGELQPDETVDA---NREAKLLSKLDHPAIVKFHDSFVEKESFCIVTE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMPRGSLENHL---FRRGLYFQP---LSWKLRLKVALgaakglAFLHssETRVIYRDFKTSNILLDSEYnAKLSDFGLAK 226
Cdd:cd08222  83 YCEGGDLDDKIseyKKSGTTIDEnqiLDWFIQLLLAV------QYMH--ERRILHRDLKAKNIFLKNNV-IKVGDFGISR 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 227 dgPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVD-KNRPSGERNLVEWAKPylvnkrki 305
Cdd:cd08222 154 --ILMGTSDLATTFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDgQNLLSVMYKIVEGETP-------- 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 15222437 306 frvidnRLQDQYSMEeackVATLSLRCLTTEIKLRPNMSEVVSH 349
Cdd:cd08222 224 ------SLPDKYSKE----LNAIYSRMLNKDPALRPSAAEILKI 257
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
74-278 3.69e-12

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: 66.30  E-value: 3.69e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWIDEksltasrpgTGLVIAVKK--LNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGyCLEDEHRL-LV 150
Cdd:cd07839   8 IGEGTYGTVFKAKNRE---------THEIVALKRvrLDDDDEGVPSSALREICLLKELKHKNIVRLYD-VLHSDKKLtLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 151 YEFMP----------RGSLENHLFRrGLYFQPLswklrlkvalgaaKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLS 220
Cdd:cd07839  78 FEYCDqdlkkyfdscNGDIDPEIVK-SFMFQLL-------------KGLAFCHSH--NVLHRDLKPQNLLINKNGELKLA 141
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 221 DFGLAKDGPIGDKSHvSTRVMgTHGYAAPEYL--ATGHlTTKSDVYSFGVVLLELLSGRR 278
Cdd:cd07839 142 DFGLARAFGIPVRCY-SAEVV-TLWYRPPDVLfgAKLY-STSIDMWSAGCIFAELANAGR 198
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
74-277 3.86e-12

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: 66.63  E-value: 3.86e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQDGWQGHQE-WLAEVNYLgQFSHR--HLVKLIGYCLEDEHRLLV 150
Cdd:cd06618  23 IGSGTCGQVYK---------MRHKKTGHVMAVKQMRRSGNKEENKrILMDLDVV-LKSHDcpYIVKCYGYFITDSDVFIC 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 151 YEFMprGSLENHLFRRglYFQPLSWKLRLKVALGAAKGLAFL---HSsetrVIYRDFKTSNILLDSEYNAKLSDFGLAkd 227
Cdd:cd06618  93 MELM--STCLDKLLKR--IQGPIPEDILGKMTVSIVKALHYLkekHG----VIHRDVKPSNILLDESGNVKLCDFGIS-- 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15222437 228 GPIGDkSHVSTRVMGTHGYAAPEYL---ATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd06618 163 GRLVD-SKAKTRSAGCAAYMAPERIdppDNPKYDIRADVWSLGISLVELATGQ 214
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
74-277 4.25e-12

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: 65.75  E-value: 4.25e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWidEKSltasrpgTGLVIAVKKLNQDGwQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEF 153
Cdd:cd14006   1 LGRGRFGVVKRCI--EKA-------TGREFAAKFIPKRD-KKKEAVLREISILNQLQHPRIIQLHEAYESPTELVLILEL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 154 MPRGSLENHLFRRGLYFQPLSwKLRLKVALgaaKGLAFLHSSetRVIYRDFKTSNILLDS--EYNAKLSDFGLAKdgPIG 231
Cdd:cd14006  71 CSGGELLDRLAERGSLSEEEV-RTYMRQLL---EGLQYLHNH--HILHLDLKPENILLADrpSPQIKIIDFGLAR--KLN 142
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15222437 232 DKSHVSTRvMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd14006 143 PGEELKEI-FGTPEFVAPEIVNGEPVSLATDMWSIGVLTYVLLSGL 187
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
73-277 4.48e-12

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: 65.89  E-value: 4.48e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKGwideKSLTasrpgTGLVIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYE 152
Cdd:cd06624  15 VLGKGTFGVVYAA----RDLS-----TQVRIAIKEIPERDSREVQPLHEEIALHSRLSHKNIVQYLGSVSEDGFFKIFME 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMPRGSLeNHLFRRGlyFQPL-----SWKLRLKVALgaaKGLAFLHssETRVIYRDFKTSNILLDSeYNA--KLSDFGLA 225
Cdd:cd06624  86 QVPGGSL-SALLRSK--WGPLkdnenTIGYYTKQIL---EGLKYLH--DNKIVHRDIKGDNVLVNT-YSGvvKISDFGTS 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15222437 226 KDgpIGDKSHVSTRVMGTHGYAAPEYLATGH--LTTKSDVYSFGVVLLELLSGR 277
Cdd:cd06624 157 KR--LAGINPCTETFTGTLQYMAPEVIDKGQrgYGPPADIWSLGCTIIEMATGK 208
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
148-276 5.12e-12

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: 65.71  E-value: 5.12e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 148 LLVYEFMPRGSLENHLFRRglyfQPLSWKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAKD 227
Cdd:cd14182  86 FLVFDLMKKGELFDYLTEK----VTLSEKETRKIMRALLEVICALHKLN--IVHRDLKPENILLDDDMNIKLTDFGFSCQ 159
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15222437 228 GPIGDKSHvstRVMGTHGYAAPEYLATGH------LTTKSDVYSFGVVLLELLSG 276
Cdd:cd14182 160 LDPGEKLR---EVCGTPGYLAPEIIECSMddnhpgYGKEVDMWSTGVIMYTLLAG 211
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
74-276 6.21e-12

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: 65.81  E-value: 6.21e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVfkgwideksLTASRPGTGLVIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEF 153
Cdd:cd06657  28 IGEGSTGIV---------CIATVKSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEF 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 154 MPRGSLENHLFRRGLYFQPLSwklrlKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAKDgpIGDK 233
Cdd:cd06657  99 LEGGALTDIVTHTRMNEEQIA-----AVCLAVLKALSVLHAQG--VIHRDIKSDSILLTHDGRVKLSDFGFCAQ--VSKE 169
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 15222437 234 SHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd06657 170 VPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDG 212
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
67-273 6.44e-12

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: 65.37  E-value: 6.44e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGCVFKgwideksltASRPGTGLVIAVKKLN----QDGWQgHQEWLAEVNYLGQFSHRHLVKLIGYCL 142
Cdd:cd08224   1 NYEIEKKIGKGQFSVVYR---------ARCLLDGRLVALKKVQifemMDAKA-RQDCLKEIDLLQQLNHPNIIKYLASFI 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 143 EDEHRLLVYEFMPRGSLE---NHLFRRGLYFQ-PLSWKLRLKVALgaakGLAFLHSSetRVIYRDFKTSNILLDSEYNAK 218
Cdd:cd08224  71 ENNELNIVLELADAGDLSrliKHFKKQKRLIPeRTIWKYFVQLCS----ALEHMHSK--RIMHRDIKPANVFITANGVVK 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15222437 219 LSDFGLAKDgpIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLEL 273
Cdd:cd08224 145 LGDLGLGRF--FSSKTTAAHSLVGTPYYMSPERIREQGYDFKSDIWSLGCLLYEM 197
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
187-287 6.59e-12

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 66.44  E-value: 6.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  187 KGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAKdGPIGDKSHVStrVMGTHGYAAPEYLATGHLTTKSDVYSF 266
Cdd:PHA03209 168 EGLRYLHAQ--RIIHRDVKTENIFINDVDQVCIGDLGAAQ-FPVVAPAFLG--LAGTVETNAPEVLARDKYNSKADIWSA 242
                         90       100
                 ....*....|....*....|.
gi 15222437  267 GVVLLELLSGRRAVDKNRPSG 287
Cdd:PHA03209 243 GIVLFEMLAYPSTIFEDPPST 263
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
122-349 6.79e-12

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: 65.11  E-value: 6.79e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 122 EVNYLGQFSHRHLVKLigY-CLEDEHRL-LVYEFMPRGSLENHLFRRGLYFQPLS----WKLRLKVAlgaakglaFLHSS 195
Cdd:cd14071  49 EVQIMKMLNHPHIIKL--YqVMETKDMLyLVTEYASNGEIFDYLAQHGRMSEKEArkkfWQILSAVE--------YCHKR 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 196 etRVIYRDFKTSNILLDSEYNAKLSDFGLA---KDGpigdkSHVSTRVmGTHGYAAPE-YLATGHLTTKSDVYSFGVVLL 271
Cdd:cd14071 119 --HIVHRDLKAENLLLDANMNIKIADFGFSnffKPG-----ELLKTWC-GSPPYAAPEvFEGKEYEGPQLDIWSLGVVLY 190
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15222437 272 ELLSGRRAVDKNRPSGERNlvewakpylvnkrkifRVIDNRLQDQYSMEEACKvaTLSLRCLTTEIKLRPNMSEVVSH 349
Cdd:cd14071 191 VLVCGALPFDGSTLQTLRD----------------RVLSGRFRIPFFMSTDCE--HLIRRMLVLDPSKRLTIEQIKKH 250
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
71-276 6.91e-12

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


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 65.51  E-value: 6.91e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  71 DSVLGEGGFGCVFkgwidekslTASRPGTGLVIAVKKLNQDGWQGHQEWLAEVNYLGQFS-HRHLVKLIGYCLEDEHRLL 149
Cdd:cd14090   7 GELLGEGAYASVQ---------TCINLYTGKEYAVKIIEKHPGHSRSRVFREVETLHQCQgHPNILQLIEYFEDDERFYL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 150 VYEFMPRGSLENHLFRRGlYFQPLSWKLrlkVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNA---KLSDFGLAK 226
Cdd:cd14090  78 VFEKMRGGPLLSHIEKRV-HFTEQEASL---VVRDIASALDFLHDKG--IAHRDLKPENILCESMDKVspvKICDFDLGS 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15222437 227 DgpIGDKSHVSTRV--------MGTHGYAAPEYLAT--GHLTT---KSDVYSFGVVLLELLSG 276
Cdd:cd14090 152 G--IKLSSTSMTPVttpelltpVGSAEYMAPEVVDAfvGEALSydkRCDLWSLGVILYIMLCG 212
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
187-277 6.92e-12

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: 66.31  E-value: 6.92e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 187 KGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPIGDKSHVSTRVMgTHGYAAPEYLaTG--HLTTKSDVY 264
Cdd:cd07853 114 RGLKYLHSA--GILHRDIKPGNLLVNSNCVLKICDFGLARVEEPDESKHMTQEVV-TQYYRAPEIL-MGsrHYTSAVDIW 189
                        90
                ....*....|...
gi 15222437 265 SFGVVLLELLSGR 277
Cdd:cd07853 190 SVGCIFAELLGRR 202
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
74-349 8.54e-12

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 3, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. PAK3 belongs to group I. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAK3 is highly expressed in the brain. It is implicated in neuronal plasticity, synapse formation, dendritic spine morphogenesis, cell cycle progression, neuronal migration, and apoptosis. Inactivating mutations in the PAK3 gene cause X-linked non-syndromic mental retardation, the severity of which depends on the site of the mutation.


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 65.51  E-value: 8.54e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFkgwidekslTASRPGTGLVIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEF 153
Cdd:cd06656  27 IGQGASGTVY---------TAIDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 154 MPRGSLENHLFRRGLYFQPLSwklrlKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGL-AKDGPigD 232
Cdd:cd06656  98 LAGGSLTDVVTETCMDEGQIA-----AVCRECLQALDFLHSNQ--VIHRDIKSDNILLGMDGSVKLTDFGFcAQITP--E 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 233 KSHVSTRVmGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVDKNRPSGERNLVEW-AKPYLVNKRKIFRVIDN 311
Cdd:cd06656 169 QSKRSTMV-GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATnGTPELQNPERLSAVFRD 247
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 15222437 312 RLQdqysmeeackvatlslRCLTTEIKLRPNMSEVVSH 349
Cdd:cd06656 248 FLN----------------RCLEMDVDRRGSAKELLQH 269
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
62-282 9.69e-12

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 66.21  E-value: 9.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437   62 KSATRNFRPDSVLGEGGFGCVFKG-WIDeksltasrpgTGLVIAVKKLNQDGWQGHQEWLAEVNylgqFSHRHLVKLIGY 140
Cdd:PTZ00036  62 RSPNKSYKLGNIIGNGSFGVVYEAiCID----------TSEKVAIKKVLQDPQYKNRELLIMKN----LNHINIIFLKDY 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  141 ----CLEDEHRLL----VYEFMPRG--------SLENH---LFRRGLYfqplSWKLrlkvalgaAKGLAFLHSSetRVIY 201
Cdd:PTZ00036 128 yyteCFKKNEKNIflnvVMEFIPQTvhkymkhyARNNHalpLFLVKLY----SYQL--------CRALAYIHSK--FICH 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  202 RDFKTSNILLD-SEYNAKLSDFGLAKDGPIGDK--SHVSTRVmgthgYAAPE-YLATGHLTTKSDVYSFGVVLLE----- 272
Cdd:PTZ00036 194 RDLKPQNLLIDpNTHTLKLCDFGSAKNLLAGQRsvSYICSRF-----YRAPElMLGATNYTTHIDLWSLGCIIAEmilgy 268
                        250
                 ....*....|.
gi 15222437  273 -LLSGRRAVDK 282
Cdd:PTZ00036 269 pIFSGQSSVDQ 279
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
66-273 1.01e-11

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: 64.64  E-value: 1.01e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  66 RNFRPDSVLGEGGFGCVFKGWIDEKSLTASrpgtGLVIAVKKLNQDGWQGHQEwlaEVNYLGQFSHRHLVKLIG------ 139
Cdd:cd14033   1 RFLKFNIEIGRGSFKTVYRGLDTETTVEVA----WCELQTRKLSKGERQRFSE---EVEMLKGLQHPNIVRFYDswkstv 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 140 ---YCLedehrLLVYEFMPRGSLENHLFRrglyFQPLSWKLRLKVALGAAKGLAFLHSSETRVIYRDFKTSNILLDSEY- 215
Cdd:cd14033  74 rghKCI-----ILVTELMTSGTLKTYLKR----FREMKLKLLQRWSRQILKGLHFLHSRCPPILHRDLKCDNIFITGPTg 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15222437 216 NAKLSDFGLAKdgpiGDKSHVSTRVMGTHGYAAPEYLATGHlTTKSDVYSFGVVLLEL 273
Cdd:cd14033 145 SVKIGDLGLAT----LKRASFAKSVIGTPEFMAPEMYEEKY-DEAVDVYAFGMCILEM 197
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
74-277 1.01e-11

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


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 65.40  E-value: 1.01e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGwidEKSLTASrpgtglVIAVKKLNQDGWQGHQ-EWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYE 152
Cdd:cd07872  14 LGEGTYATVFKG---RSKLTEN------LVALKEIRLEHEEGAPcTAIREVSLLKDLKHANIVTLHDIVHTDKSLTLVFE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMPRgSLENHLFRRGLYFQPLSWKLRLKVALgaaKGLAFLHssETRVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPIGD 232
Cdd:cd07872  85 YLDK-DLKQYMDDCGNIMSMHNVKIFLYQIL---RGLAYCH--RRKVLHRDLKPQNLLINERGELKLADFGLARAKSVPT 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15222437 233 KSHVSTRVmgTHGYAAPE-YLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd07872 159 KTYSNEVV--TLWYRPPDvLLGSSEYSTQIDMWGVGCIFFEMASGR 202
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
185-349 1.29e-11

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: 64.60  E-value: 1.29e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 185 AAKGLAFLHSseTRVIYRDFKTSNILLD-----SEYNAKLSDFGLAKDGPIGDKS-HVSTRVMGTHGYAAPEYLATGH-- 256
Cdd:cd13982 108 IASGLAHLHS--LNIVHRDLKPQNILIStpnahGNVRAMISDFGLCKKLDVGRSSfSRRSGVAGTSGWIAPEMLSGSTkr 185
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 257 -LTTKSDVYSFGVVLLELLSGRRavdknRPSGERnlvewakpyLVNKRKIFRVIDNRLQDQYSMEEACKVATLSLRCLTT 335
Cdd:cd13982 186 rQTRAVDIFSLGCVFYYVLSGGS-----HPFGDK---------LEREANILKGKYSLDKLLSLGEHGPEAQDLIERMIDF 251
                       170
                ....*....|....
gi 15222437 336 EIKLRPNMSEVVSH 349
Cdd:cd13982 252 DPEKRPSAEEVLNH 265
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
74-273 1.29e-11

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: 64.53  E-value: 1.29e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWIDEKSLTASrpgtglvIAVKKLNQD-GWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYE 152
Cdd:cd05042   3 IGNGWFGKVLLGEIYSGTSVAQ-------VVVKELKASaNPKEQDTFLKEGQPYRILQHPNILQCLGQCVEAIPYLLVME 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMPRGSLENHLFRRGLYFQPLSWKLRL-KVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPIG 231
Cdd:cd05042  76 FCDLGDLKAYLRSEREHERGDSDTRTLqRMACEVAAGLAHLHKLN--FVHSDLALRNCLLTSDLTVKIGDYGLAHSRYKE 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15222437 232 DKSHVSTRVMGTHGYAAPEYLATGH-------LTTKSDVYSFGVVLLEL 273
Cdd:cd05042 154 DYIETDDKLWFPLRWTAPELVTEFHdrllvvdQTKYSNIWSLGVTLWEL 202
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
68-276 1.34e-11

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: 65.07  E-value: 1.34e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  68 FRPDSVLGEGGFGCVfkgwideksLTASRPGTGLVIAVKKLNQDGWQGHQEWLA-EVNYLGQFSHRHLVKLIGYCLEDEH 146
Cdd:cd14168  12 FEFKEVLGTGAFSEV---------VLAEERATGKLFAVKCIPKKALKGKESSIEnEIAVLRKIKHENIVALEDIYESPNH 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 147 RLLVYEFMPRGSLENHLFRRGLYFQPLSWKLRLKVAlgaaKGLAFLHSseTRVIYRDFKTSNILL---DSEYNAKLSDFG 223
Cdd:cd14168  83 LYLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVL----DAVYYLHR--MGIVHRDLKPENLLYfsqDEESKIMISDFG 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15222437 224 LAKDGPIGDkshVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14168 157 LSKMEGKGD---VMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCG 206
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
66-349 1.48e-11

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: 64.67  E-value: 1.48e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  66 RNFRPDSVLGEGGFGCVFKGWiDEKSltasrpgTGLVIAVKKLN-QDGWQGHQ----EWLAEVNYLGQFSHRHLVKLIGY 140
Cdd:cd07862   1 QQYECVAEIGEGAYGKVFKAR-DLKN-------GGRFVALKRVRvQTGEEGMPlstiREVAVLRHLETFEHPNVVRLFDV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 141 CL----EDEHRL-LVYEFMPRgSLENHLFRRGLYFQPLSWKLRLKVALgaAKGLAFLHSSetRVIYRDFKTSNILLDSEY 215
Cdd:cd07862  73 CTvsrtDRETKLtLVFEHVDQ-DLTTYLDKVPEPGVPTETIKDMMFQL--LRGLDFLHSH--RVVHRDLKPQNILVTSSG 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 216 NAKLSDFGLAKdgpIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLE------LLSGRRAVDK------- 282
Cdd:cd07862 148 QIKLADFGLAR---IYSFQMALTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEmfrrkpLFRGSSDVDQlgkildv 224
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15222437 283 -NRPSGERNLVEWAKPYLVNKRKIFRVIDNRLQDqysMEEACKvaTLSLRCLTTEIKLRPNMSEVVSH 349
Cdd:cd07862 225 iGLPGEEDWPRDVALPRQAFHSKSAQPIEKFVTD---IDELGK--DLLLKCLTFNPAKRISAYSALSH 287
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
74-279 1.77e-11

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: 64.06  E-value: 1.77e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGcvfkgwideKSLTASRPGTGLVIAVKKLNQDGWQG--HQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVY 151
Cdd:cd08218   8 IGEGSFG---------KALLVKSKEDGKQYVIKEINISKMSPkeREESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 152 EFMPRGSLENHL-FRRGLYF---QPLSWKLRLKVALGaakglaflHSSETRVIYRDFKTSNILLDSEYNAKLSDFGLAKd 227
Cdd:cd08218  79 DYCDGGDLYKRInAQRGVLFpedQILDWFVQLCLALK--------HVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIAR- 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15222437 228 gPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRA 279
Cdd:cd08218 150 -VLNSTVELARTCIGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHA 200
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
67-276 1.79e-11

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: 64.25  E-value: 1.79e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGCVFkgwideksLTASRPG--TGLVIAVKKLNQ----DGWQGHQEWLAEVNYLGQFSHRHLVKLIGY 140
Cdd:cd05613   1 NFELLKVLGTGAYGKVF--------LVRKVSGhdAGKLYAMKVLKKativQKAKTAEHTRTERQVLEHIRQSPFLVTLHY 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 141 CLEDEHRL-LVYEFMPRGSLENHLFRRGLYFQPlswklRLKVALGAAKgLAFLHSSETRVIYRDFKTSNILLDSEYNAKL 219
Cdd:cd05613  73 AFQTDTKLhLILDYINGGELFTHLSQRERFTEN-----EVQIYIGEIV-LALEHLHKLGIIYRDIKLENILLDSSGHVVL 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 220 SDFGLAKDGpIGDKSHVSTRVMGTHGYAAPEYLA---TGHlTTKSDVYSFGVVLLELLSG 276
Cdd:cd05613 147 TDFGLSKEF-LLDENERAYSFCGTIEYMAPEIVRggdSGH-DKAVDWWSLGVLMYELLTG 204
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
33-277 2.13e-11

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 64.84  E-value: 2.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437   33 SSVSVRPSPRTEGEILQSPNLKSFSfaELKSATRnfrpdsvLGEGGFGCVFKgwidekslTASRPgTGLVIAVKKLnqdg 112
Cdd:PLN00034  50 PSSSSSSSSSSSASGSAPSAAKSLS--ELERVNR-------IGSGAGGTVYK--------VIHRP-TGRLYALKVI---- 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  113 WQGHQEWLA-----EVNYLGQFSHRHLVKLIG-YCLEDEHRLLVyEFMPRGSLENH-----LFRRGLYFQPLSwklrlkv 181
Cdd:PLN00034 108 YGNHEDTVRrqicrEIEILRDVNHPNVVKCHDmFDHNGEIQVLL-EFMDGGSLEGThiadeQFLADVARQILS------- 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  182 algaakGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLakdgpigdkSHVSTRVM-------GTHGYAAPEYLAT 254
Cdd:PLN00034 180 ------GIAYLHRR--HIVHRDIKPSNLLINSAKNVKIADFGV---------SRILAQTMdpcnssvGTIAYMSPERINT 242
                        250       260       270
                 ....*....|....*....|....*....|.
gi 15222437  255 --------GHlttKSDVYSFGVVLLELLSGR 277
Cdd:PLN00034 243 dlnhgaydGY---AGDIWSLGVSILEFYLGR 270
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
104-275 2.28e-11

Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer T-cell-originated protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TOPK, also called PDZ-binding kinase (PBK), is activated at the early stage of mitosis and plays a critical role in cytokinesis. It partly functions as a mitogen-activated protein kinase (MAPK) kinase and is capable of phosphorylating p38, JNK1, and ERK2. TOPK also plays a role in DNA damage sensing and repair through its phosphorylation of histone H2AX. It contributes to cancer development and progression by downregulating the function of tumor suppressor p53 and reducing cell-cycle regulatory proteins. TOPK is found highly expressed in breast and skin cancer cells. The TOPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 63.96  E-value: 2.28e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 104 AVKKLN----QDGWQGHQEWLA-EVNYLGQFSHRHLVKLIGYC-LEDEHRLLVYEFmprgsLENHLF-----RRGLYFQP 172
Cdd:cd14001  32 AVKKINskcdKGQRSLYQERLKeEAKILKSLNHPNIVGFRAFTkSEDGSLCLAMEY-----GGKSLNdlieeRYEAGLGP 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 173 LSWKLRLKVALGAAKGLAFLHSsETRVIYRDFKTSNILLDSEYNA-KLSDFG--LAKDGPIGDKSHVSTRVMGTHGYAAP 249
Cdd:cd14001 107 FPAATILKVALSIARALEYLHN-EKKILHGDIKSGNVLIKGDFESvKLCDFGvsLPLTENLEVDSDPKAQYVGTEPWKAK 185
                       170       180
                ....*....|....*....|....*..
gi 15222437 250 EYLATGHL-TTKSDVYSFGVVLLELLS 275
Cdd:cd14001 186 EALEEGGViTDKADIFAYGLVLWEMMT 212
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
74-277 2.33e-11

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: 64.25  E-value: 2.33e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGwidEKSLTASrpgtglVIAVKKLNQDGWQGHQ-EWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYE 152
Cdd:cd07873  10 LGEGTYATVYKG---RSKLTDN------LVALKEIRLEHEEGAPcTAIREVSLLKDLKHANIVTLHDIIHTEKSLTLVFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMPRgSLENHLFRRGLYFQPLSWKLRLKVALgaaKGLAFLHssETRVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPIGD 232
Cdd:cd07873  81 YLDK-DLKQYLDDCGNSINMHNVKLFLFQLL---RGLAYCH--RRKVLHRDLKPQNLLINERGELKLADFGLARAKSIPT 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15222437 233 KSHVSTRVmgTHGYAAPE-YLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd07873 155 KTYSNEVV--TLWYRPPDiLLGSTDYSTQIDMWGVGCIFYEMSTGR 198
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
187-276 2.35e-11

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: 63.91  E-value: 2.35e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 187 KGLAFLHssETRVIYRDFKTSNILLDSEYNA---KLSDFGLAKdgPIGDKSHVStRVMGTHGYAAPEYLATGHLTTKSDV 263
Cdd:cd14106 119 EGVQYLH--ERNIVHLDLKPQNILLTSEFPLgdiKLCDFGISR--VIGEGEEIR-EILGTPDYVAPEILSYEPISLATDM 193
                        90
                ....*....|...
gi 15222437 264 YSFGVVLLELLSG 276
Cdd:cd14106 194 WSIGVLTYVLLTG 206
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
74-277 2.58e-11

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: 63.88  E-value: 2.58e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGwidEKSLTASrpgtglVIAVKKLNQDGWQGHQ-EWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYE 152
Cdd:cd07871  13 LGEGTYATVFKG---RSKLTEN------LVALKEIRLEHEEGAPcTAIREVSLLKNLKHANIVTLHDIIHTERCLTLVFE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMpRGSLENHLFRRGLYFQPLSWKLRLKVALgaaKGLAFLHssETRVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPIGD 232
Cdd:cd07871  84 YL-DSDLKQYLDNCGNLMSMHNVKIFMFQLL---RGLSYCH--KRKILHRDLKPQNLLINEKGELKLADFGLARAKSVPT 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15222437 233 KSHVSTRVmgTHGYAAPE-YLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd07871 158 KTYSNEVV--TLWYRPPDvLLGSTEYSTPIDMWGVGCILYEMATGR 201
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
149-296 2.62e-11

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: 63.65  E-value: 2.62e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 LVYEFMPRGSLENHLFRRGlyfqPLSWKLRLKVALGAAKGLAFLHssETRVIYRDFKTSNILLDSEYNAKLSDFGLAKDG 228
Cdd:cd05611  74 LVMEYLNGGDCASLIKTLG----GLPEDWAKQYIAEVVLGVEDLH--QRGIIHRDIKPENLLIDQTGHLKLTDFGLSRNG 147
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15222437 229 PIGDKshvSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVDKNRPSG-----ERNLVEWAK 296
Cdd:cd05611 148 LEKRH---NKKFVGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPDAvfdniLSRRINWPE 217
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
75-275 2.72e-11

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: 64.23  E-value: 2.72e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  75 GEGGFGCVFKGWIDEksltasrPGTGLVIAVKKLNQDGWQG---HQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRL--L 149
Cdd:cd07842   9 GRGTYGRVYKAKRKN-------GKDGKEYAIKKFKGDKEQYtgiSQSACREIALLRELKHENVVSLVEVFLEHADKSvyL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 150 VYEFMPRGSLE---NHLFRRGLYFQPLSWKLRLKVALgaaKGLAFLHSSetRVIYRDFKTSNILLDSEYNA----KLSDF 222
Cdd:cd07842  82 LFDYAEHDLWQiikFHRQAKRVSIPPSMVKSLLWQIL---NGIHYLHSN--WVLHRDLKPANILVMGEGPErgvvKIGDL 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15222437 223 GLAK--DGPIGDKSHVStRVMGTHGYAAPE-YLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:cd07842 157 GLARlfNAPLKPLADLD-PVVVTIWYRAPElLLGARHYTKAIDIWAIGCIFAELLT 211
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
59-281 2.89e-11

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 64.89  E-value: 2.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437   59 AELKSATRNFRPDSVLGEGGFGCVfkgwideksLTASRPGTGLVIAVKKLNQDGW--QGHQEWLAEVNYLGQFSHRHLVK 136
Cdd:PTZ00283  25 ATAKEQAKKYWISRVLGSGATGTV---------LCAKRVSDGEPFAVKVVDMEGMseADKNRAQAEVCCLLNCDFFSIVK 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  137 ligyCLED---------EHRL---LVYEFMPRGSLE---------NHLFRR---GLYF-QPLswklrlkvalgaakgLAF 191
Cdd:PTZ00283  96 ----CHEDfakkdprnpENVLmiaLVLDYANAGDLRqeiksraktNRTFREheaGLLFiQVL---------------LAV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  192 LHSSETRVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLL 271
Cdd:PTZ00283 157 HHVHSKHMIHRDIKSANILLCSNGLVKLGDFGFSKMYAATVSDDVGRTFCGTPYYVAPEIWRRKPYSKKADMFSLGVLLY 236
                        250
                 ....*....|
gi 15222437  272 ELLSGRRAVD 281
Cdd:PTZ00283 237 ELLTLKRPFD 246
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
104-284 2.94e-11

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: 63.32  E-value: 2.94e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 104 AVKKLNQDgWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEFMPRGSLENHLFRRGLYFQPLSWKLrLKVAL 183
Cdd:cd14087  30 AIKMIETK-CRGREVCESELNVLRRVRHTNIIQLIEVFETKERVYMVMELATGGELFDRIIAKGSFTERDATRV-LQMVL 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 184 gaaKGLAFLHSseTRVIYRDFKTSNILL-DSEYNAKL--SDFGLAKDGPIGDKSHVSTrVMGTHGYAAPEYLATGHLTTK 260
Cdd:cd14087 108 ---DGVKYLHG--LGITHRDLKPENLLYyHPGPDSKImiTDFGLASTRKKGPNCLMKT-TCGTPEYIAPEILLRKPYTQS 181
                       170       180
                ....*....|....*....|....*
gi 15222437 261 SDVYSFGVVLLELLSGRRAV-DKNR 284
Cdd:cd14087 182 VDMWAVGVIAYILLSGTMPFdDDNR 206
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
73-276 3.06e-11

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: 63.11  E-value: 3.06e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFG----CVFKGWIDEKsltasrpgtglviAVKKLNQDGWQGHQEWLA-EVNYLGQFSHRHLVKLIGYCLEDEHR 147
Cdd:cd14095   7 VIGDGNFAvvkeCRDKATDKEY-------------ALKIIDKAKCKGKEHMIEnEVAILRRVKHPNIVQLIEEYDTDTEL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 148 LLVYEFMPRGSLENHLFRRGLYFQPLSwkLRLKVALGAAkgLAFLHSseTRVIYRDFKTSNILL----DSEYNAKLSDFG 223
Cdd:cd14095  74 YLVMELVKGGDLFDAITSSTKFTERDA--SRMVTDLAQA--LKYLHS--LSIVHRDIKPENLLVveheDGSKSLKLADFG 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15222437 224 LAK--DGPIgdkshvSTrVMGTHGYAAPEYLA-TGHlTTKSDVYSFGVVLLELLSG 276
Cdd:cd14095 148 LATevKEPL------FT-VCGTPTYVAPEILAeTGY-GLKVDIWAAGVITYILLCG 195
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
74-350 3.15e-11

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: 64.23  E-value: 3.15e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVfkgwIDEKSLTASRPGTGLVIAVKKLNQDGwqGHQEWLAEVNYLGQFSH--RHL--VKLIGYCLEDEHRLL 149
Cdd:cd05103  15 LGRGAFGQV----IEADAFGIDKTATCRTVAVKMLKEGA--THSEHRALMSELKILIHigHHLnvVNLLGACTKPGGPLM 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 150 V-YEFMPRGSLENHL----------------FRRG--------------------------------------------- 167
Cdd:cd05103  89 ViVEFCKFGNLSAYLrskrsefvpyktkgarFRQGkdyvgdisvdlkrrldsitssqssassgfveekslsdveeeeagq 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 168 --LYFQPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAKDgPIGDKSHV---STRVmg 242
Cdd:cd05103 169 edLYKDFLTLEDLICYSFQVAKGMEFLASR--KCIHRDLAARNILLSENNVVKICDFGLARD-IYKDPDYVrkgDARL-- 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 243 THGYAAPEYLATGHLTTKSDVYSFGVVLLELLSgrravdknrpsgernlvEWAKPYlvNKRKIFRVIDNRLQDQYSME-- 320
Cdd:cd05103 244 PLKWMAPETIFDRVYTIQSDVWSFGVLLWEIFS-----------------LGASPY--PGVKIDEEFCRRLKEGTRMRap 304
                       330       340       350
                ....*....|....*....|....*....|..
gi 15222437 321 --EACKVATLSLRCLTTEIKLRPNMSEVVSHL 350
Cdd:cd05103 305 dyTTPEMYQTMLDCWHGEPSQRPTFSELVEHL 336
PHA02988 PHA02988
hypothetical protein; Provisional
122-351 3.16e-11

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 63.61  E-value: 3.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  122 EVNYLGQFSHRHLVKLIGYCLEdehrllVYEFMPRGSLENHLFRRGL------YFQPLSWKLRLKVALGAAKGLAFLHSS 195
Cdd:PHA02988  68 EIKNLRRIDSNNILKIYGFIID------IVDDLPRLSLILEYCTRGYlrevldKEKDLSFKTKLDMAIDCCKGLYNLYKY 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  196 eTRVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPIGDKSHVSTRVmgthgYAAPEYLAT--GHLTTKSDVYSFGVVLLEL 273
Cdd:PHA02988 142 -TNKPYKNLTSVSFLVTENYKLKIICHGLEKILSSPPFKNVNFMV-----YFSYKMLNDifSEYTIKDDIYSLGVVLWEI 215
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15222437  274 LSGRRAVDKNRPSGERNLvewakpyLVNKRKIFRV-IDNRLQDQYSMEeackvatlslRCLTTEIKLRPNMSEVVSHLE 351
Cdd:PHA02988 216 FTGKIPFENLTTKEIYDL-------IINKNNSLKLpLDCPLEIKCIVE----------ACTSHDSIKRPNIKEILYNLS 277
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
73-274 4.07e-11

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: 63.07  E-value: 4.07e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFkgwidekslTASRPGTGLVIAVKKL---NQDGWQGHQewlAEVNYLGQFS-HRHLVKLIGY---CLEDE 145
Cdd:cd14037  10 YLAEGGFAHVY---------LVKTSNGGNRAALKRVyvnDEHDLNVCK---REIEIMKRLSgHKNIVGYIDSsanRSGNG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 146 --HRLLVYEFMPRGSLENHLFRRglyfqpLSWKLR----LKVALGAAKGLAFLHSSETRVIYRDFKTSNILLDSEYNAKL 219
Cdd:cd14037  78 vyEVLLLMEYCKGGGVIDLMNQR------LQTGLTeseiLKIFCDVCEAVAAMHYLKPPLIHRDLKVENVLISDSGNYKL 151
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15222437 220 SDFGLAkdgpigdkSHVSTRVMGTHG---------------YAAPE----YLATGhLTTKSDVYSFGVVLLELL 274
Cdd:cd14037 152 CDFGSA--------TTKILPPQTKQGvtyveedikkyttlqYRAPEmidlYRGKP-ITEKSDIWALGCLLYKLC 216
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
74-276 4.48e-11

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: 62.99  E-value: 4.48e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVfkgwideksLTASRPGTGLVIAVKKLNQDGWQGHQEWLA-EVNYLGQFSHRHLVKLIGYCLEDEHRLLVYE 152
Cdd:cd14169  11 LGEGAFSEV---------VLAQERGSQRLVALKCIPKKALRGKEAMVEnEIAVLRRINHENIVSLEDIYESPTHLYLAME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMPRGSLENHLFRRGLYFQPLSWKLRLKVaLGAAKglaFLHssETRVIYRDFKTSNILLDSEY-NAKL--SDFGLAKdgp 229
Cdd:cd14169  82 LVTGGELFDRIIERGSYTEKDASQLIGQV-LQAVK---YLH--QLGIVHRDLKPENLLYATPFeDSKImiSDFGLSK--- 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15222437 230 IGDKSHVSTrVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14169 153 IEAQGMLST-ACGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCG 198
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
67-273 4.49e-11

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: 63.12  E-value: 4.49e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGCVFKG--WIDEKSltasrpgtglvIAVKKLN----QDGwQGHQEWLAEVNYLGQFSHRHLVKLIGY 140
Cdd:cd08228   3 NFQIEKKIGRGQFSEVYRAtcLLDRKP-----------VALKKVQifemMDA-KARQDCVKEIDLLKQLNHPNVIKYLDS 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 141 CLEDEHRLLVYEFMPRGSLENHL--FRRGLYFQPLSWKLRLKVALGAAkgLAFLHSSetRVIYRDFKTSNILLDSEYNAK 218
Cdd:cd08228  71 FIEDNELNIVLELADAGDLSQMIkyFKKQKRLIPERTVWKYFVQLCSA--VEHMHSR--RVMHRDIKPANVFITATGVVK 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15222437 219 LSDFGLAKDgpIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLEL 273
Cdd:cd08228 147 LGDLGLGRF--FSSKTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEM 199
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
74-278 4.52e-11

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: 63.40  E-value: 4.52e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFkgwideksLTASRPgTGLVIAVKKLNQD-GWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHR----- 147
Cdd:cd14039   1 LGTGGFGNVC--------LYQNQE-TGEKIAIKSCRLElSVKNKDRWCHEIQIMKKLNHPNVVKACDVPEEMNFLvndvp 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 148 LLVYEFMPRGSLenhlfrRGLYFQPL-------SWKLRLKVALGAakGLAFLHssETRVIYRDFKTSNILLDSEYNA--- 217
Cdd:cd14039  72 LLAMEYCSGGDL------RKLLNKPEnccglkeSQVLSLLSDIGS--GIQYLH--ENKIIHRDLKPENIVLQEINGKivh 141
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15222437 218 KLSDFGLAKDGpigDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRR 278
Cdd:cd14039 142 KIIDLGYAKDL---DQGSLCTSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFR 199
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
70-347 5.11e-11

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: 62.45  E-value: 5.11e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  70 PDSVLGEGGFG-CVFKGWIDEKSLTASRPgTGLVIAVKKLNQDGwqghqewLAEVNYLGQFSHRHLVKLIGYCLEDEHRL 148
Cdd:cd08221   4 PVRVLGRGAFGeAVLYRKTEDNSLVVWKE-VNLSRLSEKERRDA-------LNEIDILSLLNHDNIITYYNHFLDGESLF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 LVYEFMPRGSL-------ENHLFRRglyfQPLSWKLRLKVAlgaakglAFLHSSETRVIYRDFKTSNILLDSEYNAKLSD 221
Cdd:cd08221  76 IEMEYCNGGNLhdkiaqqKNQLFPE----EVVLWYLYQIVS-------AVSHIHKAGILHRDIKTLNIFLTKADLVKLGD 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 222 FGLAKDgpIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVDKNRPsgeRNLVEwakpylvn 301
Cdd:cd08221 145 FGISKV--LDSESSMAESIVGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFDATNP---LRLAV-------- 211
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 15222437 302 krKIFRVIDNRLQDQYSMEeackVATLSLRCLTTEIKLRPNMSEVV 347
Cdd:cd08221 212 --KIVQGEYEDIDEQYSEE----IIQLVHDCLHQDPEDRPTAEELL 251
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
72-277 5.24e-11

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: 63.49  E-value: 5.24e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  72 SVLGEGGFGCVfkgwidekSLTASRpGTGLVIAVKKLNQ-DGWQGHQ--EWLAEVNYLGQFSHRHLVKLIgYCLEDEHRL 148
Cdd:cd05598   7 KTIGVGAFGEV--------SLVRKK-DTNALYAMKTLRKkDVLKRNQvaHVKAERDILAEADNEWVVKLY-YSFQDKENL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 -LVYEFMPRGSLENHLFRRGLYFQPLS--WKLRLKVALGAAKGLAFLHssetrviyRDFKTSNILLDSEYNAKLSDFGLA 225
Cdd:cd05598  77 yFVMDYIPGGDLMSLLIKKGIFEEDLArfYIAELVCAIESVHKMGFIH--------RDIKPDNILIDRDGHIKLTDFGLC 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15222437 226 KdgpiG------DKSHVSTRVMGTHGYAAPEYLA-TGHlTTKSDVYSFGVVLLELLSGR 277
Cdd:cd05598 149 T----GfrwthdSKYYLAHSLVGTPNYIAPEVLLrTGY-TQLCDWWSVGVILYEMLVGQ 202
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
70-276 5.56e-11

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: 62.67  E-value: 5.56e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  70 PDSVLGEGGFGCVFKgwIDEKSltasrpgTGLVIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGyCLEDEHRL- 148
Cdd:cd14192   8 PHEVLGGGRFGQVHK--CTELS-------TGLTLAAKIIKVKGAKEREEVKNEINIMNQLNHVNLIQLYD-AFESKTNLt 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 LVYEFMPRGSLENHLFRRGLYFQPLSWKLRLKvalGAAKGLAFLHssETRVIYRDFKTSNILL--DSEYNAKLSDFGLAK 226
Cdd:cd14192  78 LIMEYVDGGELFDRITDESYQLTELDAILFTR---QICEGVHYLH--QHYILHLDLKPENILCvnSTGNQIKIIDFGLAR 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15222437 227 DGPIGDKSHVStrvMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14192 153 RYKPREKLKVN---FGTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSG 199
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
72-292 6.24e-11

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: 62.90  E-value: 6.24e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  72 SVLGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQDGWQGHQEWLA--EVNYLGQFSHRHLVKLIGYCLEDEHRL- 148
Cdd:cd07864  13 GIIGEGTYGQVYK---------AKDKDTGELVALKKVRLDNEKEGFPITAirEIKILRQLNHRSVVNLKEIVTDKQDALd 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 ---------LVYEFMPR---GSLENHLfrrgLYFQPLSWKLRLKVALgaaKGLAFLHssETRVIYRDFKTSNILLDSEYN 216
Cdd:cd07864  84 fkkdkgafyLVFEYMDHdlmGLLESGL----VHFSEDHIKSFMKQLL---EGLNYCH--KKNFLHRDIKCSNILLNNKGQ 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15222437 217 AKLSDFGLAKDGPIGDKSHVSTRVMgTHGYAAPEYLATGHLTTKS-DVYSFGVVLLELLSGRRAVDKNRPSGERNLV 292
Cdd:cd07864 155 IKLADFGLARLYNSEESRPYTNKVI-TLWYRPPELLLGEERYGPAiDVWSCGCILGELFTKKPIFQANQELAQLELI 230
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
122-278 6.91e-11

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 63.32  E-value: 6.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  122 EVNYLGQFSHRHLVKLIgycleDEHRL--LVYEFMP--RGSLENHLFRRGlyfqPLSWKLRLKVALGAAKGLAFLHssET 197
Cdd:PHA03207 136 EIDILKTISHRAIINLI-----HAYRWksTVCMVMPkyKCDLFTYVDRSG----PLPLEQAITIQRRLLEALAYLH--GR 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  198 RVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:PHA03207 205 GIIHRDVKTENIFLDEPENAVLGDFGAACKLDAHPDTPQCYGWSGTLETNSPELLALDPYCAKTDIWSAGLVLFEMSVKN 284

                 .
gi 15222437  278 R 278
Cdd:PHA03207 285 V 285
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
73-276 7.30e-11

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: 62.97  E-value: 7.30e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGcvfkgwideKSLTASRPGTGLVIAVKKLNQDGWQGHQE---WLAEVNYLGQFSHRHLVKLIGYCLEDEHRLL 149
Cdd:cd05585   1 VIGKGSFG---------KVMQVRKKDTSRIYALKTIRKAHIVSRSEvthTLAERTVLAQVDCPFIVPLKFSFQSPEKLYL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 150 VYEFMPRGSLENHLFRRGLYFQPLS--WKLRLKVALGAakglafLHssETRVIYRDFKTSNILLDSEYNAKLSDFGLAKD 227
Cdd:cd05585  72 VLAFINGGELFHHLQREGRFDLSRArfYTAELLCALEC------LH--KFNVIYRDLKPENILLDYTGHIALCDFGLCKL 143
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15222437 228 GPigDKSHVSTRVMGTHGYAAPEYLaTGHLTTKS-DVYSFGVVLLELLSG 276
Cdd:cd05585 144 NM--KDDDKTNTFCGTPEYLAPELL-LGHGYTKAvDWWTLGVLLYEMLTG 190
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
74-281 8.26e-11

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: 61.89  E-value: 8.26e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKgwideksltaSRPGTGLVIAVKKLNQDGWQGHQEWL---AEVNYLGQFSHRHLVKlIGYCLEDEHRL-L 149
Cdd:cd14161  11 LGKGTYGRVKK----------ARDSSGRLVAIKSIRKDRIKDEQDLLhirREIEIMSSLNHPHIIS-VYEVFENSSKIvI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 150 VYEFMPRGSLENHLFRRglyfQPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAKdgp 229
Cdd:cd14161  80 VMEYASRGDLYDYISER----QRLSELEARHFFRQIVSAVHYCHAN--GIVHRDLKLENILLDANGNIKIADFGLSN--- 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15222437 230 IGDKSHVSTRVMGTHGYAAPEYL-ATGHLTTKSDVYSFGVVLLELLSGRRAVD 281
Cdd:cd14161 151 LYNQDKFLQTYCGSPLYASPEIVnGRPYIGPEVDSWSLGVLLYILVHGTMPFD 203
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
73-276 9.40e-11

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: 61.89  E-value: 9.40e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVfkgwidekslTASRP-GTGLVIAVKKLNQDGWQGHQEWL-AEVNYLGQFSHRHLVKLIGYCLEDEHRLLV 150
Cdd:cd14185   7 TIGDGNFAVV----------KECRHwNENQEYAMKIIDKSKLKGKEDMIeSEILIIKSLSHPNIVKLFEVYETEKEIYLI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 151 YEFMPRGSLENHLFRRGLYFQPLSWKLRLKVAlgaaKGLAFLHSSEtrVIYRDFKTSNILL----DSEYNAKLSDFGLAK 226
Cdd:cd14185  77 LEYVRGGDLFDAIIESVKFTEHDAALMIIDLC----EALVYIHSKH--IVHRDLKPENLLVqhnpDKSTTLKLADFGLAK 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15222437 227 --DGPIgdkshvsTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14185 151 yvTGPI-------FTVCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCG 195
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
73-353 9.89e-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: 62.43  E-value: 9.89e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKGwideksltaSRPGTGLVIAVKKLNQDGWQgHQEWLAEVNYLGQFSH-RHLVKLIGYCLE------DE 145
Cdd:cd06637  13 LVGNGTYGQVYKG---------RHVKTGQLAAIKVMDVTGDE-EEEIKQEINMLKKYSHhRNIATYYGAFIKknppgmDD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 146 HRLLVYEFMPRGSLENHLfrRGLYFQPLSWKLRLKVALGAAKGLAFLHssETRVIYRDFKTSNILLDSEYNAKLSDFGLA 225
Cdd:cd06637  83 QLWLVMEFCGAGSVTDLI--KNTKGNTLKEEWIAYICREILRGLSHLH--QHKVIHRDIKGQNVLLTENAEVKLVDFGVS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 226 K--DGPIGDKShvstRVMGTHGYAAPEYLATGH-----LTTKSDVYSFGVVLLELLSGRRAVDKNRPSgeRNLvewakpY 298
Cdd:cd06637 159 AqlDRTVGRRN----TFIGTPYWMAPEVIACDEnpdatYDFKSDLWSLGITAIEMAEGAPPLCDMHPM--RAL------F 226
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15222437 299 LVNKRKIFRVIDNRLQDQY-SMEEACKVATLSLRCLTTE------IKLRPNMSEVVSHL-EHI 353
Cdd:cd06637 227 LIPRNPAPRLKSKKWSKKFqSFIESCLVKNHSQRPSTEQlmkhpfIRDQPNERQVRIQLkDHI 289
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
39-273 1.21e-10

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: 61.97  E-value: 1.21e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  39 PSPRTEGEILQSPNLKSFSFAelksatrNFRPDSVLGEGGFGCVFKgwideksltASRPGTGLVIAVKKLN----QDGwQ 114
Cdd:cd08229   4 PVPQFQPQKALRPDMGYNTLA-------NFRIEKKIGRGQFSEVYR---------ATCLLDGVPVALKKVQifdlMDA-K 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 115 GHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEFMPRGSLENHL--FRRGLYFQPLSWKLRLKVALGAAkgLAFL 192
Cdd:cd08229  67 ARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLELADAGDLSRMIkhFKKQKRLIPEKTVWKYFVQLCSA--LEHM 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 193 HSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAKDgpIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLE 272
Cdd:cd08229 145 HSR--RVMHRDIKPANVFITATGVVKLGDLGLGRF--FSSKTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYE 220

                .
gi 15222437 273 L 273
Cdd:cd08229 221 M 221
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
122-277 1.24e-10

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: 61.61  E-value: 1.24e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 122 EVNYLGQFSHRHLVKLIgYCLED---EHRLLVYEFMPRGS---------LENHLFRRglYFQPLswklrlkvalgaAKGL 189
Cdd:cd14118  64 EIAILKKLDHPNVVKLV-EVLDDpneDNLYMVFELVDKGAvmevptdnpLSEETARS--YFRDI------------VLGI 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 190 AFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAkDGPIGDKSHVSTRVmGTHGYAAPEYLATGHLTTKS---DVYSF 266
Cdd:cd14118 129 EYLHYQ--KIIHRDIKPSNLLLGDDGHVKIADFGVS-NEFEGDDALLSSTA-GTPAFMAPEALSESRKKFSGkalDIWAM 204
                       170
                ....*....|.
gi 15222437 267 GVVLLELLSGR 277
Cdd:cd14118 205 GVTLYCFVFGR 215
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
66-302 1.39e-10

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: 61.66  E-value: 1.39e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  66 RNFRPDSVLGEGGFGCVFKGWIDEKSLTASrpgtGLVIAVKKLNQDGWQGHQEwlaEVNYLGQFSHRHLVKLIGY----- 140
Cdd:cd14031  10 RFLKFDIELGRGAFKTVYKGLDTETWVEVA----WCELQDRKLTKAEQQRFKE---EAEMLKGLQHPNIVRFYDSwesvl 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 141 ----CLedehrLLVYEFMPRGSLENHLFRrglyFQPLSWKLRLKVALGAAKGLAFLHSSETRVIYRDFKTSNILLDSEYN 216
Cdd:cd14031  83 kgkkCI-----VLVTELMTSGTLKTYLKR----FKVMKPKVLRSWCRQILKGLQFLHTRTPPIIHRDLKCDNIFITGPTG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 217 A-KLSDFGLAKDGpigdKSHVSTRVMGTHGYAAPEyLATGHLTTKSDVYSFGVVLLELLSGRRAVDKNRPSGE--RNLVE 293
Cdd:cd14031 154 SvKIGDLGLATLM----RTSFAKSVIGTPEFMAPE-MYEEHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQiyRKVTS 228

                ....*....
gi 15222437 294 WAKPYLVNK 302
Cdd:cd14031 229 GIKPASFNK 237
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
73-275 1.51e-10

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: 61.92  E-value: 1.51e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVfkgwIDEKSLTASRPGTGLVIAVKKLNQDGWQG-HQEWLAEVNYLGQF-SHRHLVKLIGYCLEDEHRLLV 150
Cdd:cd05102  14 VLGHGAFGKV----VEASAFGIDKSSSCETVAVKMLKEGATASeHKALMSELKILIHIgNHLNVVNLLGACTKPNGPLMV 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 151 -YEFMPRGSLENHLFRRGLYFQPL---SWKLRLKV--------------------------------------------- 181
Cdd:cd05102  90 iVEFCKYGNLSNFLRAKREGFSPYrerSPRTRSQVrsmveavradrrsrqgsdrvasftestsstnqprqevddlwqspl 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 182 --------ALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAKDgPIGDKSHV---STRVmgTHGYAAPE 250
Cdd:cd05102 170 tmedlicySFQVARGMEFLASR--KCIHRDLAARNILLSENNVVKICDFGLARD-IYKDPDYVrkgSARL--PLKWMAPE 244
                       250       260
                ....*....|....*....|....*
gi 15222437 251 YLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:cd05102 245 SIFDKVYTTQSDVWSFGVLLWEIFS 269
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
54-349 1.70e-10

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: 61.57  E-value: 1.70e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  54 KSFSFAELKSATRNFRPDSVLGEGGFGCVFKgWIDEKSltASRPGTGLVIAVKKLNQdgwqghqEWLAEVNYLGQFS-HR 132
Cdd:cd06638   6 KTIIFDSFPDPSDTWEIIETIGKGTYGKVFK-VLNKKN--GSKAAVKILDPIHDIDE-------EIEAEYNILKALSdHP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 133 HLVKLIG-YCLED----EHRLLVYEFMPRGS---LENHLFRRGLYFQPLSWKLRLKVALgaaKGLAFLHSSETrvIYRDF 204
Cdd:cd06638  76 NVVKFYGmYYKKDvkngDQLWLVLELCNGGSvtdLVKGFLKRGERMEEPIIAYILHEAL---MGLQHLHVNKT--IHRDV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 205 KTSNILLDSEYNAKLSDFGLAKDgpIGDKSHVSTRVMGTHGYAAPEYLATGH-----LTTKSDVYSFGVVLLELLSGRRA 279
Cdd:cd06638 151 KGNNILLTTEGGVKLVDFGVSAQ--LTSTRLRRNTSVGTPFWMAPEVIACEQqldstYDARCDVWSLGITAIELGDGDPP 228
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15222437 280 VDKNRPsgernlvewakpylvnKRKIFRVIDN-----RLQDQYSMEeackVATLSLRCLTTEIKLRPNMSEVVSH 349
Cdd:cd06638 229 LADLHP----------------MRALFKIPRNppptlHQPELWSNE----FNDFIRKCLTKDYEKRPTVSDLLQH 283
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
191-349 2.06e-10

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: 60.64  E-value: 2.06e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 191 FLHssETRVIYRDFKTSNILLDS-EYNAKLSDFGLAKDgpIGDKSHVSTRVMGTHGYAAPE-YLATGHLTTKSDVYSFGV 268
Cdd:cd14164 115 YLH--DMNIVHRDLKCENILLSAdDRKIKIADFGFARF--VEDYPELSTTFCGSRAYTPPEvILGTPYDPKKYDVWSLGV 190
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 269 VLLELLSGRRAVDK---NRPSGERNLVEwakpYLVNkrkifrvidnrlqdqYSMEEACKVATLSLrcLTTEIKLRPNMSE 345
Cdd:cd14164 191 VLYVMVTGTMPFDEtnvRRLRLQQRGVL----YPSG---------------VALEEPCRALIRTL--LQFNPSTRPSIQQ 249

                ....
gi 15222437 346 VVSH 349
Cdd:cd14164 250 VAGN 253
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
71-276 2.15e-10

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: 61.20  E-value: 2.15e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  71 DSVLGEGGFGCVfkgwideksLTASRPGTGLVIAVKKLNQDGWQGHQEWLAEVNYLGQFS-HRHLVKLIGYCLEDEHRLL 149
Cdd:cd14173   7 EEVLGEGAYARV---------QTCINLITNKEYAVKIIEKRPGHSRSRVFREVEMLYQCQgHRNVLELIEFFEEEDKFYL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 150 VYEFMPRGSLENHLFRRGlYFQPLSWKLrlkVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYN---AKLSDFGLAK 226
Cdd:cd14173  78 VFEKMRGGSILSHIHRRR-HFNELEASV---VVQDIASALDFLHNKG--IAHRDLKPENILCEHPNQvspVKICDFDLGS 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 227 DGPI-GDKSHVSTRVM----GTHGYAAPEYLATGH-----LTTKSDVYSFGVVLLELLSG 276
Cdd:cd14173 152 GIKLnSDCSPISTPELltpcGSAEYMAPEVVEAFNeeasiYDKRCDLWSLGVILYIMLSG 211
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
187-276 2.21e-10

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: 61.10  E-value: 2.21e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 187 KGLAFLHSSEtrVIYRDFKTSNILLDSEY---NAKLSDFGLAKdgpIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDV 263
Cdd:cd14197 122 EGVSFLHNNN--VVHLDLKPQNILLTSESplgDIKIVDFGLSR---ILKNSEELREIMGTPEYVAPEILSYEPISTATDM 196
                        90
                ....*....|...
gi 15222437 264 YSFGVVLLELLSG 276
Cdd:cd14197 197 WSIGVLAYVMLTG 209
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
66-276 2.36e-10

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: 60.71  E-value: 2.36e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  66 RNFRPDSVLGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQDG-WQGHQ--EWLAEVNYLGQFSHRHLVKLIGYcL 142
Cdd:cd14189   1 RSYCKGRLLGKGGFARCYE---------MTDLATNKTYAVKVIPHSRvAKPHQreKIVNEIELHRDLHHKHVVKFSHH-F 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 143 EDEHRLLVY-EFMPRGSLEnHLFR-RGLYFQP-LSWKLRLKVAlgaakGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKL 219
Cdd:cd14189  71 EDAENIYIFlELCSRKSLA-HIWKaRHTLLEPeVRYYLKQIIS-----GLKYLHLKG--ILHRDLKLGNFFINENMELKV 142
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15222437 220 SDFGLA-KDGPIGDKSHVstrVMGTHGYAAPEYL-ATGHlTTKSDVYSFGVVLLELLSG 276
Cdd:cd14189 143 GDFGLAaRLEPPEQRKKT---ICGTPNYLAPEVLlRQGH-GPESDVWSLGCVMYTLLCG 197
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
52-276 2.54e-10

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


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 60.79  E-value: 2.54e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  52 NLKSFSFAELKSATRNFRPDSVLGEGGFGCVFKGwideksltaSRPGTGLVIAVKKLNQDGwQGHQEWLAEVNYLGQFSH 131
Cdd:cd06636   2 SLDDIDLSALRDPAGIFELVEVVGNGTYGQVYKG---------RHVKTGQLAAIKVMDVTE-DEEEEIKLEINMLKKYSH 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 132 -RHLVKLIGYCLE------DEHRLLVYEFMPRGSLENHLFR-RGLYFQPlSWKLRLKVALgaAKGLAFLHSSetRVIYRD 203
Cdd:cd06636  72 hRNIATYYGAFIKksppghDDQLWLVMEFCGAGSVTDLVKNtKGNALKE-DWIAYICREI--LRGLAHLHAH--KVIHRD 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 204 FKTSNILLDSEYNAKLSDFGLAK--DGPIGDKShvstRVMGTHGYAAPEYLATGH-----LTTKSDVYSFGVVLLELLSG 276
Cdd:cd06636 147 IKGQNVLLTENAEVKLVDFGVSAqlDRTVGRRN----TFIGTPYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEMAEG 222
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
66-273 2.69e-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: 60.48  E-value: 2.69e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  66 RNFRPDSVLGEGGFGCVFKGWIDEKSLTASrpgtGLVIAVKKLNQDGWQGHQEwlaEVNYLGQFSHRHLVKLIGYcLEDE 145
Cdd:cd14032   1 RFLKFDIELGRGSFKTVYKGLDTETWVEVA----WCELQDRKLTKVERQRFKE---EAEMLKGLQHPNIVRFYDF-WESC 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 146 HR-----LLVYEFMPRGSLENHLFRrglyFQPLSWKLRLKVALGAAKGLAFLHSSETRVIYRDFKTSNILLDSEYNA-KL 219
Cdd:cd14032  73 AKgkrciVLVTELMTSGTLKTYLKR----FKVMKPKVLRSWCRQILKGLLFLHTRTPPIIHRDLKCDNIFITGPTGSvKI 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15222437 220 SDFGLAKDgpigDKSHVSTRVMGTHGYAAPEyLATGHLTTKSDVYSFGVVLLEL 273
Cdd:cd14032 149 GDLGLATL----KRASFAKSVIGTPEFMAPE-MYEEHYDESVDVYAFGMCMLEM 197
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
74-349 2.72e-10

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: 60.78  E-value: 2.72e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKgwideksLTASRPGTglVIAVKKLNQDGwQGHQEWLAEVNYLGQFS-HRHLVKLIGYCLEDEHRL---- 148
Cdd:cd06639  30 IGKGTYGKVYK-------VTNKKDGS--LAAVKILDPIS-DVDEEIEAEYNILRSLPnHPNVVKFYGMFYKADQYVggql 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 -LVYEFMPRGS---LENHLFRRGlyfQPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGL 224
Cdd:cd06639 100 wLVLELCNGGSvteLVKGLLKCG---QRLDEAMISYILYGALLGLQHLHNN--RIIHRDVKGNNILLTTEGGVKLVDFGV 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 225 AkdgpigdKSHVSTRV-----MGTHGYAAPEYLATGH-----LTTKSDVYSFGVVLLELLSGRRAVDKNRPSgernlvew 294
Cdd:cd06639 175 S-------AQLTSARLrrntsVGTPFWMAPEVIACEQqydysYDARCDVWSLGITAIELADGDPPLFDMHPV-------- 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15222437 295 akpylvnkRKIFRVIDNRLQDQYSMEEACK-VATLSLRCLTTEIKLRPNMSEVVSH 349
Cdd:cd06639 240 --------KALFKIPRNPPPTLLNPEKWCRgFSHFISQCLIKDFEKRPSVTHLLEH 287
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
167-275 3.19e-10

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: 61.17  E-value: 3.19e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 167 GLYFQPLSWKLRLKVALGAAKGLAFLhsSETRVIYRDFKTSNILLDSEYNAKLSDFGLAKD---GP----IGDkSHVSTR 239
Cdd:cd14207 171 DFYKRPLTMEDLISYSFQVARGMEFL--SSRKCIHRDLAARNILLSENNVVKICDFGLARDiykNPdyvrKGD-ARLPLK 247
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15222437 240 VMgthgyaAPEYLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:cd14207 248 WM------APESIFDKIYSTKSDVWSYGVLLWEIFS 277
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
140-276 3.40e-10

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: 61.24  E-value: 3.40e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 140 YCLEDEHRL-LVYEFMPRGSLENHLFRrglYFQPLSWK----LRLKVALGAAKGLAFLHssetrviyRDFKTSNILLDSE 214
Cdd:cd05596  93 YAFQDDKYLyMVMDYMPGGDLVNLMSN---YDVPEKWArfytAEVVLALDAIHSMGFVH--------RDVKPDNMLLDAS 161
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 215 YNAKLSDFG----LAKDGpigdKSHVSTRVmGTHGYAAPEYLAT----GHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd05596 162 GHLKLADFGtcmkMDKDG----LVRSDTAV-GTPDYISPEVLKSqggdGVYGRECDWWSVGVFLYEMLVG 226
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
131-276 4.20e-10

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: 59.83  E-value: 4.20e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 131 HRHLVKLIGYCLEDEHRLLVYEFMPRGSLENHLFRRglyfQPLSWKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNIL 210
Cdd:cd14070  62 HPNITQLLDILETENSYYLVMELCPGGNLMHRIYDK----KRLEEREARRYIRQLVSAVEHLHRAG--VVHRDLKIENLL 135
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15222437 211 LDSEYNAKLSDFGLAKDGPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14070 136 LDENDNIKLIDFGLSNCAGILGYSDPFSTQCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTG 201
PK_NRBP1_like cd13984
Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The ...
126-349 5.07e-10

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: 59.47  E-value: 5.07e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 126 LGQFSHRHLVKLIGYCL---EDEHRLL-VYEFMPRGSLENHL--FRRGLYFQPL-SWKLRLKVALGAakgLAFLHSSETR 198
Cdd:cd13984  49 LIQLDHPNIVKFHRYWTdvqEEKARVIfITEYMSSGSLKQFLkkTKKNHKTMNEkSWKRWCTQILSA---LSYLHSCDPP 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 199 VIYRDFKTSNILLdsEYNaklsdfGLAKDGPIGDKS---HVST--RVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLEL 273
Cdd:cd13984 126 IIHGNLTCDTIFI--QHN------GLIKIGSVAPDAihnHVKTcrEEHRNLHFFAPEYGYLEDVTTAVDIYSFGMCALEM 197
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15222437 274 lsgrrAVDKNRPSGErnlvewakPYLVNKRKIFRVI---DNRLQDQYSMeeackvatlslRCLTTEIKLRPNMSEVVSH 349
Cdd:cd13984 198 -----AALEIQSNGE--------KVSANEEAIIRAIfslEDPLQKDFIR-----------KCLSVAPQDRPSARDLLFH 252
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
67-278 5.11e-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: 60.46  E-value: 5.11e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGCVfkgwideksLTASRPGTGLVIAVKKLNQ--DGWQGHQEWLAEVNYLGQFSHRHLVKLI------ 138
Cdd:cd07855   6 RYEPIETIGSGAYGVV---------CSAIDTKSGQKVAIKKIPNafDVVTTAKRTLRELKILRHFKHDNIIAIRdilrpk 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 139 GYCLEDEHRLLVYEFMP---------RGSLENHLFRRGLYfQPLswklrlkvalgaaKGLAFLHSSEtrVIYRDFKTSNI 209
Cdd:cd07855  77 VPYADFKDVYVVLDLMEsdlhhiihsDQPLTLEHIRYFLY-QLL-------------RGLKYIHSAN--VIHRDLKPSNL 140
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15222437 210 LLDSEYNAKLSDFGLAK---DGPIgDKSHVSTRVMGTHGYAAPEYLATGH-LTTKSDVYSFGVVLLELLsGRR 278
Cdd:cd07855 141 LVNENCELKIGDFGMARglcTSPE-EHKYFMTEYVATRWYRAPELMLSLPeYTQAIDMWSVGCIFAEML-GRR 211
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
74-275 5.17e-10

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: 59.98  E-value: 5.17e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGwideKSLTasrpgTGLVIAVKKLNQdgwqgHQEWLAEVNYLGQF-------SHRHLVKLIGYCLEDEH 146
Cdd:cd07831   7 IGEGTFSEVLKA----QSRK-----TGKYYAIKCMKK-----HFKSLEQVNNLREIqalrrlsPHPNILRLIEVLFDRKT 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 147 -RL-LVYEFMpRGSLENHLFRRGLYFQPLSWKLRLKVALgaaKGLAFLHSSEtrVIYRDFKTSNILLDSEyNAKLSDFGL 224
Cdd:cd07831  73 gRLaLVFELM-DMNLYELIKGRKRPLPEKRVKNYMYQLL---KSLDHMHRNG--IFHRDIKPENILIKDD-ILKLADFGS 145
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15222437 225 AKDgpIGDK----SHVSTRvmgthGYAAPEYLAT-GHLTTKSDVYSFGVVLLELLS 275
Cdd:cd07831 146 CRG--IYSKppytEYISTR-----WYRAPECLLTdGYYGPKMDIWAVGCVFFEILS 194
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
74-273 7.07e-10

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: 59.46  E-value: 7.07e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKgwideksltASRPGTGLVIAVKK--LNQDGWQGHQEWLAEVNYLGQFSHR-HLVKLIgyCLEDEHR--- 147
Cdd:cd07837   9 IGEGTYGKVYK---------ARDKNTGKLVALKKtrLEMEEEGVPSTALREVSLLQMLSQSiYIVRLL--DVEHVEEngk 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 148 ---LLVYEFMPRgSLENHL--FRRGLYfQPLSWKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNA-KLSD 221
Cdd:cd07837  78 pllYLVFEYLDT-DLKKFIdsYGRGPH-NPLPAKTIQSFMYQLCKGVAHCHSHG--VMHRDLKPQNLLVDKQKGLlKIAD 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15222437 222 FGLAKDGPIGDKSHvsTRVMGTHGYAAPE-YLATGHLTTKSDVYSFGVVLLEL 273
Cdd:cd07837 154 LGLGRAFTIPIKSY--THEIVTLWYRAPEvLLGSTHYSTPVDMWSVGCIFAEM 204
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
73-284 8.13e-10

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 59.69  E-value: 8.13e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKGWidekSLTASRPgtgLVIAVKKLNQDgWQG------HQEWLAEVNYLGQFSHRHLVKLIGY-CLEDE 145
Cdd:cd14041  13 LLGRGGFSEVYKAF----DLTEQRY---VAVKIHQLNKN-WRDekkenyHKHACREYRIHKELDHPRIVKLYDYfSLDTD 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 146 HRLLVYEFMPRGSLENHLFRRGLyfqpLSWKLRLKVALGAAKGLAFLHSSETRVIYRDFKTSNILLDSEY---NAKLSDF 222
Cdd:cd14041  85 SFCTVLEYCEGNDLDFYLKQHKL----MSEKEARSIIMQIVNALKYLNEIKPPIIHYDLKPGNILLVNGTacgEIKITDF 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15222437 223 GLAK---DGPIG--DKSHVSTRVMGTHGYAAPEYLATGH----LTTKSDVYSFGVVLLELLSGRRAVDKNR 284
Cdd:cd14041 161 GLSKimdDDSYNsvDGMELTSQGAGTYWYLPPECFVVGKeppkISNKVDVWSVGVIFYQCLYGRKPFGHNQ 231
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
74-276 8.27e-10

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: 59.22  E-value: 8.27e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKgwIDEKsltasrpGTGLVIAVKKLNQDGWQGHQEwLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEF 153
Cdd:cd14113  15 LGRGRFSVVKK--CDQR-------GTKRAVATKFVNKKLMKRDQV-THELGVLQSLQHPQLVGLLDTFETPTSYILVLEM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 154 MPRGSLENHLFRRG-LYFQPLSWKLRlkvalGAAKGLAFLHSseTRVIYRDFKTSNILLD---SEYNAKLSDFGlakDGP 229
Cdd:cd14113  85 ADQGRLLDYVVRWGnLTEEKIRFYLR-----EILEALQYLHN--CRIAHLDLKPENILVDqslSKPTIKLADFG---DAV 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15222437 230 IGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14113 155 QLNTTYYIHQLLGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSG 201
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
73-321 8.50e-10

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A splice variant of TLK1, called TLK1B, is expressed in the presence of double strand breaks (DSBs). It lacks the N-terminal part of TLK1, but is expected to phosphorylate the same substrates. TLK1/1B interacts with Rad9, which is critical in DNA damage-activated checkpoint response, and plays a role in the repair of linearized DNA with incompatible ends. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. The TLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 59.30  E-value: 8.50e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKGW-IDEKSLTAsrpgtglvIAVKKLNQDgWQG------HQEWLAEVNYLGQFSHRHLVKLIGY-CLED 144
Cdd:cd14040  13 LLGRGGFSEVYKAFdLYEQRYAA--------VKIHQLNKS-WRDekkenyHKHACREYRIHKELDHPRIVKLYDYfSLDT 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 145 EHRLLVYEFMPRGSLENHLFRRGLyfqpLSWKLRLKVALGAAKGLAFLHSSETRVIYRDFKTSNILL---DSEYNAKLSD 221
Cdd:cd14040  84 DTFCTVLEYCEGNDLDFYLKQHKL----MSEKEARSIVMQIVNALRYLNEIKPPIIHYDLKPGNILLvdgTACGEIKITD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 222 FGLAK---DGPIG-DKSHVSTRVMGTHGYAAPEYLATGH----LTTKSDVYSFGVVLLELLSGRRAVDKNRPSG---ERN 290
Cdd:cd14040 160 FGLSKimdDDSYGvDGMDLTSQGAGTYWYLPPECFVVGKeppkISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQdilQEN 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 15222437 291 LVEWA-------KPYLVNKRKIF--RVIDNRLQDQYSMEE 321
Cdd:cd14040 240 TILKAtevqfpvKPVVSNEAKAFirRCLAYRKEDRFDVHQ 279
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
122-276 9.62e-10

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: 59.07  E-value: 9.62e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 122 EVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEFMPRGSLENHLFRRGLYFQplswklrlKVALGAAK----GLAFLHssET 197
Cdd:cd14085  48 EIGVLLRLSHPNIIKLKEIFETPTEISLVLELVTGGELFDRIVEKGYYSE--------RDAADAVKqileAVAYLH--EN 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 198 RVIYRDFKTSNILLDSEYN---AKLSDFGLAKdgpIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELL 274
Cdd:cd14085 118 GIVHRDLKPENLLYATPAPdapLKIADFGLSK---IVDQQVTMKTVCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILL 194

                ..
gi 15222437 275 SG 276
Cdd:cd14085 195 CG 196
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
71-277 9.77e-10

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: 59.28  E-value: 9.77e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  71 DSVLGEGGFG----CVFKGwideksltasrpgTGLVIAVKKLNQDGWQGHQEWLAEVNYLGqfSHRHLVKLIGYCLEDEH 146
Cdd:cd14179  12 DKPLGEGSFSicrkCLHKK-------------TNQEYAVKIVSKRMEANTQREIAALKLCE--GHPNIVKLHEVYHDQLH 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 147 RLLVYEFMPRGSLENHLFRRGLYFQP-LSWKLRLKVAlgaakglAFLHSSETRVIYRDFKTSNILLDSEYN---AKLSDF 222
Cdd:cd14179  77 TFLVMELLKGGELLERIKKKQHFSETeASHIMRKLVS-------AVSHMHDVGVVHRDLKPENLLFTDESDnseIKIIDF 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15222437 223 GLAKDGPiGDKSHVSTRVMGTHgYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd14179 150 GFARLKP-PDNQPLKTPCFTLH-YAAPELLNYNGYDESCDLWSLGVILYTMLSGQ 202
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
60-277 9.77e-10

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: 9.77e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  60 ELKSATRNFRPdsvLGEGGFGCVFKGWiDEKsltasrpgTGLVIAVKKLNQDgWQG---HQEWLAEVNYLGQFSHRHLVK 136
Cdd:cd07877  14 EVPERYQNLSP---VGSGAYGSVCAAF-DTK--------TGLRVAVKKLSRP-FQSiihAKRTYRELRLLKHMKHENVIG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 137 LI-----GYCLEDEHRLLVYEFMPRGSLENHLFRRGL---YFQPLSWKLrlkvalgaAKGLAFLHSSEtrVIYRDFKTSN 208
Cdd:cd07877  81 LLdvftpARSLEEFNDVYLVTHLMGADLNNIVKCQKLtddHVQFLIYQI--------LRGLKYIHSAD--IIHRDLKPSN 150
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 209 ILLDSEYNAKLSDFGLAKDGPIGDKSHVSTRvmgthGYAAPEYLATG-HLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd07877 151 LAVNEDCELKILDFGLARHTDDEMTGYVATR-----WYRAPEIMLNWmHYNQTVDIWSVGCIMAELLTGR 215
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
199-349 1.04e-09

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: 58.85  E-value: 1.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 199 VIYRDFKTSNILLDSeYNAKLSDFGLAKDGPIGDKsHVSTRVMGTHGYAAPEYL-ATGHLTTKSDVYSFGVVLLELLSGr 277
Cdd:cd14163 122 VAHRDLKCENALLQG-FTLKLTDFGFAKQLPKGGR-ELSQTFCGSTAYAAPEVLqGVPHDSRKGDIWSMGVVLYVMLCA- 198
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15222437 278 ravdkNRPSGERNLvewakPYLVNKRKIFRVIDNRLqdqySMEEACKvaTLSLRCLTTEIKLRPNMSEVVSH 349
Cdd:cd14163 199 -----QLPFDDTDI-----PKMLCQQQKGVSLPGHL----GVSRTCQ--DLLKRLLEPDMVLRPSIEEVSWH 254
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
60-277 1.08e-09

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: 59.41  E-value: 1.08e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  60 ELKSATRNFRPdsvLGEGGFGCVFKGwIDEKSltasrpgtGLVIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIG 139
Cdd:cd07854   2 DLGSRYMDLRP---LGCGSNGLVFSA-VDSDC--------DKRVAVKKIVLTDPQSVKHALREIKIIRRLDHDNIVKVYE 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 140 YCLEDEHRL--------------LVYEFMprgslENHLfRRGLYFQPLSWKLRLKVALGAAKGLAFLHSSEtrVIYRDFK 205
Cdd:cd07854  70 VLGPSGSDLtedvgsltelnsvyIVQEYM-----ETDL-ANVLEQGPLSEEHARLFMYQLLRGLKYIHSAN--VLHRDLK 141
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15222437 206 TSNILLDSE-YNAKLSDFGLAK--DGPIGDKSHVSTRVMgTHGYAAPE-YLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd07854 142 PANVFINTEdLVLKIGDFGLARivDPHYSHKGYLSEGLV-TKWYRSPRlLLSPNNYTKAIDMWAAGCIFAEMLTGK 216
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
188-284 1.29e-09

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: 59.34  E-value: 1.29e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 188 GLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAK---DGPIGDKSHVsTRVMGTHGYAAPEYLATGHLTTKS-DV 263
Cdd:cd07857 117 GLKYIHSAN--VLHRDLKPGNLLVNADCELKICDFGLARgfsENPGENAGFM-TEYVATRWYRAPEIMLSFQSYTKAiDV 193
                        90       100
                ....*....|....*....|.
gi 15222437 264 YSFGVVLLELLsGRRAVDKNR 284
Cdd:cd07857 194 WSVGCILAELL-GRKPVFKGK 213
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
74-277 1.49e-09

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: 58.71  E-value: 1.49e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKgwidekslTASRPgTGLVIAVK--KLNQDGWQGHQeWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVY 151
Cdd:cd06622   9 LGKGNYGSVYK--------VLHRP-TGVTMAMKeiRLELDESKFNQ-IIMELDILHKAVSPYIVDFYGAFFIEGAVYMCM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 152 EFMPRGSLENhLFRRGLYFQPLSWKLRLKVALGAAKGLAFLhSSETRVIYRDFKTSNILLDSEYNAKLSDFGLAkdGPIg 231
Cdd:cd06622  79 EYMDAGSLDK-LYAGGVATEGIPEDVLRRITYAVVKGLKFL-KEEHNIIHRDVKPTNVLVNGNGQVKLCDFGVS--GNL- 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15222437 232 DKSHVSTRVmGTHGYAAPEYLATGHL------TTKSDVYSFGVVLLELLSGR 277
Cdd:cd06622 154 VASLAKTNI-GCQSYMAPERIKSGGPnqnptyTVQSDVWSLGLSILEMALGR 204
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
73-278 1.76e-09

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I Receptor and Activin Type IB/IC Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR1, also called Activin receptor-Like Kinase 5 (ALK5), functions as a receptor for TGFbeta and phoshorylates SMAD2/3. TGFbeta proteins are cytokines that regulate cell growth, differentiation, and survival, and are critical in the development and progression of many human cancers. Mutations in TGFbR1 (and TGFbR2) can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. ACVR1b (also called ALK4) and ACVR1c (also called ALK7) act as receptors for activin A and B, respectively. TGFbR1, ACVR1b, and ACVR1c belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like TGFbR1, ACVR1b, and ACVR1c, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The TGFbR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 58.22  E-value: 1.76e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKG-WIDEKsltasrpgtglvIAVKKLNQdgwQGHQEWLAEVNYLGQFSHRHlVKLIGYCLEDE------ 145
Cdd:cd14143   2 SIGKGRFGEVWRGrWRGED------------VAVKIFSS---REERSWFREAEIYQTVMLRH-ENILGFIAADNkdngtw 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 146 -HRLLVYEFMPRGSLENHLFRrglyfQPLSWKLRLKVALGAAKGLAFLH------SSETRVIYRDFKTSNILLDSEYNAK 218
Cdd:cd14143  66 tQLWLVSDYHEHGSLFDYLNR-----YTVTVEGMIKLALSIASGLAHLHmeivgtQGKPAIAHRDLKSKNILVKKNGTCC 140
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15222437 219 LSDFGLA-KDGPIGDKSHV-STRVMGTHGYAAPEYL----ATGHLTT--KSDVYSFGVVLLELlsGRR 278
Cdd:cd14143 141 IADLGLAvRHDSATDTIDIaPNHRVGTKRYMAPEVLddtiNMKHFESfkRADIYALGLVFWEI--ARR 206
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
74-274 1.86e-09

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: 58.08  E-value: 1.86e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWIDEKSLTASrpgtglvIAVKKLNQD-GWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYE 152
Cdd:cd05087   5 IGHGWFGKVFLGEVNSGLSSTQ-------VVVKELKASaSVQDQMQFLEEAQPYRALQHTNLLQCLAQCAEVTPYLLVME 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMPRGSLENHL----FRRGLYFQPLSWKlrlKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLA--- 225
Cdd:cd05087  78 FCPLGDLKGYLrscrAAESMAPDPLTLQ---RMACEVACGLLHLHRNN--FVHSDLALRNCLLTADLTVKIGDYGLShck 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15222437 226 -KDG--PIGDKSHVSTRvmgthgYAAPEYLATGH-------LTTKSDVYSFGVVLLELL 274
Cdd:cd05087 153 yKEDyfVTADQLWVPLR------WIAPELVDEVHgnllvvdQTKQSNVWSLGVTIWELF 205
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
187-277 1.92e-09

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: 58.74  E-value: 1.92e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 187 KGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPIGDKSHVSTRVmgthgYAAPEYLATGH-LTTKSDVYS 265
Cdd:cd07856 119 RGLKYVHSAG--VIHRDLKPSNILVNENCDLKICDFGLARIQDPQMTGYVSTRY-----YRAPEIMLTWQkYDVEVDIWS 191
                        90
                ....*....|..
gi 15222437 266 FGVVLLELLSGR 277
Cdd:cd07856 192 AGCIFAEMLEGK 203
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
187-277 2.04e-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: 58.46  E-value: 2.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 187 KGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAKdgpigDKSHVSTRVMGTHGYAAPE-YLATGHLTTKSDVYS 265
Cdd:cd07851 129 RGLKYIHSA--GIIHRDLKPSNLAVNEDCELKILDFGLAR-----HTDDEMTGYVATRWYRAPEiMLNWMHYNQTVDIWS 201
                        90
                ....*....|..
gi 15222437 266 FGVVLLELLSGR 277
Cdd:cd07851 202 VGCIMAELLTGK 213
PTK_Jak1_rpt1 cd05077
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely ...
128-309 2.04e-09

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; 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 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. It modulates the kinase activity of the C-terminal catalytic domain. The Jak1 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: 270662 [Multi-domain]  Cd Length: 266  Bit Score: 58.02  E-value: 2.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 128 QFSHRHLVKLIGYCLEDEHRLLVYEFMPRGSLENHLFRRGlyfQPLSWKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTS 207
Cdd:cd05077  64 QVSHKHIVLLYGVCVRDVENIMVEEFVEFGPLDLFMHRKS---DVLTTPWKFKVAKQLASALSYLEDKD--LVHGNVCTK 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 208 NILL-----DSEYNA--KLSDFGLakdgPIG--DKSHVSTRVmgthGYAAPEYLA-TGHLTTKSDVYSFGVVLLEL---- 273
Cdd:cd05077 139 NILLaregiDGECGPfiKLSDPGI----PITvlSRQECVERI----PWIAPECVEdSKNLSIAADKWSFGTTLWEIcyng 210
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15222437 274 ---LSGRRAVDKNR----------PSGER--NLVEWAKPYLVNKRKIFRVI 309
Cdd:cd05077 211 eipLKDKTLAEKERfyegqcmlvtPSCKElaDLMTHCMNYDPNQRPFFRAI 261
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
74-280 2.08e-09

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1 functions as a receptor for morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Vertebrates contain two type I BMP receptors, BMPR1a and BMPR1b. BMPR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that also includes TGFbeta, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 58.26  E-value: 2.08e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKG-WIDEKsltasrpgtglvIAVKKlnqdgWQGHQE--WLAEVNYLGQFSHRHlVKLIGYCLED------ 144
Cdd:cd14144   3 VGKGRYGEVWKGkWRGEK------------VAVKI-----FFTTEEasWFRETEIYQTVLMRH-ENILGFIAADikgtgs 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 145 -EHRLLVYEFMPRGSLENHLFRRGLYFQPLswklrLKVALGAAKGLAFLHSS------ETRVIYRDFKTSNILLDSEYNA 217
Cdd:cd14144  65 wTQLYLITDYHENGSLYDFLRGNTLDTQSM-----LKLAYSAACGLAHLHTEifgtqgKPAIAHRDIKSKNILVKKNGTC 139
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15222437 218 KLSDFGLA-KDGPIGDKSHV--STRVmGTHGYAAPEYLAT----GHLTT--KSDVYSFGVVLLELlsGRRAV 280
Cdd:cd14144 140 CIADLGLAvKFISETNEVDLppNTRV-GTKRYMAPEVLDEslnrNHFDAykMADMYSFGLVLWEI--ARRCI 208
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
69-276 2.30e-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: 57.95  E-value: 2.30e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  69 RPdsvLGEGGFGCVFkgwidekslTASRPGTGLVIAVK-----KLNQDGWQgHQeWLAEVNYLGQFSHRHLVKLIGYCLE 143
Cdd:cd14117  12 RP---LGKGKFGNVY---------LAREKQSKFIVALKvlfksQIEKEGVE-HQ-LRREIEIQSHLRHPNILRLYNYFHD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 144 DEHRLLVYEFMPRGSLENHLFRRGLYFQPLSWKLRLKVAlgaaKGLAFLHssETRVIYRDFKTSNILLDSEYNAKLSDFG 223
Cdd:cd14117  78 RKRIYLILEYAPRGELYKELQKHGRFDEQRTATFMEELA----DALHYCH--EKKVIHRDIKPENLLMGYKGELKIADFG 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15222437 224 LAKDGPigdksHVSTRVM-GTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14117 152 WSVHAP-----SLRRRTMcGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVG 200
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
73-277 2.31e-09

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: 58.16  E-value: 2.31e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKGwideKSLTasrpgTGLVIAVKKLNQDgwqgHQEWLA-----EVNYLGQFSHRHLVKLIGYCLEDEHR 147
Cdd:cd07844   7 KLGEGSYATVYKG----RSKL-----TGQLVALKEIRLE----HEEGAPftairEASLLKDLKHANIVTLHDIIHTKKTL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 148 LLVYEFMPRgSLENHLFRRGLYFQPLSWKLRLKVALgaaKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAKD 227
Cdd:cd07844  74 TLVFEYLDT-DLKQYMDDCGGGLSMHNVRLFLFQLL---RGLAYCHQR--RVLHRDLKPQNLLISERGELKLADFGLARA 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15222437 228 GPIGDKSHVSTRVmgTHGYAAPEYL--ATGHlTTKSDVYSFGVVLLELLSGR 277
Cdd:cd07844 148 KSVPSKTYSNEVV--TLWYRPPDVLlgSTEY-STSLDMWGVGCIFYEMATGR 196
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
73-283 2.43e-09

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: 57.68  E-value: 2.43e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGcvfkgwideKSLTASRPGTGLVIAVKKLN-QDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVY 151
Cdd:cd08219   7 VVGEGSFG---------RALLVQHVNSDQKYAMKEIRlPKSSSAVEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 152 EFMPRGSLENHL-FRRGLYFQP---LSWKLRLkvalgaakGLAFLHSSETRVIYRDFKTSNILLDSEYNAKLSDFGLAK- 226
Cdd:cd08219  78 EYCDGGDLMQKIkLQRGKLFPEdtiLQWFVQM--------CLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARl 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15222437 227 -DGPIgdkSHVSTRVmGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGRRAVDKN 283
Cdd:cd08219 150 lTSPG---AYACTYV-GTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQAN 203
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
149-276 2.44e-09

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: 58.35  E-value: 2.44e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 LVYEFMPRGSLENHLFRRGLYFQPlswklRLKVALgAAKGLAFLHSSETRVIYRDFKTSNILLDSEYNAKLSDFGLAKDG 228
Cdd:cd05586  73 LVTDYMSGGELFWHLQKEGRFSED-----RAKFYI-AELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSKAD 146
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15222437 229 PIGDKShvSTRVMGTHGYAAPEYL--ATGHlTTKSDVYSFGVVLLELLSG 276
Cdd:cd05586 147 LTDNKT--TNTFCGTTEYLAPEVLldEKGY-TKMVDFWSLGVLVFEMCCG 193
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
130-277 2.76e-09

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: 57.96  E-value: 2.76e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 130 SHRHLVKLIGYCLEDEHRLLVYEFMPRGSLENHLFRRGLYFQPLSWKLrLKVALGAakgLAFLHssETRVIYRDFKTSNI 209
Cdd:cd14180  59 SHPNIVALHEVLHDQYHTYLVMELLRGGELLDRIKKKARFSESEASQL-MRSLVSA---VSFMH--EAGVVHRDLKPENI 132
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15222437 210 LLDSEYNA---KLSDFGLAKDGPIGDKShVSTRVMGTHgYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd14180 133 LYADESDGavlKVIDFGFARLRPQGSRP-LQTPCFTLQ-YAAPELFSNQGYDESCDLWSLGVILYTMLSGQ 201
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
73-273 3.24e-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: 57.52  E-value: 3.24e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQDGWQGHQEWLAEVNYLGQFS-HRHLVKLIG--YCLEDEHRLL 149
Cdd:cd14036   7 VIAEGGFAFVYE---------AQDVGTGKEYALKRLLSNEEEKNKAIIQEINFMKKLSgHPNIVQFCSaaSIGKEESDQG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 150 VYEFM-----PRGSLENhLFRRGLYFQPLSWKLRLKVALGAAKGLAFLHSSETRVIYRDFKTSNILLDSEYNAKLSDFGL 224
Cdd:cd14036  78 QAEYLlltelCKGQLVD-FVKKVEAPGPFSPDTVLKIFYQTCRAVQHMHKQSPPIIHRDLKIENLLIGNQGQIKLCDFGS 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15222437 225 AKDGPI--------GDKSHVS---TRVMgTHGYAAPEYLATGH---LTTKSDVYSFGVVLLEL 273
Cdd:cd14036 157 ATTEAHypdyswsaQKRSLVEdeiTRNT-TPMYRTPEMIDLYSnypIGEKQDIWALGCILYLL 218
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
68-276 3.61e-09

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: 56.96  E-value: 3.61e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  68 FRPDSVLGEGGFGCVfKGWIDEKsltasrpgTGLVIAVKKLNQDGWQGHQEWLA-EVNYLGQFSHRHLVKLIGYCLEDEH 146
Cdd:cd14184   3 YKIGKVIGDGNFAVV-KECVERS--------TGKEFALKIIDKAKCCGKEHLIEnEVSILRRVKHPNIIMLIEEMDTPAE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 147 RLLVYEFMPRGSLENHLFRRGLYFQplswKLRLKVALGAAKGLAFLHSseTRVIYRDFKTSNILL----DSEYNAKLSDF 222
Cdd:cd14184  74 LYLVMELVKGGDLFDAITSSTKYTE----RDASAMVYNLASALKYLHG--LCIVHRDIKPENLLVceypDGTKSLKLGDF 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15222437 223 GLAK--DGPIgdkshvsTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14184 148 GLATvvEGPL-------YTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCG 196
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
74-276 3.71e-09

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 57.73  E-value: 3.71e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWideksltasRPGTGLVIAVKKLNQDGWQGHQEWLaEVNYLGQFSHR-----HLVKLIGYCLEDEHRL 148
Cdd:cd14229   8 LGRGTFGQVVKCW---------KRGTNEIVAVKILKNHPSYARQGQI-EVGILARLSNEnadefNFVRAYECFQHRNHTC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 LVYEFmprgsLENHL--FRRGLYFQPLSWKL------RLKVALGAAKGLAFLHSsetrviyrDFKTSNILL----DSEYN 216
Cdd:cd14229  78 LVFEM-----LEQNLydFLKQNKFSPLPLKVirpilqQVATALKKLKSLGLIHA--------DLKPENIMLvdpvRQPYR 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15222437 217 AKLSDFGLAkdgpigdkSHVSTRVMGTH----GYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14229 145 VKVIDFGSA--------SHVSKTVCSTYlqsrYYRAPEIILGLPFCEAIDMWSLGCVIAELFLG 200
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
121-278 3.76e-09

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 58.49  E-value: 3.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  121 AEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEFMPRGSLENHLFRR---GLYFQPLSWKLRL-KVALGaakgLAFLHSSe 196
Cdd:PTZ00267 114 SELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYGSGGDLNKQIKQRlkeHLPFQEYEVGLLFyQIVLA----LDEVHSR- 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  197 tRVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:PTZ00267 189 -KMMHRDLKSANIFLMPTGIIKLGDFGFSKQYSDSVSLDVASSFCGTPYYLAPELWERKRYSKKADMWSLGVILYELLTL 267

                 ..
gi 15222437  277 RR 278
Cdd:PTZ00267 268 HR 269
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
74-349 3.94e-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: 3.94e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGwideksltASRPgTGLVIAVKKLNQDGWQGHQ-EWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYE 152
Cdd:cd07870   8 LGEGSYATVYKG--------ISRI-NGQLVALKVISMKTEEGVPfTAIREASLLKGLKHANIVLLHDIIHTKETLTFVFE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMpRGSLENHLFRRGLYFQPLSWKLRLKVALgaaKGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPIGD 232
Cdd:cd07870  79 YM-HTDLAQYMIQHPGGLHPYNVRLFMFQLL---RGLAYIHGQ--HILHRDLKPQNLLISYLGELKLADFGLARAKSIPS 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 233 KSHVSTRVmgTHGYAAPEYL--ATGHlTTKSDVYSFGVVLLELLSGRRAVDKNRPSGERNLVEWA--------------- 295
Cdd:cd07870 153 QTYSSEVV--TLWYRPPDVLlgATDY-SSALDIWGAGCIFIEMLQGQPAFPGVSDVFEQLEKIWTvlgvptedtwpgvsk 229
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 296 ----KP--YLVNKRKIFRVIDNRLQDQYSMEEackvatLSLRCLTTEIKLRPNMSEVVSH 349
Cdd:cd07870 230 lpnyKPewFLPCKPQQLRVVWKRLSRPPKAED------LASQMLMMFPKDRISAQDALLH 283
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
72-277 4.05e-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: 57.55  E-value: 4.05e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  72 SVLGEGGFGCVFKGwIDEKsltasrpgTGLVIAVKKL-NQDGWqgHQEWLAEVNYL------GQFSHRHLVKLIGYCLED 144
Cdd:cd14210  19 SVLGKGSFGQVVKC-LDHK--------TGQLVAIKIIrNKKRF--HQQALVEVKILkhlndnDPDDKHNIVRYKDSFIFR 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 145 EHRLLVYEfmprgslenhLFRRGLY-------FQPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILL--DSEY 215
Cdd:cd14210  88 GHLCIVFE----------LLSINLYellksnnFQGLSLSLIRKFAKQILQALQFLHKL--NIIHCDLKPENILLkqPSKS 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15222437 216 NAKLSDFGLAkdGPIGDKSH--VSTRVmgthgYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd14210 156 SIKVIDFGSS--CFEGEKVYtyIQSRF-----YRAPEVILGLPYDTAIDMWSLGCILAELYTGY 212
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
131-277 4.13e-09

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: 57.55  E-value: 4.13e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 131 HRHLVKLIGYCLEDEHRLLVYEFMPRGSLENHLFRR---GLYFQPLSWKLRLKVALGAakgLAFLHssETRVIYRDFKTS 207
Cdd:cd14094  64 HPHIVELLETYSSDGMLYMVFEFMDGADLCFEIVKRadaGFVYSEAVASHYMRQILEA---LRYCH--DNNIIHRDVKPH 138
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15222437 208 NILLDSEYNA---KLSDFGLAKDGPiGDKSHVSTRVmGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd14094 139 CVLLASKENSapvKLGGFGVAIQLG-ESGLVAGGRV-GTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGC 209
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
148-276 4.22e-09

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: 57.24  E-value: 4.22e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 148 LLVYEFMPRGSLENHLFRRGLYFQPLSWKLRLKVALgaAKGLAFLHssETRVIYRDFKTSNILLDSEY---NAKLSDFGL 224
Cdd:cd14198  84 ILILEYAAGGEIFNLCVPDLAEMVSENDIIRLIRQI--LEGVYYLH--QNNIVHLDLKPQNILLSSIYplgDIKIVDFGM 159
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 15222437 225 AKDgpIGDKSHVStRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14198 160 SRK--IGHACELR-EIMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTH 208
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
134-276 4.56e-09

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: 57.70  E-value: 4.56e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 134 LVKLIGYCLEDEHRLLVYEFMPRGSLENHLfrrGLYFQPLSW----KLRLKVALGAAKGLAFLHssetrviyRDFKTSNI 209
Cdd:cd05621 114 VVQLFCAFQDDKYLYMVMEYMPGGDLVNLM---SNYDVPEKWakfyTAEVVLALDAIHSMGLIH--------RDVKPDNM 182
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15222437 210 LLDSEYNAKLSDFGLAKDGPIGDKSHVSTRVmGTHGYAAPEYLAT----GHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd05621 183 LLDKYGHLKLADFGTCMKMDETGMVHCDTAV-GTPDYISPEVLKSqggdGYYGRECDWWSVGVFLFEMLVG 252
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
129-276 4.99e-09

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: 57.71  E-value: 4.99e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 129 FSHRHLVKLIGYCLEDEHRL-LVYEFMPRGSLENHLFRrglYFQPLSW----KLRLKVALGAAKGLAFLHssetrviyRD 203
Cdd:cd05622 129 FANSPWVVQLFYAFQDDRYLyMVMEYMPGGDLVNLMSN---YDVPEKWarfyTAEVVLALDAIHSMGFIH--------RD 197
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 204 FKTSNILLDSEYNAKLSDFG----LAKDGPIGDKSHVstrvmGTHGYAAPEYLAT----GHLTTKSDVYSFGVVLLELLS 275
Cdd:cd05622 198 VKPDNMLLDKSGHLKLADFGtcmkMNKEGMVRCDTAV-----GTPDYISPEVLKSqggdGYYGRECDWWSVGVFLYEMLV 272

                .
gi 15222437 276 G 276
Cdd:cd05622 273 G 273
PTK_Jak3_rpt1 cd14208
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is ...
74-276 6.56e-09

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; 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 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. It modulates the kinase activity of the C-terminal catalytic domain. Jaks 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 Jak3 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: 271110 [Multi-domain]  Cd Length: 260  Bit Score: 56.45  E-value: 6.56e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGwIDEKSLTASRPGTGLVIAVkklnQDGWQGH--QEWLAEVNYLGQFSHRHLVKLIGYCLEDEhRLLVY 151
Cdd:cd14208   7 LGKGSFTKIYRG-LRTDEEDDERCETEVLLKV----MDPTHGNcqESFLEAASIMSQISHKHLVLLHGVCVGKD-SIMVQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 152 EFMPRGSLENHLFRRGLYFQ-PLSWKlrLKVALGAAKGLAFLHssETRVIYRDFKTSNILLDSEYNA------KLSDFGL 224
Cdd:cd14208  81 EFVCHGALDLYLKKQQQKGPvAISWK--LQVVKQLAYALNYLE--DKQLVHGNVSAKKVLLSREGDKgsppfiKLSDPGV 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15222437 225 AKdgPIGDKSHVSTRVmgthGYAAPEYLATGH-LTTKSDVYSFGVVLLELLSG 276
Cdd:cd14208 157 SI--KVLDEELLAERI----PWVAPECLSDPQnLALEADKWGFGATLWEIFSG 203
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
71-276 8.20e-09

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: 56.58  E-value: 8.20e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  71 DSVLGEGGF----GCVfkgwidekSLTasrpgTGLVIAVKKLNQDGWQGHQEWLAEVNYLGQFS-HRHLVKLIGYCLEDE 145
Cdd:cd14174   7 DELLGEGAYakvqGCV--------SLQ-----NGKEYAVKIIEKNAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDT 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 146 HRLLVYEFMPRGSLENHLFRRGlYFQPlswKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYN---AKLSDF 222
Cdd:cd14174  74 RFYLVFEKLRGGSILAHIQKRK-HFNE---REASRVVRDIASALDFLHTKG--IAHRDLKPENILCESPDKvspVKICDF 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15222437 223 GLAKDGPIGDK-SHVSTRVM----GTHGYAAPEYLA--TGHLT---TKSDVYSFGVVLLELLSG 276
Cdd:cd14174 148 DLGSGVKLNSAcTPITTPELttpcGSAEYMAPEVVEvfTDEATfydKRCDLWSLGVILYIMLSG 211
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
68-349 8.34e-09

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


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 56.01  E-value: 8.34e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  68 FRPDSVLGEGGFGCVFKGwideksltaSRPGTGLVIAVKKLNQD---GWQ---GHQEWLAEVNYL----GQFSHRHLVKL 137
Cdd:cd14101   2 YTMGNLLGKGGFGTVYAG---------HRISDGLQVAIKQISRNrvqQWSklpGVNPVPNEVALLqsvgGGPGHRGVIRL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 138 IGYCLEDEHRLLVYEF-MPRGSLENHLFRRGlyfqPLSWKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEY- 215
Cdd:cd14101  73 LDWFEIPEGFLLVLERpQHCQDLFDYITERG----ALDESLARRFFKQVVEAVQHCHSKG--VVHRDIKDENILVDLRTg 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 216 NAKLSDFG---LAKDGPIGDKShvstrvmGTHGYAAPEYLAT-GHLTTKSDVYSFGVVLLELLSGRRAVDKnrpsgERNL 291
Cdd:cd14101 147 DIKLIDFGsgaTLKDSMYTDFD-------GTRVYSPPEWILYhQYHALPATVWSLGILLYDMVCGDIPFER-----DTDI 214
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15222437 292 VEwAKPYLvNKRkifrvIDNRLQDqysmeeackvatLSLRCLTTEIKLRPNMSEVVSH 349
Cdd:cd14101 215 LK-AKPSF-NKR-----VSNDCRS------------LIRSCLAYNPSDRPSLEQILLH 253
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
171-275 8.85e-09

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: 56.78  E-value: 8.85e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 171 QPLSWKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAKDgPIGDKSHVstrVMGTH----GY 246
Cdd:cd05106 207 WPLDLDDLLRFSSQVAQGMDFLASKN--CIHRDVAARNVLLTDGRVAKICDFGLARD-IMNDSNYV---VKGNArlpvKW 280
                        90       100
                ....*....|....*....|....*....
gi 15222437 247 AAPEYLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:cd05106 281 MAPESIFDCVYTVQSDVWSYGILLWEIFS 309
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
140-277 9.52e-09

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: 56.55  E-value: 9.52e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 140 YCLEDEHRL-LVYEFMPRGSLENHLFRRGLYFQPLSWKLRLK---VALGAAKGLAFLHssetrviyRDFKTSNILLDSEY 215
Cdd:cd05601  68 YAFQDSENLyLVMEYHPGGDLLSLLSRYDDIFEESMARFYLAelvLAIHSLHSMGYVH--------RDIKPENILIDRTG 139
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15222437 216 NAKLSDFG-LAKDGPigDKSHVSTRVMGTHGYAAPEYLAT------GHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd05601 140 HIKLADFGsAAKLSS--DKTVTSKMPVGTPDYIAPEVLTSmnggskGTYGVECDWWSLGIVAYEMLYGK 206
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
74-274 1.29e-08

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: 55.73  E-value: 1.29e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWIDEKSLTASRPGTGLVIAVKKLNQdgwqghQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEF 153
Cdd:cd14206   5 IGNGWFGKVILGEIFSDYTPAQVVVKELRVSAGPLEQ------RKFISEAQPYRSLQHPNILQCLGLCTETIPFLLIMEF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 154 MPRGSLENHLFRR----GLYFQPLSWKLRL--KVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAKD 227
Cdd:cd14206  79 CQLGDLKRYLRAQrkadGMTPDLPTRDLRTlqRMAYEITLGLLHLHKNN--YIHSDLALRNCLLTSDLTVRIGDYGLSHN 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15222437 228 GPIGDKSHVSTRVMGTHGYAAPEYLATGH-------LTTKSDVYSFGVVLLELL 274
Cdd:cd14206 157 NYKEDYYLTPDRLWIPLRWVAPELLDELHgnlivvdQSKESNVWSLGVTIWELF 210
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
151-275 1.54e-08

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR alpha is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR alpha forms homodimers or heterodimers with PDGFR beta, depending on the nature of the PDGF ligand. PDGF-AA, PDGF-AB, and PDGF-CC induce PDGFR alpha homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR alpha signaling is important in the formation of lung alveoli, intestinal villi, mesenchymal dermis, and hair follicles, as well as in the development of oligodendrocytes, retinal astrocytes, neural crest cells, and testicular cells. Aberrant PDGFR alpha expression is associated with some human cancers. Mutations in PDGFR alpha have been found within a subset of gastrointestinal stromal tumors (GISTs). An active fusion protein FIP1L1-PDGFR alpha, derived from interstitial deletion, is associated with idiopathic hypereosinophilic syndrome and chronic eosinophilic leukemia. The PDGFR alpha subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 56.19  E-value: 1.54e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 151 YEFMPRGSLENHLFRRGlyFQPLSWKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAKDgPI 230
Cdd:cd05105 214 YKGSNDSEVKNLLSDDG--SEGLTTLDLLSFTYQVARGMEFLASKN--CVHRDLAARNVLLAQGKIVKICDFGLARD-IM 288
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 15222437 231 GDKSHVST-RVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:cd05105 289 HDSNYVSKgSTFLPVKWMAPESIFDNLYTTLSDVWSYGILLWEIFS 334
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
74-276 1.88e-08

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: 55.21  E-value: 1.88e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKgwIDEKSltasrpgTGLVIAVKKLNQDGWQghqewLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEF 153
Cdd:cd13991  14 IGRGSFGEVHR--MEDKQ-------TGFQCAVKKVRLEVFR-----AEELMACAGLTSPRVVPLYGAVREGPWVNIFMDL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 154 MPRGSLENHLFRRGLyfqpLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSE-YNAKLSDFGLA---KDGP 229
Cdd:cd13991  80 KEGGSLGQLIKEQGC----LPEDRALHYLGQALEGLEYLHSR--KILHGDVKADNVLLSSDgSDAFLCDFGHAeclDPDG 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15222437 230 IGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd13991 154 LGKSLFTGDYIPGTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNG 200
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
74-276 2.15e-08

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: 54.70  E-value: 2.15e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGwiDEKSltasrpgTGLVIAVKKLNQDGWQGHQEWL---AEVNYLGQFSHRHLVKLIGYCLEDEHRLLV 150
Cdd:cd14073   9 LGKGTYGKVKLA--IERA-------TGREVAIKSIKKDKIEDEQDMVrirREIEIMSSLNHPHIIRIYEVFENKDKIVIV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 151 YEFMPRGSLENHLFRRglyfQPLSWKLRLKVALGAAKGLAFLHssETRVIYRDFKTSNILLDSEYNAKLSDFGLAKdgpI 230
Cdd:cd14073  80 MEYASGGELYDYISER----RRLPEREARRIFRQIVSAVHYCH--KNGVVHRDLKLENILLDQNGNAKIADFGLSN---L 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15222437 231 GDKSHVSTRVMGTHGYAAPEYL-ATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14073 151 YSKDKLLQTFCGSPLYASPEIVnGTPYQGPEVDCWSLGVLLYTLVYG 197
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
74-273 2.85e-08

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


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 54.65  E-value: 2.85e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKgwideksltASRPGTGLVIAVK--KLNQ-DGWQGHQEwlaEVNYLGQFSHRHLVKLIGYCLEDEHRLLV 150
Cdd:cd06646  17 VGSGTYGDVYK---------ARNLHTGELAAVKiiKLEPgDDFSLIQQ---EIFMVKECKHCNIVAYFGSYLSREKLWIC 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 151 YEFMPRGSLENHLFRRGlyfqPLSWKLRLKVALGAAKGLAFLHSSETrvIYRDFKTSNILLDSEYNAKLSDFGLAkdGPI 230
Cdd:cd06646  85 MEYCGGGSLQDIYHVTG----PLSELQIAYVCRETLQGLAYLHSKGK--MHRDIKGANILLTDNGDVKLADFGVA--AKI 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15222437 231 GDKSHVSTRVMGTHGYAAPEYLA---TGHLTTKSDVYSFGVVLLEL 273
Cdd:cd06646 157 TATIAKRKSFIGTPYWMAPEVAAvekNGGYNQLCDIWAVGITAIEL 202
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
74-273 3.11e-08

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: 54.68  E-value: 3.11e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQDgwqghQE-------WLAEVNYLGQFSHRHLVKLIGYC----- 141
Cdd:cd07865  20 IGQGTFGEVFK---------ARHRKTGQIVALKKVLME-----NEkegfpitALREIKILQLLKHENVVNLIEICrtkat 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 142 LEDEHR---LLVYEFMPR---GSLENHLFRrglyFQPLSWKLRLKVALgaaKGLAFLHSSetRVIYRDFKTSNILLDSEY 215
Cdd:cd07865  86 PYNRYKgsiYLVFEFCEHdlaGLLSNKNVK----FTLSEIKKVMKMLL---NGLYYIHRN--KILHRDMKAANILITKDG 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15222437 216 NAKLSDFGLAK--DGPIGDKSHVSTRVMGTHGYAAPE-YLATGHLTTKSDVYSFGVVLLEL 273
Cdd:cd07865 157 VLKLADFGLARafSLAKNSQPNRYTNRVVTLWYRPPElLLGERDYGPPIDMWGAGCIMAEM 217
PTK_Jak2_rpt1 cd05078
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely ...
74-276 3.45e-08

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: 54.18  E-value: 3.45e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWIDEKSLTASRPGTGLVIAVkkLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEF 153
Cdd:cd05078   7 LGQGTFTKIFKGIRREVGDYGQLHETEVLLKV--LDKAHRNYSESFFEAASMMSQLSHKHLVLNYGVCVCGDENILVQEY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 154 MPRGSLENHLfRRGLYFQPLSWKLRLkvalgaAKGLAF-LHSSETR-VIYRDFKTSNILLDSEYN--------AKLSDFG 223
Cdd:cd05078  85 VKFGSLDTYL-KKNKNCINILWKLEV------AKQLAWaMHFLEEKtLVHGNVCAKNILLIREEDrktgnppfIKLSDPG 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15222437 224 LAKDgpIGDKSHVSTRVmgthGYAAPEYLATG-HLTTKSDVYSFGVVLLELLSG 276
Cdd:cd05078 158 ISIT--VLPKDILLERI----PWVPPECIENPkNLSLATDKWSFGTTLWEICSG 205
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
63-277 3.56e-08

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 54.77  E-value: 3.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437   63 SATRNFRP-DSVLGEGGFGCVFKGwIDEKsltasrpgTGLVIAVKKLNQDGWQG--------------HQEWLAEVNYLG 127
Cdd:PTZ00024   5 SISERYIQkGAHLGEGTYGKVEKA-YDTL--------TGKIVAIKKVKIIEISNdvtkdrqlvgmcgiHFTTLRELKIMN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  128 QFSHRHLVKLIGYCLEDEHRLLVYEFMpRGSLENhLFRRGLYFQPLSWKLRLKVALgaaKGLAFLHSSEtrVIYRDFKTS 207
Cdd:PTZ00024  76 EIKHENIMGLVDVYVEGDFINLVMDIM-ASDLKK-VVDRKIRLTESQVKCILLQIL---NGLNVLHKWY--FMHRDLSPA 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  208 NILLDSEYNAKLSDFGLAK--------DGPIGDKSHVSTRVMG----THGYAAPEYLATGHLTTKS-DVYSFGVVLLELL 274
Cdd:PTZ00024 149 NIFINSKGICKIADFGLARrygyppysDTLSKDETMQRREEMTskvvTLWYRAPELLMGAEKYHFAvDMWSVGCIFAELL 228

                 ...
gi 15222437  275 SGR 277
Cdd:PTZ00024 229 TGK 231
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
122-270 3.74e-08

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


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 54.20  E-value: 3.74e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 122 EVNYLGQFSHRHLVKLIgYCLED---EHRLLVYEFMPRGSLENHLFRRGL-------YFQPLswklrlkvalgaAKGLAF 191
Cdd:cd14199  75 EIAILKKLDHPNVVKLV-EVLDDpseDHLYMVFELVKQGPVMEVPTLKPLsedqarfYFQDL------------IKGIEY 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 192 LHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPIGDKSHVSTrvMGTHGYAAPEYLATGH--LTTKS-DVYSFGV 268
Cdd:cd14199 142 LHYQ--KIIHRDVKPSNLLVGEDGHIKIADFGVSNEFEGSDALLTNT--VGTPAFMAPETLSETRkiFSGKAlDVWAMGV 217

                ..
gi 15222437 269 VL 270
Cdd:cd14199 218 TL 219
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
66-273 3.76e-08

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: 54.29  E-value: 3.76e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  66 RNFRPDSVLGEGGFGCVFKGWIDEKSLTASrpgtGLVIAVKKLNQDGWQGHQEwlaEVNYLGQFSHRHLVKLIGyCLEDE 145
Cdd:cd14030  25 RFLKFDIEIGRGSFKTVYKGLDTETTVEVA----WCELQDRKLSKSERQRFKE---EAGMLKGLQHPNIVRFYD-SWEST 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 146 HR-----LLVYEFMPRGSLENHLFRrglyFQPLSWKLRLKVALGAAKGLAFLHSSETRVIYRDFKTSNILLDSEYNA-KL 219
Cdd:cd14030  97 VKgkkciVLVTELMTSGTLKTYLKR----FKVMKIKVLRSWCRQILKGLQFLHTRTPPIIHRDLKCDNIFITGPTGSvKI 172
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15222437 220 SDFGLAKDgpigDKSHVSTRVMGTHGYAAPEYLATGHlTTKSDVYSFGVVLLEL 273
Cdd:cd14030 173 GDLGLATL----KRASFAKSVIGTPEFMAPEMYEEKY-DESVDVYAFGMCMLEM 221
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
187-277 4.35e-08

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: 54.67  E-value: 4.35e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 187 KGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPIGDKSHVSTRvmgthGYAAPE-YLATGHLTTKSDVYS 265
Cdd:cd07878 129 RGLKYIHSAG--IIHRDLKPSNVAVNEDCELRILDFGLARQADDEMTGYVATR-----WYRAPEiMLNWMHYNQTVDIWS 201
                        90
                ....*....|..
gi 15222437 266 FGVVLLELLSGR 277
Cdd:cd07878 202 VGCIMAELLKGK 213
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
63-276 4.40e-08

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: 53.85  E-value: 4.40e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  63 SATRNFRPDSVLGEGGFGCVFKgwIDEKSltasrpgTGLVIAVKKLNQDGWQGHQEWLA-EVNYLGQFSHRHLVKLIGYC 141
Cdd:cd14183   3 SISERYKVGRTIGDGNFAVVKE--CVERS-------TGREYALKIINKSKCRGKEHMIQnEVSILRRVKHPNIVLLIEEM 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 142 LEDEHRLLVYEFMPRGSLENHLFRRGLYFQPLSWKLRLKVAlgaaKGLAFLHSseTRVIYRDFKTSNILL----DSEYNA 217
Cdd:cd14183  74 DMPTELYLVMELVKGGDLFDAITSTNKYTERDASGMLYNLA----SAIKYLHS--LNIVHRDIKPENLLVyehqDGSKSL 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15222437 218 KLSDFGLAK--DGPIgdkshvsTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14183 148 KLGDFGLATvvDGPL-------YTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCG 201
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
71-277 4.47e-08

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: 54.23  E-value: 4.47e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  71 DSVLGEGGFG----CVFKGwideksltasrpgTGLVIAVKKLNQDgWQGHQEwlaeVNYLGQF-SHRHLVKLIGyCLEDE 145
Cdd:cd14092  11 EEALGDGSFSvcrkCVHKK-------------TGQEFAVKIVSRR-LDTSRE----VQLLRLCqGHPNIVKLHE-VFQDE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 146 -HRLLVYEFMPRGSLENHLFRRGLYFQPLSWKLRLKVAlgaaKGLAFLHSSetRVIYRDFKTSNILL-DSEYNA--KLSD 221
Cdd:cd14092  72 lHTYLVMELLRGGELLERIRKKKRFTESEASRIMRQLV----SAVSFMHSK--GVVHRDLKPENLLFtDEDDDAeiKIVD 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 222 FGLAKDGPigDKSHVSTRVMGTHgYAAPEYLATGHLTT----KSDVYSFGVVLLELLSGR 277
Cdd:cd14092 146 FGFARLKP--ENQPLKTPCFTLP-YAAPEVLKQALSTQgydeSCDLWSLGVILYTMLSGQ 202
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
99-276 4.62e-08

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: 54.22  E-value: 4.62e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  99 TGLVIAVKKLNQDGwQGHQEW---LAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEFMPRGS----LENHlFRRGLYFQ 171
Cdd:cd08216  24 TNTLVAVKKINLES-DSKEDLkflQQEILTSRQLQHPNILPYVTSFVVDNDLYVVTPLMAYGScrdlLKTH-FPEGLPEL 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 172 PLSWKLRlkvalGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLA--------KDGPIGDKSHVSTRVMGt 243
Cdd:cd08216 102 AIAFILR-----DVLNALEYIHSKG--YIHRSVKASHILISGDGKVVLSGLRYAysmvkhgkRQRVVHDFPKSSEKNLP- 173
                       170       180       190
                ....*....|....*....|....*....|....*
gi 15222437 244 hgYAAPEYLATGHL--TTKSDVYSFGVVLLELLSG 276
Cdd:cd08216 174 --WLSPEVLQQNLLgyNEKSDIYSVGITACELANG 206
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
74-276 4.62e-08

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: 53.97  E-value: 4.62e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQDGW--QGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVY 151
Cdd:cd14086   9 LGKGAFSVVRR---------CVQKSTGQEFAAKIINTKKLsaRDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 152 EFMPRGSLENHLFRRGLY---------FQPLSwklrlkvalgaakglAFLHSSETRVIYRDFKTSNILLDS-EYNA--KL 219
Cdd:cd14086  80 DLVTGGELFEDIVAREFYseadashciQQILE---------------SVNHCHQNGIVHRDLKPENLLLASkSKGAavKL 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15222437 220 SDFGLAKDGPIGDKSHVStrVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14086 145 ADFGLAIEVQGDQQAWFG--FAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVG 199
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
150-274 5.08e-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: 54.10  E-value: 5.08e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 150 VYEFMPRGSLENHLFRRglyfQPlSWKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDS---EYNAKLSDFGLAK 226
Cdd:cd13977 113 VMEFCDGGDMNEYLLSR----RP-DRQTNTSFMLQLSSALAFLHRNQ--IVHRDLKPDNILISHkrgEPILKVADFGLSK 185
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15222437 227 ----DGPIGDKS-----HVSTRVMGTHGYAAPEyLATGHLTTKSDVYSFGVVLLELL 274
Cdd:cd13977 186 vcsgSGLNPEEPanvnkHFLSSACGSDFYMAPE-VWEGHYTAKADIFALGIIIWAMV 241
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
187-277 6.25e-08

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: 54.19  E-value: 6.25e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 187 KGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPIGDKSHVSTRvmgthGYAAPEY-LATGHLTTKSDVYS 265
Cdd:cd07880 129 KGLKYIHAAG--IIHRDLKPGNLAVNEDCELKILDFGLARQTDSEMTGYVVTR-----WYRAPEViLNWMHYTQTVDIWS 201
                        90
                ....*....|..
gi 15222437 266 FGVVLLELLSGR 277
Cdd:cd07880 202 VGCIMAEMLTGK 213
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
130-276 6.29e-08

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: 53.45  E-value: 6.29e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 130 SHRHLVKLIG-Y--------CLedehrLLVYEFMPRGSLENHLFRRGLyfQPLSWKLRLKVALGAAKGLAFLHSseTRVI 200
Cdd:cd14089  52 GCPHIVRIIDvYentyqgrkCL-----LVVMECMEGGELFSRIQERAD--SAFTEREAAEIMRQIGSAVAHLHS--MNIA 122
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15222437 201 YRDFKTSNILL-DSEYNA--KLSDFGLAKDgPIGDKShVSTRVMgTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14089 123 HRDLKPENLLYsSKGPNAilKLTDFGFAKE-TTTKKS-LQTPCY-TPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCG 198
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
122-282 6.84e-08

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 54.74  E-value: 6.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437   122 EVNYLGQFSHRHLVKLIGYCLEDEHRLL--VYEFMPRGSLENHLFRRGLYFQPLSWKLRLKVALGAAKGLAFLHS----- 194
Cdd:PTZ00266   62 EVNVMRELKHKNIVRYIDRFLNKANQKLyiLMEFCDAGDLSRNIQKCYKMFGKIEEHAIVDITRQLLHALAYCHNlkdgp 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437   195 SETRVIYRDFKTSNILLDSEYN-----------------AKLSDFGLAKDGPIGDKSHvstRVMGTHGYAAPEYL--ATG 255
Cdd:PTZ00266  142 NGERVLHRDLKPQNIFLSTGIRhigkitaqannlngrpiAKIGDFGLSKNIGIESMAH---SCVGTPYYWSPELLlhETK 218
                         170       180
                  ....*....|....*....|....*..
gi 15222437   256 HLTTKSDVYSFGVVLLELLSGRRAVDK 282
Cdd:PTZ00266  219 SYDDKSDMWALGCIIYELCSGKTPFHK 245
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
74-277 7.41e-08

Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 53.65  E-value: 7.41e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGwiDEKSltasrpgTGLVIAVKKLNQDGWQGHQE-WLAEVNYLGQFSHRHLVKLigYCLEDE----HRL 148
Cdd:cd13988   1 LGQGATANVFRG--RHKK-------TGDLYAVKVFNNLSFMRPLDvQMREFEVLKKLNHKNIVKL--FAIEEElttrHKV 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 LVYEFMPRGSLENHLFR-RGLYFQPLSWKLRLKVALGAakGLAFLHssETRVIYRDFKTSNILL----DSEYNAKLSDFG 223
Cdd:cd13988  70 LVMELCPCGSLYTVLEEpSNAYGLPESEFLIVLRDVVA--GMNHLR--ENGIVHRDIKPGNIMRvigeDGQSVYKLTDFG 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15222437 224 LAKDgpIGDKSHVSTrVMGTHGYAAPEYLATGHL--------TTKSDVYSFGVVLLELLSGR 277
Cdd:cd13988 146 AARE--LEDDEQFVS-LYGTEEYLHPDMYERAVLrkdhqkkyGATVDLWSIGVTFYHAATGS 204
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
149-280 1.13e-07

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1a, also called Activin receptor-Like Kinase 3 (ALK3), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Germline mutations in BMPR1a are associated with an increased risk to Juvenile Polyposis Syndrome, a hamartomatous disorder that may lead to gastrointestinal cancer. BMPR1a may also play an indirect role in the development of hematopoietic stem cells (HSCs) as osteoblasts are a major component of the HSC niche within the bone marrow. BMPR1a belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1a, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 52.74  E-value: 1.13e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 LVYEFMPRGSLENHLfrrglYFQPLSWKLRLKVALGAAKGLAFLHSS------ETRVIYRDFKTSNILLDSEYNAKLSDF 222
Cdd:cd14220  70 LITDYHENGSLYDFL-----KCTTLDTRALLKLAYSAACGLCHLHTEiygtqgKPAIAHRDLKSKNILIKKNGTCCIADL 144
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15222437 223 GLAKDGPiGDKSHV----STRvMGTHGYAAPEY----LATGHLTT--KSDVYSFGVVLLELlsGRRAV 280
Cdd:cd14220 145 GLAVKFN-SDTNEVdvplNTR-VGTKRYMAPEVldesLNKNHFQAyiMADIYSFGLIIWEM--ARRCV 208
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
114-269 1.17e-07

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: 52.58  E-value: 1.17e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 114 QGHQEwlaeVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEFMPRGSLENHLFRRGLYFQPlSWKLRLKVALgaaKGLAFLH 193
Cdd:cd14107  44 RAFQE----RDILARLSHRRLTCLLDQFETRKTLILILELCSSEELLDRLFLKGVVTEA-EVKLYIQQVL---EGIGYLH 115
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15222437 194 SSEtrVIYRDFKTSNILLDS--EYNAKLSDFGLAKDgpiGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVV 269
Cdd:cd14107 116 GMN--ILHLDIKPDNILMVSptREDIKICDFGFAQE---ITPSEHQFSKYGSPEFVAPEIVHQEPVSAATDIWALGVI 188
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
187-277 1.30e-07

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: 52.86  E-value: 1.30e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 187 KGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAK----DGP--IGDKSHVSTRvmgthGYAAPEYLAT--GHLT 258
Cdd:cd07859 114 RALKYIHTAN--VFHRDLKPKNILANADCKLKICDFGLARvafnDTPtaIFWTDYVATR-----WYRAPELCGSffSKYT 186
                        90
                ....*....|....*....
gi 15222437 259 TKSDVYSFGVVLLELLSGR 277
Cdd:cd07859 187 PAIDIWSIGCIFAEVLTGK 205
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
187-277 1.92e-07

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: 52.60  E-value: 1.92e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 187 KGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPIGDKSHVSTRvmgthGYAAPEY-LATGHLTTKSDVYS 265
Cdd:cd07879 128 CGLKYIHSAG--IIHRDLKPGNLAVNEDCELKILDFGLARHADAEMTGYVVTR-----WYRAPEViLNWMHYNQTVDIWS 200
                        90
                ....*....|..
gi 15222437 266 FGVVLLELLSGR 277
Cdd:cd07879 201 VGCIMAEMLTGK 212
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
186-275 1.98e-07

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


Pssm-ID: 270682 [Multi-domain]  Cd Length: 375  Bit Score: 52.60  E-value: 1.98e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 186 AKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAKDgPIGDKSHVstrVMGTH----GYAAPEYLATGHLTTKS 261
Cdd:cd05104 224 AKGMEFLASKN--CIHRDLAARNILLTHGRITKICDFGLARD-IRNDSNYV---VKGNArlpvKWMAPESIFECVYTFES 297
                        90
                ....*....|....
gi 15222437 262 DVYSFGVVLLELLS 275
Cdd:cd05104 298 DVWSYGILLWEIFS 311
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
74-271 2.12e-07

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: 51.95  E-value: 2.12e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQD--GWQGHQEWLAEV---NYLGQfsHRHLVKLIGYCLEDEHRL 148
Cdd:cd14138  13 IGSGEFGSVFK---------CVKRLDGCIYAIKRSKKPlaGSVDEQNALREVyahAVLGQ--HSHVVRYYSAWAEDDHML 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 LVYEFMPRGSLENHL---FRRGLYFQPLSWK-LRLKValgaAKGLAFLHSseTRVIYRDFKTSNILLDSEY---NAKLSD 221
Cdd:cd14138  82 IQNEYCNGGSLADAIsenYRIMSYFTEPELKdLLLQV----ARGLKYIHS--MSLVHMDIKPSNIFISRTSipnAASEEG 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15222437 222 FGLAKDGP-----IGDKSHVsTRVM------GTHGYAAPEYLATG--HLtTKSDVYSFGVVLL 271
Cdd:cd14138 156 DEDEWASNkvifkIGDLGHV-TRVSspqveeGDSRFLANEVLQENytHL-PKADIFALALTVV 216
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
121-277 2.27e-07

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


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 52.32  E-value: 2.27e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 121 AEVNYLGQFSHRHLVKLIgYCLEDEHRL-LVYEFMPRGSLENHLFRRGLYFQPLS--WKLRLKVALGAAKGLAFLHsset 197
Cdd:cd05626  50 AERDILAEADNEWVVKLY-YSFQDKDNLyFVMDYIPGGDMMSLLIRMEVFPEVLArfYIAELTLAIESVHKMGFIH---- 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 198 rviyRDFKTSNILLDSEYNAKLSDFGL--------------------------------AKDGPIGD----------KSH 235
Cdd:cd05626 125 ----RDIKPDNILIDLDGHIKLTDFGLctgfrwthnskyyqkgshirqdsmepsdlwddVSNCRCGDrlktleqratKQH 200
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 15222437 236 ---VSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd05626 201 qrcLAHSLVGTPNYIAPEVLLRKGYTQLCDWWSVGVILFEMLVGQ 245
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
74-279 2.58e-07

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: 52.00  E-value: 2.58e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGwideKSLTasrpgTGLVIAVKKLNQDGWQGHQ-EWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYE 152
Cdd:cd07869  13 LGEGSYATVYKG----KSKV-----NGKLVALKVIRLQEEEGTPfTAIREASLLKGLKHANIVLLHDIIHTKETLTLVFE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMpRGSLENHLFRRGLYFQPLSWKLRLKVALgaaKGLAFLHssETRVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPIgd 232
Cdd:cd07869  84 YV-HTDLCQYMDKHPGGLHPENVKLFLFQLL---RGLSYIH--QRYILHRDLKPQNLLISDTGELKLADFGLARAKSV-- 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15222437 233 KSHVSTRVMGTHGYAAPE-YLATGHLTTKSDVYSFGVVLLELLSGRRA 279
Cdd:cd07869 156 PSHTYSNEVVTLWYRPPDvLLGSTEYSTCLDMWGVGCIFVEMIQGVAA 203
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
74-294 2.59e-07

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


Pssm-ID: 270915 [Multi-domain]  Cd Length: 318  Bit Score: 52.05  E-value: 2.59e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKGWIDEKSLtasrPGTGLVIAVKKLNQDGwqGHQEWLAE----------VNYLGQFSHRHLVKligycLE 143
Cdd:cd14013   3 LGEGGFGTVYKGSLLQKDP----GGEKRRVVLKKAKEYG--EVEIWMNErvrracpsscAEFVGAFLDTTSKK-----FT 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 144 DEHRLLVYEF---------MPRGS----LENHLFRRGLYfQPLSWKLRLKVALGAAK----GLAFLHSseTRVIYRDFKT 206
Cdd:cd14013  72 KPSLWLVWKYegdatladlMQGKEfpynLEPIIFGRVLI-PPRGPKRENVIIKSIMRqilvALRKLHS--TGIVHRDVKP 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 207 SNILLDSEY-NAKLSDFGLAKDGPIGdKSHVSTRVMGTHGYAAPEYLATGHLTTKS----------------------DV 263
Cdd:cd14013 149 QNIIVSEGDgQFKIIDLGAAADLRIG-INYIPKEFLLDPRYAPPEQYIMSTQTPSAppapvaaalspvlwqmnlpdrfDM 227
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 15222437 264 YSFGVVLLELL-------SGRRAVDKNRPSGERNLVEW 294
Cdd:cd14013 228 YSAGVILLQMAfpnlrsdSNLIAFNRQLKQCDYDLNAW 265
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
73-277 2.67e-07

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: 51.92  E-value: 2.67e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKGWIDEksltasrpgTGLVIAVKKL--NQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLV 150
Cdd:cd07848   8 VVGEGAYGVVLKCRHKE---------TKEIVAIKKFkdSEENEEVKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 151 YEFMPRGSLEnhlFRRGLYFQPLSWKLRLKVaLGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPI 230
Cdd:cd07848  79 FEYVEKNMLE---LLEEMPNGVPPEKVRSYI-YQLIKAIHWCHKND--IVHRDIKPENLLISHNDVLKLCDFGFARNLSE 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15222437 231 GDKSHVsTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd07848 153 GSNANY-TEYVATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQ 198
pknD PRK13184
serine/threonine-protein kinase PknD;
74-284 2.84e-07

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 52.85  E-value: 2.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437   74 LGEGGFGCVFKGWideksltasRPGTGLVIAVKKLNQDGWQG---HQEWLAEVNYLGQFSHRHLVKLIGYCLEDEhrlLV 150
Cdd:PRK13184  10 IGKGGMGEVYLAY---------DPVCSRRVALKKIREDLSENpllKKRFLREAKIAADLIHPGIVPVYSICSDGD---PV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  151 YEFMP--RGSLENHLFRRGLYFQPLSWKLRLKVALGA--------AKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLS 220
Cdd:PRK13184  78 YYTMPyiEGYTLKSLLKSVWQKESLSKELAEKTSVGAflsifhkiCATIEYVHSKG--VLHRDLKPDNILLGLFGEVVIL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  221 DFGLAK------------DGPIGDKSH----VSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLS--------- 275
Cdd:PRK13184 156 DWGAAIfkkleeedlldiDVDERNICYssmtIPGKIVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTlsfpyrrkk 235

                 ....*....
gi 15222437  276 GRRAVDKNR 284
Cdd:PRK13184 236 GRKISYRDV 244
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
120-285 3.01e-07

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 51.90  E-value: 3.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  120 LAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEFMPRGSLENHLFRRGLYFQPLSWKLRLKVALgaakglAFLHSSETRV 199
Cdd:PTZ00426  79 FSERKILNYINHPFCVNLYGSFKDESYLYLVLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVL------IFEYLQSLNI 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  200 IYRDFKTSNILLDSEYNAKLSDFGLAKDgpigdkshVSTR---VMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:PTZ00426 153 VYRDLKPENLLLDKDGFIKMTDFGFAKV--------VDTRtytLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVG 224

                 ....*....
gi 15222437  277 RRAVDKNRP 285
Cdd:PTZ00426 225 CPPFYANEP 233
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
67-368 3.63e-07

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: 51.60  E-value: 3.63e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGCVfkgwideksLTASRPGTGLVIAVKKLNQ-DGWQGHQ--EWLAEVNYLGQFSHRHLVKLIgYCLE 143
Cdd:cd05627   3 DFESLKVIGRGAFGEV---------RLVQKKDTGHIYAMKILRKaDMLEKEQvaHIRAERDILVEADGAWVVKMF-YSFQ 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 144 DEHRL-LVYEFMPRGSLENHLFRRGLYFQPLS--WKLRLKVALGAAKGLAFLHssetrviyRDFKTSNILLDSEYNAKLS 220
Cdd:cd05627  73 DKRNLyLIMEFLPGGDMMTLLMKKDTLSEEATqfYIAETVLAIDAIHQLGFIH--------RDIKPDNLLLDAKGHVKLS 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 221 DFGLA---------------KDGPIGD------------------KSHVSTRVMGTHGYAAPE-YLATGHlTTKSDVYSF 266
Cdd:cd05627 145 DFGLCtglkkahrtefyrnlTHNPPSDfsfqnmnskrkaetwkknRRQLAYSTVGTPDYIAPEvFMQTGY-NKLCDWWSL 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 267 GVVLLELLSGRRAVDKNRPSGE-RNLVEWaKPYLVNKRKIfrVIDNRLQD---QYSMEEACKVATLSLRclttEIKLRPN 342
Cdd:cd05627 224 GVIMYEMLIGYPPFCSETPQETyRKVMNW-KETLVFPPEV--PISEKAKDlilRFCTDAENRIGSNGVE----EIKSHPF 296
                       330       340
                ....*....|....*....|....*.
gi 15222437 343 MSEVvsHLEHIQSLNAAIGGNMDKTD 368
Cdd:cd05627 297 FEGV--DWEHIRERPAAIPIEIKSID 320
PTK_Tyk2_rpt1 cd05076
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; Tyk2 is ...
126-350 3.67e-07

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; 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 domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. The Tyk2 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: 270661 [Multi-domain]  Cd Length: 273  Bit Score: 51.06  E-value: 3.67e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 126 LGQFSHRHLVKLIGYCLEDEHRLLVYEFMPRGSLENHLFRRGLYFqPLSWKlrLKVALGAAKGLAFLHSSetRVIYRDFK 205
Cdd:cd05076  69 MSQVSHTHLVFVHGVCVRGSENIMVEEFVEHGPLDVWLRKEKGHV-PMAWK--FVVARQLASALSYLENK--NLVHGNVC 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 206 TSNILLDS---EYNA----KLSDFGLAKdGPIGDKSHVStRVmgthGYAAPEYLATGH-LTTKSDVYSFGVVLLELlsgr 277
Cdd:cd05076 144 AKNILLARlglEEGTspfiKLSDPGVGL-GVLSREERVE-RI----PWIAPECVPGGNsLSTAADKWGFGATLLEI---- 213
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15222437 278 rAVDKNRPSGERNLVEWAKPYlvnkrkifrvidnrlQDQYSMEE-ACK-VATLSLRCLTTEIKLRPNMSEVVSHL 350
Cdd:cd05076 214 -CFNGEAPLQSRTPSEKERFY---------------QRQHRLPEpSCPeLATLISQCLTYEPTQRPSFRTILRDL 272
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
68-276 3.93e-07

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: 51.57  E-value: 3.93e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  68 FRPDSVLGEGGFGCVFkgwidekslTASRPGTGLVIAVKKLNQDgwqgHQEWLAEVNY-------LGQFSHRHLVKLIgY 140
Cdd:cd05600  13 FQILTQVGQGGYGSVF---------LARKKDTGEICALKIMKKK----VLFKLNEVNHvlterdiLTTTNSPWLVKLL-Y 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 141 CLED-EHRLLVYEFMPRGSLENHLFRRGL--------YFqplswkLRLKVALGAAKGLAFLHssetrviyRDFKTSNILL 211
Cdd:cd05600  79 AFQDpENVYLAMEYVPGGDFRTLLNNSGIlseeharfYI------AEMFAAISSLHQLGYIH--------RDLKPENFLI 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 212 DSEYNAKLSDFGLA-------------------KDGPIGDKSHVSTR----------------VMGTHGYAAPEYLATGH 256
Cdd:cd05600 145 DSSGHIKLTDFGLAsgtlspkkiesmkirleevKNTAFLELTAKERRniyramrkedqnyansVVGSPDYMAPEVLRGEG 224
                       250       260
                ....*....|....*....|
gi 15222437 257 LTTKSDVYSFGVVLLELLSG 276
Cdd:cd05600 225 YDLTVDYWSLGCILFECLVG 244
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
72-276 4.17e-07

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: 50.72  E-value: 4.17e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  72 SVLGEGGFGCVFKGwideksltaSRPGTGLVIAVKKLNQD-----GWQGHQEWLAEVNYLGQF--SHRHLVKLIGYCLED 144
Cdd:cd14102   6 SVLGSGGFGTVYAG---------SRIADGLPVAVKHVVKErvtewGTLNGVMVPLEIVLLKKVgsGFRGVIKLLDWYERP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 145 EHRLLVyefMPRGSLENHLF----RRGLYFQPLSWKLRLKVaLGAAKglaflHSSETRVIYRDFKTSNILLDSEYNA-KL 219
Cdd:cd14102  77 DGFLIV---MERPEPVKDLFdfitEKGALDEDTARGFFRQV-LEAVR-----HCYSCGVVHRDIKDENLLVDLRTGElKL 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15222437 220 SDFG---LAKDGpigdkshVSTRVMGTHGYAAPEYLATGHLTTKS-DVYSFGVVLLELLSG 276
Cdd:cd14102 148 IDFGsgaLLKDT-------VYTDFDGTRVYSPPEWIRYHRYHGRSaTVWSLGVLLYDMVCG 201
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
61-276 4.70e-07

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors including homeodomain proteins (Nkx and HOX families), Smad1-4, Pax6, c-Myb, AML1, the histone acetyltransferase p300, and the tumor repressor p53, among others. It regulates gene transcription during development and in DNA damage response (DDR), and mediates cell processes such as apoptosis, survival, differentiation, and proliferation. HIPK2 mediates apoptosis by phosphorylating and activating p53 during DDR, resulting in the activation of apoptotic genes. In the absence of p53, HIPK2 targets the anti-apoptotic corepressor C-terminal binding protein (CtBP), leading to CtBP's degradation and the promotion of apoptosis. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 51.24  E-value: 4.70e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  61 LKSATRNFRPDSVLGEGGFGCVFKGWideksltasRPGTGLVIAVKKLNQDGWQGHQEWLaEVNYLGQFSHR-----HLV 135
Cdd:cd14227  10 LCSMTNTYEVLEFLGRGTFGQVVKCW---------KRGTNEIVAIKILKNHPSYARQGQI-EVSILARLSTEsaddyNFV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 136 KLIGYCLEDEHRLLVYEFmprgsLENHL--FRRGLYFQPLSWKLRLKVALGAAKGLAFLHSseTRVIYRDFKTSNILL-- 211
Cdd:cd14227  80 RAYECFQHKNHTCLVFEM-----LEQNLydFLKQNKFSPLPLKYIRPILQQVATALMKLKS--LGLIHADLKPENIMLvd 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15222437 212 --DSEYNAKLSDFGLAkdgpigdkSHVSTRVMGTH----GYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14227 153 psRQPYRVKVIDFGSA--------SHVSKAVCSTYlqsrYYRAPEIILGLPFCEAIDMWSLGCVIAELFLG 215
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
121-277 5.25e-07

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: 51.20  E-value: 5.25e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 121 AEVNYLGQFSHRHLVKLIgYCLEDEHRL-LVYEFMPRGSLENHLFRRGLYFQPLS--WKLRLKVALGAAKGLAFLHsset 197
Cdd:cd05625  50 AERDILAEADNEWVVRLY-YSFQDKDNLyFVMDYIPGGDMMSLLIRMGVFPEDLArfYIAELTCAVESVHKMGFIH---- 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 198 rviyRDFKTSNILLDSEYNAKLSDFGL--------------AKDGPIGDKSHVSTR------------------------ 239
Cdd:cd05625 125 ----RDIKPDNILIDRDGHIKLTDFGLctgfrwthdskyyqSGDHLRQDSMDFSNEwgdpencrcgdrlkplerraarqh 200
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 15222437 240 -------VMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd05625 201 qrclahsLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQ 245
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
129-275 5.71e-07

Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. ILK contains N-terminal ankyrin repeats, a Pleckstrin Homology (PH) domain, and a C-terminal pseudokinase domain. It is a component of the IPP (ILK/PINCH/Parvin) complex that couples beta integrins to the actin cytoskeleton, and plays important roles in cell adhesion, spreading, invasion, and migration. ILK was initially thought to be an active kinase despite the lack of key conserved residues because of in vitro studies showing that it can phosphorylate certain protein substrates. However, in vivo experiments in Caenorhabditis elegans, Drosophila melanogaster, and mice (ILK-null and knock-in) proved that ILK is not an active kinase. In addition to actin cytoskeleton regulation, ILK also influences the microtubule network and mitotic spindle orientation. The pseudokinase domain of ILK binds several adaptor proteins including the parvins and paxillin. The ILK 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: 270959 [Multi-domain]  Cd Length: 251  Bit Score: 50.56  E-value: 5.71e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 129 FSHRHLVKLIGYCLEDEHRLLVYEFMPRGSLENHLFRRGLYFQPLSWKLrlKVALGAAKGLAFLHSSEtRVIYRDFKTS- 207
Cdd:cd14057  49 FSHPNVLPVLGACNSPPNLVVISQYMPYGSLYNVLHEGTGVVVDQSQAV--KFALDIARGMAFLHTLE-PLIPRHHLNSk 125
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15222437 208 NILLDSEYNAKLSdfglakdgpIGDK--SHVSTRVMGTHGYAAPEYLATGH--LTTKS-DVYSFGVVLLELLS 275
Cdd:cd14057 126 HVMIDEDMTARIN---------MADVkfSFQEPGKMYNPAWMAPEALQKKPedINRRSaDMWSFAILLWELVT 189
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
186-275 6.31e-07

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


Pssm-ID: 133238 [Multi-domain]  Cd Length: 401  Bit Score: 51.16  E-value: 6.31e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 186 AKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAKDgPIGDKSHVST-RVMGTHGYAAPEYLATGHLTTKSDVY 264
Cdd:cd05107 249 ANGMEFLASKN--CVHRDLAARNVLICEGKLVKICDFGLARD-IMRDSNYISKgSTFLPLKWMAPESIFNNLYTTLSDVW 325
                        90
                ....*....|.
gi 15222437 265 SFGVVLLELLS 275
Cdd:cd05107 326 SFGILLWEIFT 336
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
186-279 7.86e-07

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: 50.13  E-value: 7.86e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 186 AKGLAFLHssETRVIYRDFKTSNILLDSEYNAKLSDFGLAKdgPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYS 265
Cdd:cd08223 112 AMALQYMH--ERNILHRDLKTQNIFLTKSNIIKVGDLGIAR--VLESSSDMATTLIGTPYYMSPELFSNKPYNHKSDVWA 187
                        90
                ....*....|....
gi 15222437 266 FGVVLLELLSGRRA 279
Cdd:cd08223 188 LGCCVYEMATLKHA 201
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
120-277 8.22e-07

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: 50.31  E-value: 8.22e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 120 LAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEFMPRGSLeNHLFRRglyfQPLSwklRLKVAlgAAK--------GLAF 191
Cdd:cd05574  49 LTEREILATLDHPFLPTLYASFQTSTHLCFVMDYCPGGEL-FRLLQK----QPGK---RLPEE--VARfyaaevllALEY 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 192 LHSseTRVIYRDFKTSNILLDSEYNAKLSDFGLAK-----DGPIGDKSHVSTRVM----------------------GTH 244
Cdd:cd05574 119 LHL--LGFVYRDLKPENILLHESGHIMLTDFDLSKqssvtPPPVRKSLRKGSRRSsvksieketfvaepsarsnsfvGTE 196
                       170       180       190
                ....*....|....*....|....*....|....
gi 15222437 245 GYAAPEYLA-TGHlTTKSDVYSFGVVLLELLSGR 277
Cdd:cd05574 197 EYIAPEVIKgDGH-GSAVDWWTLGILLYEMLYGT 229
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
74-276 9.03e-07

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: 49.92  E-value: 9.03e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKgwIDEKSltasrpgTGLVIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGyCLEDEHRL-LVYE 152
Cdd:cd14103   1 LGRGKFGTVYR--CVEKA-------TGKELAAKFIKCRKAKDREDVRNEIEIMNQLRHPRLLQLYD-AFETPREMvLVME 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 153 FMPRGslenHLFRRGL--YFQpLSWKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNIL-LDSEYNA-KLSDFGLA-KD 227
Cdd:cd14103  71 YVAGG----ELFERVVddDFE-LTERDCILFMRQICEGVQYMHKQG--ILHLDLKPENILcVSRTGNQiKIIDFGLArKY 143
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15222437 228 GPigDKShvsTRVM-GTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14103 144 DP--DKK---LKVLfGTPEFVAPEVVNYEPISYATDMWSVGVICYVLLSG 188
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
74-276 9.25e-07

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: 50.00  E-value: 9.25e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKgwIDEKSltasrpgTGLVIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEF 153
Cdd:cd14191  10 LGSGKFGQVFR--LVEKK-------TKKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 154 MPRGSLENHLFRRGLyfqPLSWKLRLKVALGAAKGLAFLHssETRVIYRDFKTSNILLDSEYNA--KLSDFGLAKDgpig 231
Cdd:cd14191  81 VSGGELFERIIDEDF---ELTERECIKYMRQISEGVEYIH--KQGIVHLDLKPENIMCVNKTGTkiKLIDFGLARR---- 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15222437 232 DKSHVSTRVM-GTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14191 152 LENAGSLKVLfGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSG 197
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
200-276 9.49e-07

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: 50.42  E-value: 9.49e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 200 IYRDFKTSNILLDSEYNAKLSDFG----LAKDGPIgdkshVSTRVMGTHGYAAPEYL-----ATGHLTTKSDVYSFGVVL 270
Cdd:cd05597 124 VHRDIKPDNVLLDRNGHIRLADFGsclkLREDGTV-----QSSVAVGTPDYISPEILqamedGKGRYGPECDWWSLGVCM 198

                ....*.
gi 15222437 271 LELLSG 276
Cdd:cd05597 199 YEMLYG 204
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
72-276 1.05e-06

Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of proteins with similarity to Saccharomyces cerevisiae YAK1 (or Yak1p), a dual-specificity kinase that autophosphorylates at tyrosine residues and phosphorylates substrates on S/T residues. YAK1 phosphorylates and activates the transcription factors Hsf1 and Msn2, which play important roles in cellular homeostasis during stress conditions including heat shock, oxidative stress, and nutrient deficiency. It also phosphorylates the protein POP2, a component of a complex that regulates transcription, under glucose-deprived conditions. It functions as a part of a glucose-sensing system that is involved in controlling growth in yeast. The YAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 50.33  E-value: 1.05e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  72 SVLGEGGFGCVFKGWIDEksltasrpgTGLVIAVKKL-NQDGW--QGHQE--WLAEVN-YLGQFSHRHLVKLIGYCLEDE 145
Cdd:cd14212   5 DLLGQGTFGQVVKCQDLK---------TNKLVAVKVLkNKPAYfrQAMLEiaILTLLNtKYDPEDKHHIVRLLDHFMHHG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 146 HRLLVYEFmprgsLENHLFR-------RGLYFQPLswKLRLKVALGAAKGLaflhsSETRVIYRDFKTSNILLDSEYNA- 217
Cdd:cd14212  76 HLCIVFEL-----LGVNLYEllkqnqfRGLSLQLI--RKFLQQLLDALSVL-----KDARIIHCDLKPENILLVNLDSPe 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 218 -KLSDFGLAKDgpigDKSHVSTRVMGTHgYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14212 144 iKLIDFGSACF----ENYTLYTYIQSRF-YRSPEVLLGLPYSTAIDMWSLGCIAAELFLG 198
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
122-277 1.23e-06

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: 49.56  E-value: 1.23e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 122 EVNYLGQFSHRHLVKLIgYCLED--EHRL-LVYEFMPRGSL----ENHLF---RRGLYFQPLswklrlkvalgaAKGLAF 191
Cdd:cd14200  73 EIAILKKLDHVNIVKLI-EVLDDpaEDNLyMVFDLLRKGPVmevpSDKPFsedQARLYFRDI------------VLGIEY 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 192 LHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPIGDKSHVSTrvMGTHGYAAPEYLA-TGH-LTTKS-DVYSFGV 268
Cdd:cd14200 140 LHYQ--KIVHRDIKPSNLLLGDDGHVKIADFGVSNQFEGNDALLSST--AGTPAFMAPETLSdSGQsFSGKAlDVWAMGV 215

                ....*....
gi 15222437 269 VLLELLSGR 277
Cdd:cd14200 216 TLYCFVYGK 224
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
74-286 1.33e-06

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


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 49.58  E-value: 1.33e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKG-WIDEksltasrpgtglvIAVKKLNQDGwqGHQEWLA----EVNYLGQFSHRHLVKLIGYCLEDEHRL 148
Cdd:cd14152   8 IGQGRWGKVHRGrWHGE-------------VAIRLLEIDG--NNQDHLKlfkkEVMNYRQTRHENVVLFMGACMHPPHLA 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 LVYEFMPRGSLenHLFRRGLYFQPLSWKLRlKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEyNAKLSDFGLAKDG 228
Cdd:cd14152  73 IITSFCKGRTL--YSFVRDPKTSLDINKTR-QIAQEIIKGMGYLHAKG--IVHKDLKSKNVFYDNG-KVVITDFGLFGIS 146
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 229 PIGDKSHVSTRVMGTHG---YAAPEY---LATGH------LTTKSDVYSFGVVLLElLSGRRAVDKNRPS 286
Cdd:cd14152 147 GVVQEGRRENELKLPHDwlcYLAPEIvreMTPGKdedclpFSKAADVYAFGTIWYE-LQARDWPLKNQPA 215
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
73-276 1.67e-06

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: 49.20  E-value: 1.67e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  73 VLGEGGFGCVFKGwideksltaSRPGTGLVIAVKKLNQDGWQghqEW---------LAEVNYLGQFSH--RHLVKLIGYC 141
Cdd:cd14100   7 LLGSGGFGSVYSG---------IRVADGAPVAIKHVEKDRVS---EWgelpngtrvPMEIVLLKKVGSgfRGVIRLLDWF 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 142 LEDEHRLLVYE-----------FMPRGSLENHLfRRGLYFQPLSwklrlkvalgaakglAFLHSSETRVIYRDFKTSNIL 210
Cdd:cd14100  75 ERPDSFVLVLErpepvqdlfdfITERGALPEEL-ARSFFRQVLE---------------AVRHCHNCGVLHRDIKDENIL 138
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15222437 211 LD-SEYNAKLSDFG---LAKDGpigdkshVSTRVMGTHGYAAPEYLATGHLTTKS-DVYSFGVVLLELLSG 276
Cdd:cd14100 139 IDlNTGELKLIDFGsgaLLKDT-------VYTDFDGTRVYSPPEWIRFHRYHGRSaAVWSLGILLYDMVCG 202
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
74-273 1.68e-06

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


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 49.27  E-value: 1.68e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFKgwideksltASRPGTGLVIAVKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEF 153
Cdd:cd06645  19 IGSGTYGDVYK---------ARNVNTGELAAIKVIKLEPGEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICMEF 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 154 MPRGSLENHLFRRGlyfqPLSWKLRLKVALGAAKGLAFLHSSETrvIYRDFKTSNILLDSEYNAKLSDFGLAKDgpIGDK 233
Cdd:cd06645  90 CGGGSLQDIYHVTG----PLSESQIAYVSRETLQGLYYLHSKGK--MHRDIKGANILLTDNGHVKLADFGVSAQ--ITAT 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 15222437 234 SHVSTRVMGTHGYAAPEYLAT---GHLTTKSDVYSFGVVLLEL 273
Cdd:cd06645 162 IAKRKSFIGTPYWMAPEVAAVerkGGYNQLCDIWAVGITAIEL 204
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
98-276 1.69e-06

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: 49.63  E-value: 1.69e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  98 GTGLVIAVKKLNQDGWQGHQEWLAEVNYlGQfsHRHLVKLIGYCLEDEHRLLVYEFMPRGSLENHLFRRGLYfqplSWKL 177
Cdd:cd14176  42 ATNMEFAVKIIDKSKRDPTEEIEILLRY-GQ--HPNIITLKDVYDDGKYVYVVTELMKGGELLDKILRQKFF----SERE 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 178 RLKVALGAAKGLAFLHSSEtrVIYRDFKTSNIL-LDSEYNA---KLSDFGLAKDgpIGDKSHVSTRVMGTHGYAAPEYLA 253
Cdd:cd14176 115 ASAVLFTITKTVEYLHAQG--VVHRDLKPSNILyVDESGNPesiRICDFGFAKQ--LRAENGLLMTPCYTANFVAPEVLE 190
                       170       180
                ....*....|....*....|...
gi 15222437 254 TGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14176 191 RQGYDAACDIWSLGVLLYTMLTG 213
PK_NRBP1 cd14034
Pseudokinase domain of Nuclear Receptor Binding Protein 1; The pseudokinase domain shows ...
126-349 1.76e-06

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: 49.36  E-value: 1.76e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 126 LGQFSHRHLVKLIGY---CLEDEHRLL-VYEFMPRGSLENHLFRRGLYFQPLSWKLRLKVALGAAKGLAFLHSSETRVIY 201
Cdd:cd14034  64 LIQLEHLNIVKFHKYwadVKENRARVIfITEYMSSGSLKQFLKKTKKNHKTMNEKAWKRWCTQILSALSYLHSCDPPIIH 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 202 RDFKTSNILLdsEYNaklsdfGLAKDGPIGDKS---HVST--RVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELlsg 276
Cdd:cd14034 144 GNLTCDTIFI--QHN------GLIKIGSVAPDTinnHVKTcrEEQKNLHFFAPEYGEVANVTTAVDIYSFGMCALEM--- 212
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15222437 277 rrAVDKNRPSGERNLVewakPYLVNKRKIfRVIDNRLQDQYSMeeackvatlslRCLTTEIKLRPNMSEVVSH 349
Cdd:cd14034 213 --AVLEIQGNGESSYV----PQEAINSAI-QLLEDPLQREFIQ-----------KCLEVDPSKRPTARELLFH 267
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
72-276 2.00e-06

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: 48.94  E-value: 2.00e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  72 SVLGEGGFGCVFK--GWIDeksltasrpgtGLVIAVKKLNQD--GWQGHQEWLAEVnY----LGQfsHRHLVKLIGYCLE 143
Cdd:cd14051   6 EKIGSGEFGSVYKciNRLD-----------GCVYAIKKSKKPvaGSVDEQNALNEV-YahavLGK--HPHVVRYYSAWAE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 144 DEHRLLVYEFMPRGSLENHLFRRGLYFQPLSWKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLS--- 220
Cdd:cd14051  72 DDHMIIQNEYCNGGSLADAISENEKAGERFSEAELKDLLLQVAQGLKYIHSQN--LVHMDIKPGNIFISRTPNPVSSeee 149
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15222437 221 --DFGLAKDGP--------IGDKSHVsTRVM------GTHGYAAPEYLAT--GHLtTKSDVYSFGVVLLELLSG 276
Cdd:cd14051 150 eeDFEGEEDNPesnevtykIGDLGHV-TSISnpqveeGDCRFLANEILQEnySHL-PKADIFALALTVYEAAGG 221
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
192-276 2.19e-06

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: 49.62  E-value: 2.19e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 192 LHS-SETRVIYRDFKTSNILLDSEYNAKLSDFG----LAKDGPIGdkshvSTRVMGTHGYAAPEYL-----ATGHLTTKS 261
Cdd:cd05624 186 IHSiHQLHYVHRDIKPDNVLLDMNGHIRLADFGsclkMNDDGTVQ-----SSVAVGTPDYISPEILqamedGMGKYGPEC 260
                        90
                ....*....|....*
gi 15222437 262 DVYSFGVVLLELLSG 276
Cdd:cd05624 261 DWWSLGVCMYEMLYG 275
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
131-275 2.34e-06

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-2D is allso called Retinal Guanylyl Cyclase 1 (RETGC-1) or Rod Outer Segment membrane Guanylate Cyclase (ROS-GC). It is found in the photoreceptors of the retina where it anchors the reciprocal feedback loop between calcium and cGMP, which regulates the dark, light, and recovery phases in phototransduction. It is also found in other sensory neurons and may be a universal transduction component that plays a role in the perception of all senses. 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 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-2D 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: 270945 [Multi-domain]  Cd Length: 267  Bit Score: 48.56  E-value: 2.34e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 131 HRHLVKLIGyCLEDEHRL-LVYEFMPRGSLENHLFRRGLyfqPLSWKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNI 209
Cdd:cd14043  55 HENVNLFLG-LFVDCGILaIVSEHCSRGSLEDLLRNDDM---KLDWMFKSSLLLDLIKGMRYLHHRG--IVHGRLKSRNC 128
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15222437 210 LLDSEYNAKLSDFGLAKdgpI--GDKSHVSTRVMGTHGYAAPEYLATGHL----TTKSDVYSFGVVLLELLS 275
Cdd:cd14043 129 VVDGRFVLKITDYGYNE---IleAQNLPLPEPAPEELLWTAPELLRDPRLerrgTFPGDVFSFAIIMQEVIV 197
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
67-226 2.38e-06

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


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 48.61  E-value: 2.38e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGCVFKGWideksltasRPGTGLVIAVKKLNQDGWQGHQEWLAEV-NYLGQfsHRHLVKLIGYCLEDE 145
Cdd:cd14016   1 RYKLVKKIGSGSFGEVYLGI---------DLKTGEEVAIKIEKKDSKHPQLEYEAKVyKLLQG--GPGIPRLYWFGQEGD 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 146 HRLLVYEFMprG-SLEnHLFRRglYFQPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILLDSEYNAK---LSD 221
Cdd:cd14016  70 YNVMVMDLL--GpSLE-DLFNK--CGRKFSLKTVLMLADQMISRLEYLHSK--GYIHRDIKPENFLMGLGKNSNkvyLID 142

                ....*
gi 15222437 222 FGLAK 226
Cdd:cd14016 143 FGLAK 147
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
104-276 2.46e-06

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: 48.78  E-value: 2.46e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 104 AVKKLNQDGwQGHQE-----WLAEVNYLGQFS-HRHLVKLIG-----YCLEDEHRLLVYEFMPRgSLENHLFRRGlyFQP 172
Cdd:cd14020  31 ALKEFQLDH-QGSQEsgdygFAKERAALEQLQgHRNIVTLYGvftnhYSANVPSRCLLLELLDV-SVSELLLRSS--NQG 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 173 LSWKLRLKVALGAAKGLAFLHSSEtrVIYRDFKTSNILLDSEYNA-KLSDFGLA-KDGpigdksHVSTRVMGTHGYAAPE 250
Cdd:cd14020 107 CSMWMIQHCARDVLEALAFLHHEG--YVHADLKPRNILWSAEDECfKLIDFGLSfKEG------NQDVKYIQTDGYRAPE 178
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 15222437 251 Y-----LATGHL------TTKSDVYSFGVVLLELLSG 276
Cdd:cd14020 179 AelqncLAQAGLqsetecTSAVDLWSLGIVLLEMFSG 215
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
186-349 3.04e-06

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: 48.47  E-value: 3.04e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 186 AKGLAFLHSSeTRVIYRDFKTSNILLDSEYNAKLSDFGLA--KDGPIGDKSHVSTRVMGTH-------GYAAPEYLATGH 256
Cdd:cd14011 124 SEALSFLHND-VKLVHGNICPESVVINSNGEWKLAGFDFCisSEQATDQFPYFREYDPNLPplaqpnlNYLAPEYILSKT 202
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 257 LTTKSDVYSFGVVLLELLSGRRAVDKNrpsgERNLVEwakpYLVNKRKIFRVIDNRLQDQYSMeeackVATLSLRCLTTE 336
Cdd:cd14011 203 CDPASDMFSLGVLIYAIYNKGKPLFDC----VNNLLS----YKKNSNQLRQLSLSLLEKVPEE-----LRDHVKTLLNVT 269
                       170
                ....*....|...
gi 15222437 337 IKLRPNMSEVVSH 349
Cdd:cd14011 270 PEVRPDAEQLSKI 282
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
188-277 3.09e-06

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: 48.56  E-value: 3.09e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 188 GLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAKdgpIGDKSHVSTRVMGTHGYAAPEY-LATGHlTTKSDVYSF 266
Cdd:cd07850 114 GIKHLHSAG--IIHRDLKPSNIVVKSDCTLKILDFGLAR---TAGTSFMMTPYVVTRYYRAPEViLGMGY-KENVDIWSV 187
                        90
                ....*....|.
gi 15222437 267 GVVLLELLSGR 277
Cdd:cd07850 188 GCIMGEMIRGT 198
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
99-276 3.15e-06

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: 48.47  E-value: 3.15e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  99 TGLVIAVKKLNQDGWQGHQEWLAEVNYlGQfsHRHLVKLIGYCLEDEHRLLVYEFMPRGSLENHLFRRGLYfqplSWKLR 178
Cdd:cd14177  28 TNMEFAVKIIDKSKRDPSEEIEILMRY-GQ--HPNIITLKDVYDDGRYVYLVTELMKGGELLDRILRQKFF----SEREA 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 179 LKVALGAAKGLAFLHSSEtrVIYRDFKTSNIL-LDSEYNA---KLSDFGLAKDGPiGDKSHVSTRVMgTHGYAAPEYLAT 254
Cdd:cd14177 101 SAVLYTITKTVDYLHCQG--VVHRDLKPSNILyMDDSANAdsiRICDFGFAKQLR-GENGLLLTPCY-TANFVAPEVLMR 176
                       170       180
                ....*....|....*....|..
gi 15222437 255 GHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14177 177 QGYDAACDIWSLGVLLYTMLAG 198
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
122-276 3.96e-06

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: 48.03  E-value: 3.96e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 122 EVNYLGQFSHRHLVKLIGYCLEDEHRLLVYEFMPRGSLENHLFRRglyfQPLSWKLRLKVALGAAKGLAFLHSSetRVIY 201
Cdd:cd14196  58 EVSILRQVLHPNIITLHDVYENRTDVVLILELVSGGELFDFLAQK----ESLSEEEATSFIKQILDGVNYLHTK--KIAH 131
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15222437 202 RDFKTSNI-LLDSEY---NAKLSDFGLAKDgpIGDKSHVSTrVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14196 132 FDLKPENImLLDKNIpipHIKLIDFGLAHE--IEDGVEFKN-IFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSG 207
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
98-276 3.98e-06

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: 48.10  E-value: 3.98e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  98 GTGLVIAVKKLNQDGWQGHQEWLAEVNYlGQfsHRHLVKLIGYCLEDEHRLLVYEFMPRGSLENHLFRRGLYfqplSWKL 177
Cdd:cd14175  24 ATNMEYAVKVIDKSKRDPSEEIEILLRY-GQ--HPNIITLKDVYDDGKHVYLVTELMRGGELLDKILRQKFF----SERE 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 178 RLKVALGAAKGLAFLHSSEtrVIYRDFKTSNIL-LDSEYNA---KLSDFGLAKDGPiGDKSHVSTRVMgTHGYAAPEYLA 253
Cdd:cd14175  97 ASSVLHTICKTVEYLHSQG--VVHRDLKPSNILyVDESGNPeslRICDFGFAKQLR-AENGLLMTPCY-TANFVAPEVLK 172
                       170       180
                ....*....|....*....|...
gi 15222437 254 TGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14175 173 RQGYDEGCDIWSLGILLYTMLAG 195
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
187-277 4.97e-06

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: 47.51  E-value: 4.97e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 187 KGLAFLHSSetRVIYRDFKTSNILLDSEYNAKLSDFGLAKD-GPIGDKShvSTRVMGTHGYAAPEYLATGHLTTKSDVYS 265
Cdd:cd14111 110 QGLEYLHGR--RVLHLDIKPDNIMVTNLNAIKIVDFGSAQSfNPLSLRQ--LGRRTGTLEYMAPEMVKGEPVGPPADIWS 185
                        90
                ....*....|..
gi 15222437 266 FGVVLLELLSGR 277
Cdd:cd14111 186 IGVLTYIMLSGR 197
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
67-276 5.08e-06

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: 48.11  E-value: 5.08e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGCVfkgwideksLTASRPGTGLVIAVKKLNQ-DGWQGHQ--EWLAEVNYLGQFSHRHLVKLIgYCLE 143
Cdd:cd05628   2 DFESLKVIGRGAFGEV---------RLVQKKDTGHVYAMKILRKaDMLEKEQvgHIRAERDILVEADSLWVVKMF-YSFQ 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 144 DEHRL-LVYEFMPRGSLENHLFRRGLYFQPLS--WKLRLKVALGAAKGLAFLHssetrviyRDFKTSNILLDSEYNAKLS 220
Cdd:cd05628  72 DKLNLyLIMEFLPGGDMMTLLMKKDTLTEEETqfYIAETVLAIDSIHQLGFIH--------RDIKPDNLLLDSKGHVKLS 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 221 DFGLAKDGPIG---------------------------------DKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFG 267
Cdd:cd05628 144 DFGLCTGLKKAhrtefyrnlnhslpsdftfqnmnskrkaetwkrNRRQLAFSTVGTPDYIAPEVFMQTGYNKLCDWWSLG 223

                ....*....
gi 15222437 268 VVLLELLSG 276
Cdd:cd05628 224 VIMYEMLIG 232
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
188-276 5.22e-06

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: 48.10  E-value: 5.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 188 GLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAKdgpIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFG 267
Cdd:cd07876 135 GIKHLHSAG--IIHRDLKPSNIVVKSDCTLKILDFGLAR---TACTNFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVG 209

                ....*....
gi 15222437 268 VVLLELLSG 276
Cdd:cd07876 210 CIMGELVKG 218
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
131-276 5.75e-06

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: 47.46  E-value: 5.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 131 HRHLVKLIGYCLEDEHRLLVYEFMPRGSLENHLFRRG--------LYFQPLswklrlkvalgaAKGLAFLHSSEtrVIYR 202
Cdd:cd14662  55 HPNIIRFKEVVLTPTHLAIVMEYAAGGELFERICNAGrfsedearYFFQQL------------ISGVSYCHSMQ--ICHR 120
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15222437 203 DFKTSNILLDSEY--NAKLSDFGLAKDGPIGDKSHvSTrvMGTHGYAAPEYLATGHLTTK-SDVYSFGVVLLELLSG 276
Cdd:cd14662 121 DLKLENTLLDGSPapRLKICDFGYSKSSVLHSQPK-ST--VGTPAYIAPEVLSRKEYDGKvADVWSCGVTLYVMLVG 194
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
68-275 6.41e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 48.15  E-value: 6.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437   68 FRPDSVLGEGGFG----CVFKGWIDEKSLTASRPGTGLVIA-----VKKLNQDGWQGHQEWLAEVNYLGQFSHRHLVKL- 137
Cdd:PHA03210 150 FRVIDDLPAGAFGkifiCALRASTEEAEARRGVNSTNQGKPkcerlIAKRVKAGSRAAIQLENEILALGRLNHENILKIe 229
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  138 -------IGYCLEDEHRLLVYEFMPRGSLEnhlfrrgLYFQPLSWKLR--LKVALGAakgLAFLHSSetRVIYRDFKTSN 208
Cdd:PHA03210 230 eilrseaNTYMITQKYDFDLYSFMYDEAFD-------WKDRPLLKQTRaiMKQLLCA---VEYIHDK--KLIHRDIKLEN 297
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15222437  209 ILLDSEYNAKLSDFGLAKdgPIgDKSHVSTRV--MGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:PHA03210 298 IFLNCDGKIVLGDFGTAM--PF-EKEREAFDYgwVGTVATNSPEILAGDGYCEITDIWSCGLILLDMLS 363
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
98-277 7.22e-06

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: 47.24  E-value: 7.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  98 GTGLVIAVK---KLNQDGWQghqewlaEVNYLGQFS-HRHLVKLIGYCLEDEHRLLVYEFMPRGSLENHLFRRGLyfqpL 173
Cdd:cd14091  23 ATGKEYAVKiidKSKRDPSE-------EIEILLRYGqHPNIITLRDVYDDGNSVYLVTELLRGGELLDRILRQKF----F 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 174 SWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNILL-DSEYNA---KLSDFGLAKdgpigdkshvSTR-----VMG-- 242
Cdd:cd14091  92 SEREASAVMKTLTKTVEYLHSQ--GVVHRDLKPSNILYaDESGDPeslRICDFGFAK----------QLRaenglLMTpc 159
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 15222437 243 -THGYAAPEYLATGHLTTKSDVYSFGVVLLELLSGR 277
Cdd:cd14091 160 yTANFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGY 195
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
188-282 7.39e-06

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: 47.78  E-value: 7.39e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 188 GLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAKdgpIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFG 267
Cdd:cd07874 131 GIKHLHSAG--IIHRDLKPSNIVVKSDCTLKILDFGLAR---TAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVG 205
                        90       100
                ....*....|....*....|.
gi 15222437 268 VVLLE------LLSGRRAVDK 282
Cdd:cd07874 206 CIMGEmvrhkiLFPGRDYIDQ 226
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
61-276 8.07e-06

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK1 has been implicated in regulating eye size, lens formation, and retinal morphogenesis during late embryogenesis. It also contributes to the regulation of haematopoiesis and leukaemogenesis by phosphorylating and repressing the transcription factor c-Myb, which is crucial in T- and B-cell development. In glucose-deprived conditions, HIPK1 phosphorylates Daxx, leading to its relocalization from the nucleus to the cytoplasm, where it binds and stabilizes ASK1 (apoptosis signal-regulating kinase 1), a mitogen-activated protein kinase (MAPK) kinase kinase that activates the JNK and p38 MAPK pathways. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 47.39  E-value: 8.07e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  61 LKSATRNFRPDSVLGEGGFGCVFKGWideksltasRPGTGLVIAVKKLNQDGWQGHQEWLaEVNYLGQFSHR-----HLV 135
Cdd:cd14228  10 LCSMTNSYEVLEFLGRGTFGQVAKCW---------KRSTKEIVAIKILKNHPSYARQGQI-EVSILSRLSSEnadeyNFV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 136 KLIGYCLEDEHRLLVYEFmprgsLENHL--FRRGLYFQPLSWKLRLKVALGAAKGLAFLHSseTRVIYRDFKTSNILL-- 211
Cdd:cd14228  80 RSYECFQHKNHTCLVFEM-----LEQNLydFLKQNKFSPLPLKYIRPILQQVATALMKLKS--LGLIHADLKPENIMLvd 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15222437 212 --DSEYNAKLSDFGLAkdgpigdkSHVSTRVMGTH----GYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14228 153 pvRQPYRVKVIDFGSA--------SHVSKAVCSTYlqsrYYRAPEIILGLPFCEAIDMWSLGCVIAELFLG 215
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
149-276 9.28e-06

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


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 47.18  E-value: 9.28e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 149 LVYEFMPRGSLENHLFRRGLYFQPLSWKLRLKVALGaakgLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAK-- 226
Cdd:cd05610  81 LVMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALA----LDYLHRHG--IIHRDLKPDNMLISNEGHIKLTDFGLSKvt 154
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 227 ----------------DGPIGDK-----------SHVS----------------------TRVMGTHGYAAPEYLATGHL 257
Cdd:cd05610 155 lnrelnmmdilttpsmAKPKNDYsrtpgqvlsliSSLGfntptpyrtpksvrrgaarvegERILGTPDYLAPELLLGKPH 234
                       170
                ....*....|....*....
gi 15222437 258 TTKSDVYSFGVVLLELLSG 276
Cdd:cd05610 235 GPAVDWWALGVCLFEFLTG 253
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
133-287 9.48e-06

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: 46.77  E-value: 9.48e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 133 HLVKLIGYCLEDEHRLLVYEFMPRGSLENHL--FRRGL----YFQPLS------------------WKLRLKVALGAakg 188
Cdd:cd05576  52 NMVCLRKYIISEESVFLVLQHAEGGKLWSYLskFLNDKeihqLFADLDerlaaasrfyipeeciqrWAAEMVVALDA--- 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 189 lafLHssETRVIYRDFKTSNILLDSEYNAKLSDFGLAKD-GPIGDKSHVSTRvmgthgYAAPEYLATGHLTTKSDVYSFG 267
Cdd:cd05576 129 ---LH--REGIVCRDLNPNNILLNDRGHIQLTYFSRWSEvEDSCDSDAIENM------YCAPEVGGISEETEACDWWSLG 197
                       170       180
                ....*....|....*....|
gi 15222437 268 VVLLELLSGrRAVDKNRPSG 287
Cdd:cd05576 198 ALLFELLTG-KALVECHPAG 216
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
131-349 9.71e-06

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: 46.90  E-value: 9.71e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 131 HRHLVKLIGYCLEDEHRLLVYEFMPRGSLENHLFRRG--------LYFQPLswklrlkvalgaAKGLAFLHSSEtrVIYR 202
Cdd:cd14665  55 HPNIVRFKEVILTPTHLAIVMEYAAGGELFERICNAGrfsedearFFFQQL------------ISGVSYCHSMQ--ICHR 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 203 DFKTSNILLDSEYNAKLS--DFGLAKDGPIGDKSHvSTrvMGTHGYAAPEYLATGHLTTK-SDVYSFGVVLLELLSGrrA 279
Cdd:cd14665 121 DLKLENTLLDGSPAPRLKicDFGYSKSSVLHSQPK-ST--VGTPAYIAPEVLLKKEYDGKiADVWSCGVTLYVMLVG--A 195
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15222437 280 VDKNRPSGERNLvewakpylvnKRKIFRVidnrLQDQYSMEEACKVAT----LSLRCLTTEIKLRPNMSEVVSH 349
Cdd:cd14665 196 YPFEDPEEPRNF----------RKTIQRI----LSVQYSIPDYVHISPecrhLISRIFVADPATRITIPEIRNH 255
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
122-280 9.94e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 47.30  E-value: 9.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  122 EVNYLGQFSHRHLVKLIGYCLEDEHRLLVyefMPRgslenhlFRRGLYFQpLSWKLR------LKVALGAAKGLAFLHss 195
Cdd:PHA03212 133 EAHILRAINHPSIIQLKGTFTYNKFTCLI---LPR-------YKTDLYCY-LAAKRNiaicdiLAIERSVLRAIQYLH-- 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  196 ETRVIYRDFKTSNILLDSEYNAKLSDFGlAKDGPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:PHA03212 200 ENRIIHRDIKAENIFINHPGDVCLGDFG-AACFPVDINANKYYGWAGTIATNAPELLARDPYGPAVDIWSAGIVLFEMAT 278

                 ....*
gi 15222437  276 GRRAV 280
Cdd:PHA03212 279 CHDSL 283
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
67-276 1.01e-05

Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group is composed of fungal NDR-like proteins including Saccharomyces cerevisiae CBK1 (or CBK1p), Schizosaccharomyces pombe Orb6 (or Orb6p), Ustilago maydis Ukc1 (or Ukc1p), and Neurospora crassa Cot1. Like NDR kinase, group members contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. CBK1 is an essential component in the RAM (regulation of Ace2p activity and cellular morphogenesis) network. CBK1 and Orb6 play similar roles in coordinating cell morphology with cell cycle progression. Ukc1 is involved in morphogenesis, pathogenicity, and pigment formation. Cot1 plays a role in polar tip extension.The fungal NDR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 47.15  E-value: 1.01e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  67 NFRPDSVLGEGGFGcvfkgwidEKSLTaSRPGTGLVIAVKKL-NQDGWQGHQ--EWLAEVNYLGQFSHRHLVKLIgYCLE 143
Cdd:cd05629   2 DFHTVKVIGKGAFG--------EVRLV-QKKDTGKIYAMKTLlKSEMFKKDQlaHVKAERDVLAESDSPWVVSLY-YSFQ 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 144 DEHRL-LVYEFMPRGSLENHLFRRGLYFQPLS--WKLRLKVALGAAKGLAFLHssetrviyRDFKTSNILLDSEYNAKLS 220
Cdd:cd05629  72 DAQYLyLIMEFLPGGDLMTMLIKYDTFSEDVTrfYMAECVLAIEAVHKLGFIH--------RDIKPDNILIDRGGHIKLS 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 221 DFGL---------------------AKDGPIGDKSHV-------------------STRVM-----GTHGYAAPEYLATG 255
Cdd:cd05629 144 DFGLstgfhkqhdsayyqkllqgksNKNRIDNRNSVAvdsinltmsskdqiatwkkNRRLMaystvGTPDYIAPEIFLQQ 223
                       250       260
                ....*....|....*....|.
gi 15222437 256 HLTTKSDVYSFGVVLLELLSG 276
Cdd:cd05629 224 GYGQECDWWSLGAIMFECLIG 244
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
188-277 1.06e-05

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: 47.35  E-value: 1.06e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 188 GLAFLHSSEtrVIYRDFKTSNILLDSEYNAKLSDFGLAKdgpIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFG 267
Cdd:cd07875 138 GIKHLHSAG--IIHRDLKPSNIVVKSDCTLKILDFGLAR---TAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVG 212
                        90
                ....*....|
gi 15222437 268 VVLLELLSGR 277
Cdd:cd07875 213 CIMGEMIKGG 222
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
74-276 1.12e-05

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: 46.53  E-value: 1.12e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  74 LGEGGFGCVFK------------GWIDEKSLTASRPGTGlviavkklnqdgwqgHQEWLAEVNYLGQFSHRHLVKLIGYC 141
Cdd:cd14195  13 LGSGQFAIVRKcrekgtgkeyaaKFIKKRRLSSSRRGVS---------------REEIEREVNILREIQHPNIITLHDIF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 142 LEDEHRLLVYEFMPRGSLENHLFRRglyfQPLSWKLRLKVALGAAKGLAFLHSSetRVIYRDFKTSNI-LLDSEY---NA 217
Cdd:cd14195  78 ENKTDVVLILELVSGGELFDFLAEK----ESLTEEEATQFLKQILDGVHYLHSK--RIAHFDLKPENImLLDKNVpnpRI 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15222437 218 KLSDFGLAKDGPIGDKShvsTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLSG 276
Cdd:cd14195 152 KLIDFGIAHKIEAGNEF---KNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSG 207
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
122-276 1.25e-05

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: 46.55  E-value: 1.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 122 EVNYLGQFSHRHLVKLiGYCLEDEHR-LLVYEFMPRGSLENHLFRRglyfQPLSWKLRLKVALGAAKGLAFLHSseTRVI 200
Cdd:cd14194  58 EVSILKEIQHPNVITL-HEVYENKTDvILILELVAGGELFDFLAEK----ESLTEEEATEFLKQILNGVYYLHS--LQIA 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437 201 YRDFKTSNILLdSEYNA-----KLSDFGLAKDGPIGDKShvsTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLELLS 275
Cdd:cd14194 131 HFDLKPENIML-LDRNVpkpriKIIDFGLAHKIDFGNEF---KNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLS 206

                .
gi 15222437 276 G 276
Cdd:cd14194 207 G 207
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
199-285 1.26e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 47.19  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222437  199 VIYRDFKTSNILLDSEYNAKLSDFGLAKDGPIGDKSHVSTRVMGTHGYAAPEYLATGHLTTKSDVYSFGVVLLE------ 272
Cdd:PHA03211 281 IIHRDIKTENVLVNGPEDICLGDFGAACFARGSWSTPFHYGIAGTVDTNAPEVLAGDPYTPSVDIWSAGLVIFEaavhta 360
                         90
                 ....*....|....
gi 15222437  273 -LLSGRRAvDKNRP 285
Cdd:PHA03211 361 sLFSASRG-DERRP 373
 
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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