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Conserved domains on  [gi|567218350|ref|XP_006412804|]
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mitogen-activated protein kinase kinase 2 [Eutrema salsugineum]

Protein Classification

mitogen-activated protein kinase kinase( domain architecture ID 10159671)

mitogen-activated protein kinase kinase (MAP2K) is a dual-specificity kinase that catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) or tyrosine residues on protein substrates; MAP2Ks phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
68-335 1.07e-161

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: 453.20  E-value: 1.07e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  68 SDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEY 147
Cdd:cd06623    1 SDLERVKVLGQGSSGVVYKVRHKPTGKIYALKKIHVDGDEEFRKQLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 148 MDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTF 227
Cdd:cd06623   81 MDGGSLADLLKKVGKIPEPVLAYIARQILKGLDYLHTKRHIIHRDIKPSNLLINSKGEVKIADFGISKVLENTLDQCNTF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 228 VGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQeetwSSVFELMEAIVDQPPPALPSENFSPELSSFI 307
Cdd:cd06623  161 VGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPGQ----PSFFELMQAICDGPPPSLPAEEFSPEFRDFI 236
                        250       260
                 ....*....|....*....|....*...
gi 567218350 308 STCLQKDPNSRSSAKELMEHPFLNKYNN 335
Cdd:cd06623  237 SACLQKDPKKRPSAAELLQHPFIKKADN 264
 
Name Accession Description Interval E-value
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
68-335 1.07e-161

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: 453.20  E-value: 1.07e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  68 SDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEY 147
Cdd:cd06623    1 SDLERVKVLGQGSSGVVYKVRHKPTGKIYALKKIHVDGDEEFRKQLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 148 MDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTF 227
Cdd:cd06623   81 MDGGSLADLLKKVGKIPEPVLAYIARQILKGLDYLHTKRHIIHRDIKPSNLLINSKGEVKIADFGISKVLENTLDQCNTF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 228 VGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQeetwSSVFELMEAIVDQPPPALPSENFSPELSSFI 307
Cdd:cd06623  161 VGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPGQ----PSFFELMQAICDGPPPSLPAEEFSPEFRDFI 236
                        250       260
                 ....*....|....*....|....*...
gi 567218350 308 STCLQKDPNSRSSAKELMEHPFLNKYNN 335
Cdd:cd06623  237 SACLQKDPKKRPSAAELLQHPFIKKADN 264
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
71-330 5.49e-98

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 290.97  E-value: 5.49e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350    71 DMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDG 150
Cdd:smart00220   2 EILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCEG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350   151 GSLADFLKSVKTIPESYLSAIFKQVLQGLIYLhHDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTaGLANTFVGT 230
Cdd:smart00220  82 GDLFDLLKKRGRLSEDEARFYLRQILSALEYL-HSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPG-EKLTTFVGT 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350   231 YNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEetwssvFELMEAIVDQPPPAL-PSENFSPELSSFIST 309
Cdd:smart00220 160 PEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQL------LELFKKIGKPKPPFPpPEWDISPEAKDLIRK 233
                          250       260
                   ....*....|....*....|.
gi 567218350   310 CLQKDPNSRSSAKELMEHPFL 330
Cdd:smart00220 234 LLVKDPEKRLTAEEALQHPFF 254
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
65-330 2.70e-79

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 246.66  E-value: 2.70e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  65 LSLSDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLI 144
Cdd:PLN00034  71 KSLSELERVNRIGSGAGGTVYKVIHRPTGRLYALKVIYGNHEDTVRRQICREIEILRDVNHPNVVKCHDMFDHNGEIQVL 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 145 LEYMDGGSLadflKSVKTIPESYLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLA 224
Cdd:PLN00034 151 LEFMDGGSL----EGTHIADEQFLADVARQILSGIAYLHR-RHIVHRDIKPSNLLINSAKNVKIADFGVSRILAQTMDPC 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 225 NTFVGTYNYMSPERIVGN----KY-GNKSDIWSLGLVVLECATGKFPyLPPDQEETWSSvfeLMEAIVDQPPPALPSeNF 299
Cdd:PLN00034 226 NSSVGTIAYMSPERINTDlnhgAYdGYAGDIWSLGVSILEFYLGRFP-FGVGRQGDWAS---LMCAICMSQPPEAPA-TA 300
                        250       260       270
                 ....*....|....*....|....*....|.
gi 567218350 300 SPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:PLN00034 301 SREFRHFISCCLQREPAKRWSAMQLLQHPFI 331
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
73-326 7.67e-63

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 208.33  E-value: 7.67e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  73 VKFLGKGSSGVVQLVQHKWTGQFFALKVI--QLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDG 150
Cdd:COG0515   12 LRLLGRGGMGVVYLARDLRLGRPVALKVLrpELAADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEYVEG 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 151 GSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTA-GLANTFVG 229
Cdd:COG0515   92 ESLADLLRRRGPLPPAEALRILAQLAEALAAAH-AAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATlTQTGTVVG 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 230 TYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYlppdqeeTWSSVFELMEAIVDQPPPALPSEN--FSPELSSFI 307
Cdd:COG0515  171 TPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPF-------DGDSPAELLRAHLREPPPPPSELRpdLPPALDAIV 243
                        250       260
                 ....*....|....*....|
gi 567218350 308 STCLQKDPNSR-SSAKELME 326
Cdd:COG0515  244 LRALAKDPEERyQSAAELAA 263
Pkinase pfam00069
Protein kinase domain;
73-330 8.91e-62

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 197.08  E-value: 8.91e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350   73 VKFLGKGSSGVVQLVQHKWTGQFFALKVIQL-NIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGG 151
Cdd:pfam00069   4 LRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKeKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYVEGG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  152 SLADFLKSVKTIPESYLSAIFKQVLQGLiylhhdkhiihrdlkpsnllinhrgevkitdfgvstvmtNTAGLANTFVGTY 231
Cdd:pfam00069  84 SLFDLLSEKGAFSEREAKFIMKQILEGL---------------------------------------ESGSSLTTFVGTP 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  232 NYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETwssvfelMEAIVDQP--PPALPSeNFSPELSSFIST 309
Cdd:pfam00069 125 WYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEI-------YELIIDQPyaFPELPS-NLSEEAKDLLKK 196
                         250       260
                  ....*....|....*....|.
gi 567218350  310 CLQKDPNSRSSAKELMEHPFL 330
Cdd:pfam00069 197 LLKKDPSKRLTATQALQHPWF 217
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
143-326 3.19e-28

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 115.28  E-value: 3.19e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 143 LILEYMDGGSLADFLK-----SVKTIPEsylsaIFKQVLQGLIYLHHdKHIIHRDLKPSNLLINHRGEVKITDFGV---- 213
Cdd:NF033483  84 IVMEYVDGRTLKDYIRehgplSPEEAVE-----IMIQILSALEHAHR-NGIVHRDIKPQNILITKDGRVKVTDFGIaral 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 214 -STVMTNTaglaNTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYlppDQEetwSSVfelmeAI----VD 288
Cdd:NF033483 158 sSTTMTQT----NSVLGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPF---DGD---SPV-----SVaykhVQ 222
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 567218350 289 QPPPAlPSE---NFSPELSSFISTCLQKDPNSR-SSAKELME 326
Cdd:NF033483 223 EDPPP-PSElnpGIPQSLDAVVLKATAKDPDDRyQSAAEMRA 263
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
92-326 2.30e-19

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


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 89.90  E-value: 2.30e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350    92 TGQFFALKVIQLNI--DEAIRKSIAQELKINQSSQCPYLVnsyqSFYDNGA-----ISLILEYMDGGSLADFLKSVKTIP 164
Cdd:TIGR03903    2 TGHEVAIKLLRTDApeEEHQRARFRRETALCARLYHPNIV----ALLDSGEappglLFAVFEYVPGRTLREVLAADGALP 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350   165 ESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRG---EVKITDFGVSTVMTN-------TAGLANTFVGTYNYM 234
Cdd:TIGR03903   78 AGETGRLMLQVLDALACAH-NQGIVHRDLKPQNIMVSQTGvrpHAKVLDFGIGTLLPGvrdadvaTLTRTTEVLGTPTYC 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350   235 SPERIVGNKYGNKSDIWSLGLVVLECATGKfpylppdQEETWSSVFELMEAIVDQPPPALPSENFSPELSSFISTCLQKD 314
Cdd:TIGR03903  157 APEQLRGEPVTPNSDLYAWGLIFLECLTGQ-------RVVQGASVAEILYQQLSPVDVSLPPWIAGHPLGQVLRKALNKD 229
                          250
                   ....*....|...
gi 567218350   315 PNSRS-SAKELME 326
Cdd:TIGR03903  230 PRQRAaSAPALAE 242
 
Name Accession Description Interval E-value
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
68-335 1.07e-161

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: 453.20  E-value: 1.07e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  68 SDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEY 147
Cdd:cd06623    1 SDLERVKVLGQGSSGVVYKVRHKPTGKIYALKKIHVDGDEEFRKQLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 148 MDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTF 227
Cdd:cd06623   81 MDGGSLADLLKKVGKIPEPVLAYIARQILKGLDYLHTKRHIIHRDIKPSNLLINSKGEVKIADFGISKVLENTLDQCNTF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 228 VGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQeetwSSVFELMEAIVDQPPPALPSENFSPELSSFI 307
Cdd:cd06623  161 VGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPGQ----PSFFELMQAICDGPPPSLPAEEFSPEFRDFI 236
                        250       260
                 ....*....|....*....|....*...
gi 567218350 308 STCLQKDPNSRSSAKELMEHPFLNKYNN 335
Cdd:cd06623  237 SACLQKDPKKRPSAAELLQHPFIKKADN 264
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
68-335 9.56e-159

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: 445.64  E-value: 9.56e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  68 SDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEY 147
Cdd:cd06605    1 DDLEYLGELGEGNGGVVSKVRHRPSGQIMAVKVIRLEIDEALQKQILRELDVLHKCNSPYIVGFYGAFYSEGDISICMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 148 MDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTagLANTF 227
Cdd:cd06605   81 MDGGSLDKILKEVGRIPERILGKIAVAVVKGLIYLHEKHKIIHRDVKPSNILVNSRGQVKLCDFGVSGQLVDS--LAKTF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 228 VGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYlPPDQEETWSSVFELMEAIVDQPPPALPSENFSPELSSFI 307
Cdd:cd06605  159 VGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPY-PPPNAKPSMMIFELLSYIVDEPPPLLPSGKFSPDFQDFV 237
                        250       260
                 ....*....|....*....|....*...
gi 567218350 308 STCLQKDPNSRSSAKELMEHPFLNKYNN 335
Cdd:cd06605  238 SQCLQKDPTERPSYKELMEHPFIKRYEY 265
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
68-343 1.15e-100

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: 299.74  E-value: 1.15e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  68 SDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEY 147
Cdd:cd06615    1 DDFEKLGELGAGNGGVVTKVLHRPSGLIMARKLIHLEIKPAIRNQIIRELKVLHECNSPYIVGFYGAFYSDGEISICMEH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 148 MDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTagLANTF 227
Cdd:cd06615   81 MDGGSLDQVLKKAGRIPENILGKISIAVLRGLTYLREKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDS--MANSF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 228 VGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWS-----------------------------S 278
Cdd:cd06615  159 VGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGRYPIPPPDAKELEAmfgrpvsegeakeshrpvsghppdsprpmA 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 567218350 279 VFELMEAIVDQPPPALPSENFSPELSSFISTCLQKDPNSRSSAKELMEHPFLNKYNNSEINLASY 343
Cdd:cd06615  239 IFELLDYIVNEPPPKLPSGAFSDEFQDFVDKCLKKNPKERADLKELTKHPFIKRAELEEVDFAGW 303
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
71-330 5.49e-98

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 290.97  E-value: 5.49e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350    71 DMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDG 150
Cdd:smart00220   2 EILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCEG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350   151 GSLADFLKSVKTIPESYLSAIFKQVLQGLIYLhHDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTaGLANTFVGT 230
Cdd:smart00220  82 GDLFDLLKKRGRLSEDEARFYLRQILSALEYL-HSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPG-EKLTTFVGT 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350   231 YNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEetwssvFELMEAIVDQPPPAL-PSENFSPELSSFIST 309
Cdd:smart00220 160 PEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQL------LELFKKIGKPKPPFPpPEWDISPEAKDLIRK 233
                          250       260
                   ....*....|....*....|.
gi 567218350   310 CLQKDPNSRSSAKELMEHPFL 330
Cdd:smart00220 234 LLVKDPEKRLTAEEALQHPFF 254
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
64-333 3.87e-93

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: 279.71  E-value: 3.87e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  64 ELSLSDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFY-DNGAIS 142
Cdd:cd06620    1 DLKNQDLETLKDLGAGNGGSVSKVLHIPTGTIMAKKVIHIDAKSSVRKQILRELQILHECHSPYIVSFYGAFLnENNNII 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 143 LILEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTag 222
Cdd:cd06620   81 ICMEYMDCGSLDKILKKKGPFPEEVLGKIAVAVLEGLTYLYNVHRIIHRDIKPSNILVNSKGQIKLCDFGVSGELINS-- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 223 LANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWS----SVFELMEAIVDQPPPALPSEN 298
Cdd:cd06620  159 IADTFVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFAGSNDDDDGYngpmGILDLLQRIVNEPPPRLPKDR 238
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 567218350 299 -FSPELSSFISTCLQKDPNSRSSAKELMEHPFLNKY 333
Cdd:cd06620  239 iFPKDLRDFVDRCLLKDPRERPSPQLLLDHDPFIQA 274
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
69-330 6.98e-91

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: 272.92  E-value: 6.98e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  69 DLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAiRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYM 148
Cdd:cd05122    1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEK-KESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVMEFC 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 149 DGGSLADFLKS-VKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTaGLANTF 227
Cdd:cd05122   80 SGGSLKDLLKNtNKTLTEQQIAYVCKEVLKGLEYLH-SHGIIHRDIKAANILLTSDGEVKLIDFGLSAQLSDG-KTRNTF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 228 VGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPY--LPPdqeetwssvFELMEAIVDQPPPALPS-ENFSPELS 304
Cdd:cd05122  158 VGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYseLPP---------MKALFLIATNGPPGLRNpKKWSKEFK 228
                        250       260
                 ....*....|....*....|....*.
gi 567218350 305 SFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd05122  229 DFLKKCLQKDPEKRPTAEQLLKHPFI 254
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
64-344 2.05e-84

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: 258.83  E-value: 2.05e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  64 ELSLSDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISL 143
Cdd:cd06650    1 ELKDDDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 144 ILEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTagL 223
Cdd:cd06650   81 CMEHMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLREKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDS--M 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 224 ANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEE----------------------------- 274
Cdd:cd06650  159 ANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIPPPDAKElelmfgcqvegdaaetpprprtpgrplss 238
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 567218350 275 ------TWSSVFELMEAIVDQPPPALPSENFSPELSSFISTCLQKDPNSRSSAKELMEHPFLNKYNNSEINLASYF 344
Cdd:cd06650  239 ygmdsrPPMAIFELLDYIVNEPPPKLPSGVFSLEFQDFVNKCLIKNPAERADLKQLMVHAFIKRSDAEEVDFAGWL 314
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
68-347 3.49e-83

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: 254.39  E-value: 3.49e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  68 SDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEY 147
Cdd:cd06622    1 DEIEVLDELGKGNYGSVYKVLHRPTGVTMAMKEIRLELDESKFNQIIMELDILHKAVSPYIVDFYGAFFIEGAVYMCMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 148 MDGGS---LADFLKSVKTIPESYLSAIFKQVLQGLIYLHHDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMtnTAGLA 224
Cdd:cd06622   81 MDAGSldkLYAGGVATEGIPEDVLRRITYAVVKGLKFLKEEHNIIHRDVKPTNVLVNGNGQVKLCDFGVSGNL--VASLA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 225 NTFVGTYNYMSPERI-VGNKYGN-----KSDIWSLGLVVLECATGKFPYlPPdqeETWSSVFELMEAIVDQPPPALPSEn 298
Cdd:cd06622  159 KTNIGCQSYMAPERIkSGGPNQNptytvQSDVWSLGLSILEMALGRYPY-PP---ETYANIFAQLSAIVDGDPPTLPSG- 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 567218350 299 FSPELSSFISTCLQKDPNSRSSAKELMEHPFLNKYNNSEINLASYFTDA 347
Cdd:cd06622  234 YSDDAQDFVAKCLNKIPNRRPTYAQLLEHPWLVKYKNADVDMAEWVTGA 282
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
74-330 1.25e-82

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: 252.06  E-value: 1.25e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVIQL-NIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGS 152
Cdd:cd06606    6 ELLGKGSFGSVYLALNLDTGELMAVKEVELsGDSEEELEALEREIRILSSLKHPNIVRYLGTERTENTLNIFLEYVPGGS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 153 LADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVM--TNTAGLANTFVGT 230
Cdd:cd06606   86 LASLLKKFGKLPEPVVRKYTRQILEGLEYLH-SNGIVHRDIKGANILVDSDGVVKLADFGCAKRLaeIATGEGTKSLRGT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 231 YNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYlpPDQEETWSSVFELMEAivDQPPPaLPsENFSPELSSFISTC 310
Cdd:cd06606  165 PYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPW--SELGNPVAALFKIGSS--GEPPP-IP-EHLSEEAKDFLRKC 238
                        250       260
                 ....*....|....*....|
gi 567218350 311 LQKDPNSRSSAKELMEHPFL 330
Cdd:cd06606  239 LQRDPKKRPTADELLQHPFL 258
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
69-330 1.60e-81

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: 249.10  E-value: 1.60e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  69 DLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIqlNIDEAIrKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYM 148
Cdd:cd06612    4 VFDILEKLGEGSYGSVYKAIHKETGQVVAIKVV--PVEEDL-QEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVMEYC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 149 DGGSLADFLKSV-KTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTF 227
Cdd:cd06612   81 GAGSVSDIMKITnKTLTEEEIAAILYQTLKGLEYLH-SNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLTDTMAKRNTV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 228 VGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPY--LPPdqeetwssvFELMEAIVDQPPPALPS-ENFSPELS 304
Cdd:cd06612  160 IGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYsdIHP---------MRAIFMIPNKPPPTLSDpEKWSPEFN 230
                        250       260
                 ....*....|....*....|....*.
gi 567218350 305 SFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd06612  231 DFVKKCLVKDPEERPSAIQLLQHPFI 256
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
72-343 1.70e-79

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: 245.02  E-value: 1.70e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  72 MVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDN--GAISLILEYMD 149
Cdd:cd06621    5 ELSSLGEGAGGSVTKCRLRNTKTIFALKTITTDPNPDVQKQILRELEINKSCASPYIVKYYGAFLDEqdSSIGIAMEYCE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 150 GGSLADFLKSVKT----IPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTagLAN 225
Cdd:cd06621   85 GGSLDSIYKKVKKkggrIGEKVLGKIAESVLKGLSYLH-SRKIIHRDIKPSNILLTRKGQVKLCDFGVSGELVNS--LAG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 226 TFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYlPPDQEETWSSVfELMEAIVDQPPPALPSE-----NFS 300
Cdd:cd06621  162 TFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPF-PPEGEPPLGPI-ELLSYIVNMPNPELKDEpengiKWS 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 567218350 301 PELSSFISTCLQKDPNSRSSAKELMEHPFLNKYNNSEINLASY 343
Cdd:cd06621  240 ESFKDFIEKCLEKDGTRRPGPWQMLAHPWIKAQEKKKVNMAKF 282
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
73-330 2.55e-79

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: 243.52  E-value: 2.55e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  73 VKFLGKGSSGVVQLVQHKWTGQFFALKVIQL-NIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGG 151
Cdd:cd08215    5 IRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLsNMSEKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVMEYADGG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 152 SLADFLKSVKT----IPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTF 227
Cdd:cd08215   85 DLAQKIKKQKKkgqpFPEEQILDWFVQICLALKYLH-SRKILHRDLKTQNIFLTKDGVVKLGDFGISKVLESTTDLAKTV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 228 VGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKfpylPPDQEETWSSvfeLMEAIVDQPPPALPSeNFSPELSSFI 307
Cdd:cd08215  164 VGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLK----HPFEANNLPA---LVYKIVKGQYPPIPS-QYSSELRDLV 235
                        250       260
                 ....*....|....*....|...
gi 567218350 308 STCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd08215  236 NSMLQKDPEKRPSANEILSSPFI 258
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
65-330 2.70e-79

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 246.66  E-value: 2.70e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  65 LSLSDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLI 144
Cdd:PLN00034  71 KSLSELERVNRIGSGAGGTVYKVIHRPTGRLYALKVIYGNHEDTVRRQICREIEILRDVNHPNVVKCHDMFDHNGEIQVL 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 145 LEYMDGGSLadflKSVKTIPESYLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLA 224
Cdd:PLN00034 151 LEFMDGGSL----EGTHIADEQFLADVARQILSGIAYLHR-RHIVHRDIKPSNLLINSAKNVKIADFGVSRILAQTMDPC 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 225 NTFVGTYNYMSPERIVGN----KY-GNKSDIWSLGLVVLECATGKFPyLPPDQEETWSSvfeLMEAIVDQPPPALPSeNF 299
Cdd:PLN00034 226 NSSVGTIAYMSPERINTDlnhgAYdGYAGDIWSLGVSILEFYLGRFP-FGVGRQGDWAS---LMCAICMSQPPEAPA-TA 300
                        250       260       270
                 ....*....|....*....|....*....|.
gi 567218350 300 SPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:PLN00034 301 SREFRHFISCCLQREPAKRWSAMQLLQHPFI 331
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
69-343 5.73e-79

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: 243.49  E-value: 5.73e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  69 DLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKIN-QSSQCPYLVNSYQSFYDNGAISLILEY 147
Cdd:cd06617    2 DLEVIEELGRGAYGVVDKMRHVPTGTIMAVKRIRATVNSQEQKRLLMDLDISmRSVDCPYTVTFYGALFREGDVWICMEV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 148 MDGgSLADFLKSV----KTIPESYLSAIFKQVLQGLIYLHHDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTagL 223
Cdd:cd06617   82 MDT-SLDKFYKKVydkgLTIPEDILGKIAVSIVKALEYLHSKLSVIHRDVKPSNVLINRNGQVKLCDFGISGYLVDS--V 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 224 ANTF-VGTYNYMSPERIVGNK----YGNKSDIWSLGLVVLECATGKFPYlppdqeETWSSVFELMEAIVDQPPPALPSEN 298
Cdd:cd06617  159 AKTIdAGCKPYMAPERINPELnqkgYDVKSDVWSLGITMIELATGRFPY------DSWKTPFQQLKQVVEEPSPQLPAEK 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 567218350 299 FSPELSSFISTCLQKDPNSRSSAKELMEHPFLNKYNNSEINLASY 343
Cdd:cd06617  233 FSPEFQDFVNKCLKKNYKERPNYPELLQHPFFELHLSKNTDVASF 277
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
64-344 5.88e-79

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: 245.34  E-value: 5.88e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  64 ELSLSDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISL 143
Cdd:cd06649    1 ELKDDDFERISELGAGNGGVVTKVQHKPSGLIMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 144 ILEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTagL 223
Cdd:cd06649   81 CMEHMDGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLREKHQIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDS--M 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 224 ANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWS-------------------------- 277
Cdd:cd06649  159 ANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYPIPPPDAKELEAifgrpvvdgeegephsisprprppgr 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 278 -------------SVFELMEAIVDQPPPALPSENFSPELSSFISTCLQKDPNSRSSAKELMEHPFLNKYNNSEINLASYF 344
Cdd:cd06649  239 pvsghgmdsrpamAIFELLDYIVNEPPPKLPNGVFTPDFQEFVNKCLIKNPAERADLKMLMNHTFIKRSEVEEVDFAGWL 318
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
76-333 5.17e-78

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: 240.61  E-value: 5.17e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLAD 155
Cdd:cd06609    9 IGKGSFGEVYKGIDKRTNQVVAIKVIDLEEAEDEIEDIQQEIQFLSQCDSPYITKYYGSFLKGSKLWIIMEYCGGGSVLD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 156 FLKSVKtIPESYLSAIFKQVLQGLIYLHHDKHIiHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVGTYNYMS 235
Cdd:cd06609   89 LLKPGP-LDETYIAFILREVLLGLEYLHSEGKI-HRDIKAANILLSEEGDVKLADFGVSGQLTSTMSKRNTFVGTPFWMA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 236 PERIVGNKYGNKSDIWSLGLVVLECATGKFPYlppdqeetwsSVFELMEA---IVDQPPPALPSENFSPELSSFISTCLQ 312
Cdd:cd06609  167 PEVIKQSGYDEKADIWSLGITAIELAKGEPPL----------SDLHPMRVlflIPKNNPPSLEGNKFSKPFKDFVELCLN 236
                        250       260
                 ....*....|....*....|.
gi 567218350 313 KDPNSRSSAKELMEHPFLNKY 333
Cdd:cd06609  237 KDPKERPSAKELLKHKFIKKA 257
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
71-331 7.32e-76

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: 234.41  E-value: 7.32e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  71 DMVKfLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEaiRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDG 150
Cdd:cd06614    4 NLEK-IGEGASGEVYKATDRATGKEVAIKKMRLRKQN--KELIINEILIMKECKHPNIVDYYDSYLVGDELWVVMEYMDG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 151 GSLADFL-KSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVG 229
Cdd:cd06614   81 GSLTDIItQNPVRMNESQIAYVCREVLQGLEYLH-SQNVIHRDIKSDNILLSKDGSVKLADFGFAAQLTKEKSKRNSVVG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 230 TYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYL--PPdqeetwssvFELMEAIVDQPPPALP-SENFSPELSSF 306
Cdd:cd06614  160 TPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYLeePP---------LRALFLITTKGIPPLKnPEKWSPEFKDF 230
                        250       260
                 ....*....|....*....|....*
gi 567218350 307 ISTCLQKDPNSRSSAKELMEHPFLN 331
Cdd:cd06614  231 LNKCLVKDPEKRPSAEELLQHPFLK 255
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
69-330 3.83e-75

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: 232.75  E-value: 3.83e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  69 DLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVI---QLnIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLIL 145
Cdd:cd14007    1 DFEIGKPLGKGKFGNVYLAREKKSGFIVALKVIsksQL-QKSGLEHQLRREIEIQSHLRHPNILRLYGYFEDKKRIYLIL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 146 EYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNtaGLAN 225
Cdd:cd14007   80 EYAPNGELYKELKKQKRFDEKEAAKYIYQLALALDYLH-SKNIIHRDIKPENILLGSNGELKLADFGWSVHAPS--NRRK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 226 TFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETwssvfelMEAIVDQPPPaLPSeNFSPELSS 305
Cdd:cd14007  157 TFCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQET-------YKRIQNVDIK-FPS-SVSPEAKD 227
                        250       260
                 ....*....|....*....|....*
gi 567218350 306 FISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14007  228 LISKLLQKDPSKRLSLEQVLNHPWI 252
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
69-342 9.74e-75

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: 232.46  E-value: 9.74e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  69 DLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYM 148
Cdd:cd06619    2 DIQYQEILGHGNGGTVYKAYHLLTRRILAVKVIPLDITVELQKQIMSELEILYKCDSPYIIGFYGAFFVENRISICTEFM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 149 DGGSLADFlksvKTIPESYLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTagLANTFV 228
Cdd:cd06619   82 DGGSLDVY----RKIPEHVLGRIAVAVVKGLTYLWSLK-ILHRDVKPSNMLVNTRGQVKLCDFGVSTQLVNS--IAKTYV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 229 GTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFELMEAIVDQPPPALPSENFSPELSSFIS 308
Cdd:cd06619  155 GTNAYMAPERISGEQYGIHSDVWSLGISFMELALGRFPYPQIQKNQGSLMPLQLLQCIVDEDPPVLPVGQFSEKFVHFIT 234
                        250       260       270
                 ....*....|....*....|....*....|....
gi 567218350 309 TCLQKDPNSRSSAKELMEHPFLNKYNNSEINLAS 342
Cdd:cd06619  235 QCMRKQPKERPAPENLMDHPFIVQYNDGNAEVVS 268
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
76-330 7.55e-68

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: 214.01  E-value: 7.55e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLN-IDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLA 154
Cdd:cd06627    8 IGRGAFGSVYKGLNLNTGEFVAIKQISLEkIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEYVENGSLA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 155 DFLKSVKTIPESyLSAIF-KQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVGTYNY 233
Cdd:cd06627   88 SIIKKFGKFPES-LVAVYiYQVLEGLAYLH-EQGVIHRDIKGANILTTKDGLVKLADFGVATKLNEVEKDENSVVGTPYW 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 234 MSPERIVGNKYGNKSDIWSLGLVVLECATGKFPY--LPPdqeetwssvFELMEAIVDQPPPALPsENFSPELSSFISTCL 311
Cdd:cd06627  166 MAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPYydLQP---------MAALFRIVQDDHPPLP-ENISPELRDFLLQCF 235
                        250
                 ....*....|....*....
gi 567218350 312 QKDPNSRSSAKELMEHPFL 330
Cdd:cd06627  236 QKDPTLRPSAKELLKHPWL 254
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
64-347 3.11e-67

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: 213.77  E-value: 3.11e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  64 ELSLSDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELK-INQSSQCPYLVNSYQSFYDNGAIS 142
Cdd:cd06616    2 EFTAEDLKDLGEIGRGAFGTVNKMLHKPSGTIMAVKRIRSTVDEKEQKRLLMDLDvVMRSSDCPYIVKFYGALFREGDCW 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 143 LILEYMDGgSLADFLKSV-----KTIPESYLSAIFKQVLQGLIYLHHDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVM 217
Cdd:cd06616   82 ICMELMDI-SLDKFYKYVyevldSVIPEEILGKIAVATVKALNYLKEELKIIHRDVKPSNILLDRNGNIKLCDFGISGQL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 218 TNTagLANTF-VGTYNYMSPERI----VGNKYGNKSDIWSLGLVVLECATGKFPYlppdqeETWSSVFELMEAIVDQPPP 292
Cdd:cd06616  161 VDS--IAKTRdAGCRPYMAPERIdpsaSRDGYDVRSDVWSLGITLYEVATGKFPY------PKWNSVFDQLTQVVKGDPP 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 567218350 293 ALPSEN---FSPELSSFISTCLQKDPNSRSSAKELMEHPFLNKYNNSEINLASYFTDA 347
Cdd:cd06616  233 ILSNSEereFSPSFVNFVNLCLIKDESKRPKYKELLKHPFIKMYEERNVDVAAYVQKI 290
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
73-326 6.60e-67

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: 211.68  E-value: 6.60e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  73 VKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNI--DEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDG 150
Cdd:cd14014    5 VRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELaeDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVMEYVEG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 151 GSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAG-LANTFVG 229
Cdd:cd14014   85 GSLADLLRERGPLPPREALRILAQIADALAAAH-RAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLtQTGSVLG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 230 TYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEetwssvfELMEAIVDQPPPALPSEN--FSPELSSFI 307
Cdd:cd14014  164 TPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPA-------AVLAKHLQEAPPPPSPLNpdVPPALDAII 236
                        250       260
                 ....*....|....*....|
gi 567218350 308 STCLQKDPNSR-SSAKELME 326
Cdd:cd14014  237 LRALAKDPEERpQSAAELLA 256
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
76-329 7.82e-67

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: 211.22  E-value: 7.82e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKViqLNIDEAI-RKSIAQ---ELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGG 151
Cdd:cd05123    1 LGKGSFGKVLLVRKKDTGKLYAMKV--LRKKEIIkRKEVEHtlnERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 152 SLADFLKSVKTIPESYLSAIFKQVLQGLIYLH-HDkhIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVGT 230
Cdd:cd05123   79 ELFSHLSKEGRFPEERARFYAAEIVLALEYLHsLG--IIYRDLKPENILLDSDGHIKLTDFGLAKELSSDGDRTYTFCGT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 231 YNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFELmeaivdqpPPALPsENFSPELSSFISTC 310
Cdd:cd05123  157 PEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKS--------PLKFP-EYVSPEAKSLISGL 227
                        250       260
                 ....*....|....*....|..
gi 567218350 311 LQKDPNSR---SSAKELMEHPF 329
Cdd:cd05123  228 LQKDPTKRlgsGGAEEIKAHPF 249
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
76-330 1.79e-65

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: 208.18  E-value: 1.79e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVI--------------QLNIDEAIRKsIAQELKINQSSQCPYLVNSYQSFYD--NG 139
Cdd:cd14008    1 LGRGSFGKVKLALDTETGQLYAIKIFnksrlrkrregkndRGKIKNALDD-VRREIAIMKKLDHPNIVRLYEVIDDpeSD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 140 AISLILEYMDGGSLADF--LKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVM 217
Cdd:cd14008   80 KLYLVLEYCEGGPVMELdsGDRVPPLPEETARKYFRDLVLGLEYLH-ENGIVHRDIKPENLLLTADGTVKISDFGVSEMF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 218 TNTAGLANTFVGTYNYMSPERIVGNKY---GNKSDIWSLGlVVLEC-ATGKFPYLPpdqeetwSSVFELMEAIVDQPPPA 293
Cdd:cd14008  159 EDGNDTLQKTAGTPAFLAPELCDGDSKtysGKAADIWALG-VTLYClVFGRLPFNG-------DNILELYEAIQNQNDEF 230
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 567218350 294 LPSENFSPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14008  231 PIPPELSPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
71-329 1.29e-63

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: 203.13  E-value: 1.29e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  71 DMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLN-IDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMD 149
Cdd:cd14003    3 ELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSkLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETENKIYLVMEYAS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 150 GGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTnTAGLANTFVG 229
Cdd:cd14003   83 GGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHS-NGIVHRDLKLENILLDKNGNLKIIDFGLSNEFR-GGSLLKTFCG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 230 TYNYMSPERIVGNKY-GNKSDIWSLGLVVLECATGKFPYLPPDQEEtwssvfelMEAIVDQPPPALPSeNFSPELSSFIS 308
Cdd:cd14003  161 TPAYAAPEVLLGRKYdGPKADVWSLGVILYAMLTGYLPFDDDNDSK--------LFRKILKGKYPIPS-HLSPDARDLIR 231
                        250       260
                 ....*....|....*....|.
gi 567218350 309 TCLQKDPNSRSSAKELMEHPF 329
Cdd:cd14003  232 RMLVVDPSKRITIEEILNHPW 252
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
73-326 7.67e-63

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 208.33  E-value: 7.67e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  73 VKFLGKGSSGVVQLVQHKWTGQFFALKVI--QLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDG 150
Cdd:COG0515   12 LRLLGRGGMGVVYLARDLRLGRPVALKVLrpELAADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEYVEG 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 151 GSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTA-GLANTFVG 229
Cdd:COG0515   92 ESLADLLRRRGPLPPAEALRILAQLAEALAAAH-AAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATlTQTGTVVG 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 230 TYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYlppdqeeTWSSVFELMEAIVDQPPPALPSEN--FSPELSSFI 307
Cdd:COG0515  171 TPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPF-------DGDSPAELLRAHLREPPPPPSELRpdLPPALDAIV 243
                        250       260
                 ....*....|....*....|
gi 567218350 308 STCLQKDPNSR-SSAKELME 326
Cdd:COG0515  244 LRALAKDPEERyQSAAELAA 263
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
71-329 1.50e-62

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: 200.40  E-value: 1.50e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  71 DMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQL-NIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMD 149
Cdd:cd05117    3 ELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKkKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVMELCT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 150 GGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHR---GEVKITDFGVSTVMTNTaGLANT 226
Cdd:cd05117   83 GGELFDRIVKKGSFSEREAAKIMKQILSAVAYLH-SQGIVHRDLKPENILLASKdpdSPIKIIDFGLAKIFEEG-EKLKT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 227 FVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEEtwssVFEL-MEAIVDQPPPALPseNFSPELSS 305
Cdd:cd05117  161 VCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQE----LFEKiLKGKYSFDSPEWK--NVSEEAKD 234
                        250       260
                 ....*....|....*....|....
gi 567218350 306 FISTCLQKDPNSRSSAKELMEHPF 329
Cdd:cd05117  235 LIKRLLVVDPKKRLTAAEALNHPW 258
Pkinase pfam00069
Protein kinase domain;
73-330 8.91e-62

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 197.08  E-value: 8.91e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350   73 VKFLGKGSSGVVQLVQHKWTGQFFALKVIQL-NIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGG 151
Cdd:pfam00069   4 LRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKeKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYVEGG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  152 SLADFLKSVKTIPESYLSAIFKQVLQGLiylhhdkhiihrdlkpsnllinhrgevkitdfgvstvmtNTAGLANTFVGTY 231
Cdd:pfam00069  84 SLFDLLSEKGAFSEREAKFIMKQILEGL---------------------------------------ESGSSLTTFVGTP 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  232 NYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETwssvfelMEAIVDQP--PPALPSeNFSPELSSFIST 309
Cdd:pfam00069 125 WYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEI-------YELIIDQPyaFPELPS-NLSEEAKDLLKK 196
                         250       260
                  ....*....|....*....|.
gi 567218350  310 CLQKDPNSRSSAKELMEHPFL 330
Cdd:pfam00069 197 LLKKDPSKRLTATQALQHPWF 217
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
64-346 1.65e-61

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: 199.14  E-value: 1.65e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  64 ELSLSDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQ-CPYLVNSYQSFYDNGAIS 142
Cdd:cd06618   11 KADLNDLENLGEIGSGTCGQVYKMRHKKTGHVMAVKQMRRSGNKEENKRILMDLDVVLKSHdCPYIVKCYGYFITDSDVF 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 143 LILEYMdGGSLADFLKSVKT-IPESYLSAIFKQVLQGLIYLHHDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTa 221
Cdd:cd06618   91 ICMELM-STCLDKLLKRIQGpIPEDILGKMTVSIVKALHYLKEKHGVIHRDVKPSNILLDESGNVKLCDFGISGRLVDS- 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 222 gLANT-FVGTYNYMSPERIVGN---KYGNKSDIWSLGLVVLECATGKFPYLPPDQEetwssvFELMEAIVDQPPPALP-S 296
Cdd:cd06618  169 -KAKTrSAGCAAYMAPERIDPPdnpKYDIRADVWSLGISLVELATGQFPYRNCKTE------FEVLTKILNEEPPSLPpN 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 567218350 297 ENFSPELSSFISTCLQKDPNSRSSAKELMEHPFLNKYNNSEINLASYFTD 346
Cdd:cd06618  242 EGFSPDFCSFVDLCLTKDHRYRPKYRELLQHPFIRRYETAEVDVASWFQD 291
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
68-329 2.83e-61

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: 197.58  E-value: 2.83e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  68 SDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQL-----NIDEAIRksiaqELKINQSSQCPYLVNSYQSFYDNGAIS 142
Cdd:cd06610    1 DDYELIEVIGSGATAVVYAAYCLPKKEKVAIKRIDLekcqtSMDELRK-----EIQAMSQCNHPNVVSYYTSFVVGDELW 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 143 LILEYMDGGSLADFLKS---VKTIPESYLSAIFKQVLQGLIYLHHDKHIiHRDLKPSNLLINHRGEVKITDFGVS----T 215
Cdd:cd06610   76 LVMPLLSGGSLLDIMKSsypRGGLDEAIIATVLKEVLKGLEYLHSNGQI-HRDVKAGNILLGEDGSVKIADFGVSaslaT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 216 VMTNTAGLANTFVGTYNYMSPERIV-GNKYGNKSDIWSLGLVVLECATGKFPY--LPPdqeetwSSVFELmeaIVDQPPP 292
Cdd:cd06610  155 GGDRTRKVRKTFVGTPCWMAPEVMEqVRGYDFKADIWSFGITAIELATGAAPYskYPP------MKVLML---TLQNDPP 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 567218350 293 ALPSE----NFSPELSSFISTCLQKDPNSRSSAKELMEHPF 329
Cdd:cd06610  226 SLETGadykKYSKSFRKMISLCLQKDPSKRPTAEELLKHKF 266
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
69-330 5.84e-61

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: 196.61  E-value: 5.84e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  69 DLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQ-LNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYD--NGAISLIL 145
Cdd:cd08217    1 DYEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDyGKMSEKEKQQLVSEVNILRELKHPNIVRYYDRIVDraNTTLYIVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 146 EYMDGGSLADFLKSVKT----IPESYLSAIFKQVLQGLIYLHH----DKHIIHRDLKPSNLLINHRGEVKITDFGVSTVM 217
Cdd:cd08217   81 EYCEGGDLAQLIKKCKKenqyIPEEFIWKIFTQLLLALYECHNrsvgGGKILHRDLKPANIFLDSDNNVKLGDFGLARVL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 218 TNTAGLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEetwssvfELMEAIVDQPPPALPSE 297
Cdd:cd08217  161 SHDSSFAKTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAANQL-------ELAKKIKEGKFPRIPSR 233
                        250       260       270
                 ....*....|....*....|....*....|...
gi 567218350 298 nFSPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd08217  234 -YSSELNEVIKSMLNVDPDKRPSVEELLQLPLI 265
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
69-329 2.07e-60

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: 195.22  E-value: 2.07e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  69 DLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRkSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYM 148
Cdd:cd06613    1 DYELIQRIGSGTYGDVYKARNIATGELAAVKVIKLEPGDDFE-IIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVMEYC 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 149 DGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFV 228
Cdd:cd06613   80 GGGSLQDIYQVTGPLSELQIAYVCRETLKGLAYLHS-TGKIHRDIKGANILLTEDGDVKLADFGVSAQLTATIAKRKSFI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 229 GTYNYMSPERIVGNK---YGNKSDIWSLGLVVLECATGkfpyLPPdqeetwssVFEL--MEAI-----VDQPPPALPS-E 297
Cdd:cd06613  159 GTPYWMAPEVAAVERkggYDGKCDIWALGITAIELAEL----QPP--------MFDLhpMRALflipkSNFDPPKLKDkE 226
                        250       260       270
                 ....*....|....*....|....*....|..
gi 567218350 298 NFSPELSSFISTCLQKDPNSRSSAKELMEHPF 329
Cdd:cd06613  227 KWSPDFHDFIKKCLTKNPKKRPTATKLLQHPF 258
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
76-328 2.43e-60

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: 193.26  E-value: 2.43e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLAD 155
Cdd:cd00180    1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSLKD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 156 FLKS-VKTIPESYLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVG--TYN 232
Cdd:cd00180   81 LLKEnKGPLSEEEALSILRQLLSALEYLHS-NGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKTTGGttPPY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 233 YMSPERIVGNKYGNKSDIWSLGLVVLECatgkfpylppdqeetwssvfelmeaivdqpppalpsenfsPELSSFISTCLQ 312
Cdd:cd00180  160 YAPPELLGGRYYGPKVDIWSLGVILYEL----------------------------------------EELKDLIRRMLQ 199
                        250
                 ....*....|....*.
gi 567218350 313 KDPNSRSSAKELMEHP 328
Cdd:cd00180  200 YDPKKRPSAKELLEHL 215
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
71-330 2.29e-59

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: 192.90  E-value: 2.29e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  71 DMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEaiRKSIAQELKINQS-SQCPYLVNSYQSFY------DNGAISL 143
Cdd:cd06608    9 ELVEVIGEGTYGKVYKARHKKTGQLAAIKIMDIIEDE--EEEIKLEINILRKfSNHPNIATFYGAFIkkdppgGDDQLWL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 144 ILEYMDGGSLADFLKSV----KTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTN 219
Cdd:cd06608   87 VMEYCGGGSVTDLVKGLrkkgKRLKEEWIAYILRETLRGLAYLH-ENKVIHRDIKGQNILLTEEAEVKLVDFGVSAQLDS 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 220 TAGLANTFVGTYNYMSPERIVGNK-----YGNKSDIWSLGLVVLECATGKFPY--LPPDQEetwssvfelMEAIVDQPPP 292
Cdd:cd06608  166 TLGRRNTFIGTPYWMAPEVIACDQqpdasYDARCDVWSLGITAIELADGKPPLcdMHPMRA---------LFKIPRNPPP 236
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 567218350 293 ALPS-ENFSPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd06608  237 TLKSpEKWSKEFNDFISECLIKNYEQRPFTEELLEHPFI 275
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
74-330 1.30e-58

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: 190.59  E-value: 1.30e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVIQL-NIDEAIRKSIAQELKINQSSQCPYLVnsyqSFYdnGA------ISLILE 146
Cdd:cd06626    6 NKIGEGTFGKVYTAVNLDTGELMAMKEIRFqDNDPKTIKEIADEMKVLEGLDHPNLV----RYY--GVevhreeVYIFME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 147 YMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTA----- 221
Cdd:cd06626   80 YCQEGTLEELLRHGRILDEAVIRVYTLQLLEGLAYLH-ENGIVHRDIKPANIFLDSNGLIKLGDFGSAVKLKNNTttmap 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 222 GLANTFVGTYNYMSPERIVGNK---YGNKSDIWSLGLVVLECATGKFPYLPPDQEetwssvFELMEAIVDQPPPALP-SE 297
Cdd:cd06626  159 GEVNSLVGTPAYMAPEVITGNKgegHGRAADIWSLGCVVLEMATGKRPWSELDNE------WAIMYHVGMGHKPPIPdSL 232
                        250       260       270
                 ....*....|....*....|....*....|...
gi 567218350 298 NFSPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd06626  233 QLSPEGKDFLSRCLESDPKKRPTASELLDHPFI 265
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
71-331 3.69e-58

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: 189.95  E-value: 3.69e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  71 DMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNiDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDG 150
Cdd:cd06611    8 EIIGELGDGAFGKVYKAQHKETGLFAAAKIIQIE-SEEELEDFMVEIDILSECKHPNIVGLYEAYFYENKLWILIEFCDG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 151 GSLADF-LKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVG 229
Cdd:cd06611   87 GALDSImLELERGLTEPQIRYVCRQMLEALNFLH-SHKVIHRDLKAGNILLTLDGDVKLADFGVSAKNKSTLQKRDTFIG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 230 TYNYMSPERIV-----GNKYGNKSDIWSLGLVVLECATGKfpylPPDQEetwSSVFELMEAIVDQPPPAL--PSEnFSPE 302
Cdd:cd06611  166 TPYWMAPEVVAcetfkDNPYDYKADIWSLGITLIELAQME----PPHHE---LNPMRVLLKILKSEPPTLdqPSK-WSSS 237
                        250       260
                 ....*....|....*....|....*....
gi 567218350 303 LSSFISTCLQKDPNSRSSAKELMEHPFLN 331
Cdd:cd06611  238 FNDFLKSCLVKDPDDRPTAAELLKHPFVS 266
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
69-330 5.47e-58

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: 188.77  E-value: 5.47e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  69 DLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQL-NIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEY 147
Cdd:cd08529    1 DFEILNKLGKGSFGVVYKVVRKVDGRVYALKQIDIsRMSRKMREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 148 MDGGSLADFLKSVKT--IPESYLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLAN 225
Cdd:cd08529   81 AENGDLHSLIKSQRGrpLPEDQIWKFFIQTLLGLSHLHSKK-ILHRDIKSMNIFLDKGDNVKIGDLGVAKILSDTTNFAQ 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 226 TFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEetwssvfELMEAIVDQPPPALPSEnFSPELSS 305
Cdd:cd08529  160 TIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQG-------ALILKIVRGKYPPISAS-YSQDLSQ 231
                        250       260
                 ....*....|....*....|....*
gi 567218350 306 FISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd08529  232 LIDSCLTKDYRQRPDTTELLRNPSL 256
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
76-333 1.83e-55

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: 183.06  E-value: 1.83e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNIDE----AIRKSIA--QELKINQSSQcpyLVNSYQSFYDNGAISLILEYMD 149
Cdd:cd06917    9 VGRGSYGAVYRGYHVKTGRVVALKVLNLDTDDddvsDIQKEVAllSQLKLGQPKN---IIKYYGSYLKGPSLWIIMDYCE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 150 GGSLADFLKSVKtIPESYLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVG 229
Cdd:cd06917   86 GGSIRTLMRAGP-IAERYIAVIMREVLVALKFIHKDG-IIHRDIKAANILVTNTGNVKLCDFGVAASLNQNSSKRSTFVG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 230 TYNYMSPERIV-GNKYGNKSDIWSLGLVVLECATGKFPYLPPDQeetwssvFELMEAIVDQPPPALPSENFSPELSSFIS 308
Cdd:cd06917  164 TPYWMAPEVITeGKYYDTKADIWSLGITTYEMATGNPPYSDVDA-------LRAVMLIPKSKPPRLEGNGYSPLLKEFVA 236
                        250       260
                 ....*....|....*....|....*
gi 567218350 309 TCLQKDPNSRSSAKELMEHPFLNKY 333
Cdd:cd06917  237 ACLDEEPKDRLSADELLKSKWIKQH 261
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
74-329 3.36e-55

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: 181.78  E-value: 3.36e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVIQL-NIDEAIRKSIAQ---ELKINQSSQCPYLVNSYQSFYDNGAISLILEYMD 149
Cdd:cd06625    6 KLLGQGAFGQVYLCYDADTGRELAVKQVEIdPINTEASKEVKAlecEIQLLKNLQHERIVQYYGCLQDEKSLSIFMEYMP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 150 GGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTN--TAGLANTF 227
Cdd:cd06625   86 GGSVKDEIKAYGALTENVTRKYTRQILEGLAYLH-SNMIVHRDIKGANILRDSNGNVKLGDFGASKRLQTicSSTGMKSV 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 228 VGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKfpylPPdqeetWSSvFELMEA---IVDQPP-PALPSEnFSPEL 303
Cdd:cd06625  165 TGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTK----PP-----WAE-FEPMAAifkIATQPTnPQLPPH-VSEDA 233
                        250       260
                 ....*....|....*....|....*.
gi 567218350 304 SSFISTCLQKDPNSRSSAKELMEHPF 329
Cdd:cd06625  234 RDFLSLIFVRNKKQRPSAEELLSHSF 259
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
74-330 1.27e-54

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: 180.29  E-value: 1.27e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVIQLNID-----EAIrKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYM 148
Cdd:cd06632    6 QLLGSGSFGSVYEGFNGDTGDFFAVKEVSLVDDdkksrESV-KQLEQEIALLSKLRHPNIVQYYGTEREEDNLYIFLEYV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 149 DGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTaGLANTFV 228
Cdd:cd06632   85 PGGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLH-SRNTVHRDIKGANILVDTNGVVKLADFGMAKHVEAF-SFAKSFK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 229 GTYNYMSPERIV--GNKYGNKSDIWSLGLVVLECATGKFPYlppDQEETWSSVFElmeaIVDQPP-PALPsENFSPELSS 305
Cdd:cd06632  163 GSPYWMAPEVIMqkNSGYGLAVDIWSLGCTVLEMATGKPPW---SQYEGVAAIFK----IGNSGElPPIP-DHLSPDAKD 234
                        250       260
                 ....*....|....*....|....*
gi 567218350 306 FISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd06632  235 FIRLCLQRDPEDRPTASQLLEHPFV 259
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
76-326 4.40e-54

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: 178.12  E-value: 4.40e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVqhKWTGQFFALKVIQL-NIDEAIRKSIAQELKInqSSQC--PYLVNSYQSFYDNGAISLILEYMDGGS 152
Cdd:cd13999    1 IGSGSFGEVYKG--KWRGTDVAIKKLKVeDDNDELLKEFRREVSI--LSKLrhPNIVQFIGACLSPPPLCIVTEYMPGGS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 153 LADFLKSvKTIPESYLSA--IFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVGT 230
Cdd:cd13999   77 LYDLLHK-KKIPLSWSLRlkIALDIARGMNYLH-SPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKMTGVVGT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 231 YNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPY--LPPDQEetwssvfelMEAIVDQPPPALPSENFSPELSSFIS 308
Cdd:cd13999  155 PRWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFkeLSPIQI---------AAAVVQKGLRPPIPPDCPPELSKLIK 225
                        250
                 ....*....|....*...
gi 567218350 309 TCLQKDPNSRSSAKELME 326
Cdd:cd13999  226 RCWNEDPEKRPSFSEIVK 243
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
68-330 2.01e-53

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: 177.25  E-value: 2.01e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  68 SDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLnideaiRKSIAQELKINQSS-----QCPYLVNSYQSFYDNGAIS 142
Cdd:cd06648    7 SDLDNFVKIGEGSTGIVCIATDKSTGRQVAVKKMDL------RKQQRRELLFNEVVimrdyQHPNIVEMYSSYLVGDELW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 143 LILEYMDGGSLADFLKSVKtIPESYLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAG 222
Cdd:cd06648   81 VVMEFLEGGALTDIVTHTR-MNEEQIATVCRAVLKALSFLHSQG-VIHRDIKSDSILLTSDGRVKLSDFGFCAQVSKEVP 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 223 LANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYL--PPdqeetwssvFELMEAIVDQPPPALP-SENF 299
Cdd:cd06648  159 RRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFnePP---------LQAMKRIRDNEPPKLKnLHKV 229
                        250       260       270
                 ....*....|....*....|....*....|.
gi 567218350 300 SPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd06648  230 SPRLRSFLDRMLVRDPAQRATAAELLNHPFL 260
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
69-328 1.53e-52

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: 174.50  E-value: 1.53e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  69 DLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQL-NIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEY 147
Cdd:cd08530    1 DFKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLgSLSQKEREDSVNEIRLLASVNHPNIIRYKEAFLDGNRLCIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 148 MDGGSLADFL----KSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNtaGL 223
Cdd:cd08530   81 APFGDLSKLIskrkKKRRLFPEDDIWRIFIQMLRGLKALH-DQKILHRDLKSANILLSAGDLVKIGDLGISKVLKK--NL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 224 ANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEetwssvfELMEAIVDQPPPALPSeNFSPEL 303
Cdd:cd08530  158 AKTQIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQ-------ELRYKVCRGKFPPIPP-VYSQDL 229
                        250       260
                 ....*....|....*....|....*
gi 567218350 304 SSFISTCLQKDPNSRSSAKELMEHP 328
Cdd:cd08530  230 QQIIRSLLQVNPKKRPSCDKLLQSP 254
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
78-331 8.26e-51

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: 170.47  E-value: 8.26e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  78 KGSSGVVQLVQHKWTGQFFALKVIqlNIDEAIRK----SIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSL 153
Cdd:cd05579    3 RGAYGRVYLAKKKSTGDLYAIKVI--KKRDMIRKnqvdSVLAERNILSQAQNPFVVKLYYSFQGKKNLYLVMEYLPGGDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 154 ADFLKSVKTIPESYLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKITDFGVSTV-----MTNTAGLANT-- 226
Cdd:cd05579   81 YSLLENVGALDEDVARIYIAEIVLALEYLHSHG-IIHRDLKPDNILIDANGHLKLTDFGLSKVglvrrQIKLSIQKKSng 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 227 --------FVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGkfpyLPPDQEETWSSVFelmEAIV--DQPPPALPs 296
Cdd:cd05579  160 apekedrrIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVG----IPPFHAETPEEIF---QNILngKIEWPEDP- 231
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 567218350 297 eNFSPELSSFISTCLQKDPNSR---SSAKELMEHPFLN 331
Cdd:cd05579  232 -EVSDEAKDLISKLLTPDPEKRlgaKGIEEIKNHPFFK 268
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
62-333 3.81e-50

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: 169.08  E-value: 3.81e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  62 DDELSLSDLDMVkflGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAI 141
Cdd:cd06642    1 DPEELFTKLERI---GKGSFGEVYKGIDNRTKEVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYITRYYGSYLKGTKL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 142 SLILEYMDGGSLADFLKSvKTIPESYLSAIFKQVLQGLIYLHHDKHIiHRDLKPSNLLINHRGEVKITDFGVSTVMTNTA 221
Cdd:cd06642   78 WIIMEYLGGGSALDLLKP-GPLEETYIATILREILKGLDYLHSERKI-HRDIKAANVLLSEQGDVKLADFGVAGQLTDTQ 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 222 GLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPY--LPPdqeetwssvFELMEAIVDQPPPALPSENF 299
Cdd:cd06642  156 IKRNTFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNsdLHP---------MRVLFLIPKNSPPTLEGQHS 226
                        250       260       270
                 ....*....|....*....|....*....|....
gi 567218350 300 SPeLSSFISTCLQKDPNSRSSAKELMEHPFLNKY 333
Cdd:cd06642  227 KP-FKEFVEACLNKDPRFRPTAKELLKHKFITRY 259
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
74-330 8.28e-50

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: 167.73  E-value: 8.28e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVIQLN--IDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGG 151
Cdd:cd14099    7 KFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSslTKPKQREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILLELCSNG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 152 SLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVGTY 231
Cdd:cd14099   87 SLMELLKRRKALTEPEVRYFMRQILSGVKYLH-SNRIIHRDLKLGNLFLDENMNVKIGDFGLAARLEYDGERKKTLCGTP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 232 NYMSPERIVGNK-YGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSV----FElmeaivdqpppaLPSE-NFSPELSS 305
Cdd:cd14099  166 NYIAPEVLEKKKgHSFEVDIWSLGVILYTLLVGKPPFETSDVKETYKRIkkneYS------------FPSHlSISDEAKD 233
                        250       260
                 ....*....|....*....|....*
gi 567218350 306 FISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14099  234 LIRSMLQPDPTKRPSLDEILSHPFF 258
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
74-326 2.56e-49

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: 166.29  E-value: 2.56e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVIQLN--IDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGG 151
Cdd:cd08224    6 KKIGKGQFSVVYRARCLLDGRLVALKKVQIFemMDAKARQDCLKEIDLLQQLNHPNIIKYLASFIENNELNIVLELADAG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 152 SLADFLKSVKT----IPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTF 227
Cdd:cd08224   86 DLSRLIKHFKKqkrlIPERTIWKYFVQLCSALEHMH-SKRIMHRDIKPANVFITANGVVKLGDLGLGRFFSSKTTAAHSL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 228 VGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQeetwsSVFELMEAIVDQPPPALPSENFSPELSSFI 307
Cdd:cd08224  165 VGTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYGEKM-----NLYSLCKKIEKCEYPPLPADLYSQELRDLV 239
                        250
                 ....*....|....*....
gi 567218350 308 STCLQKDPNSRSSAKELME 326
Cdd:cd08224  240 AACIQPDPEKRPDISYVLD 258
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
76-330 3.06e-48

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: 164.09  E-value: 3.06e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSG-VVQLVQHKwTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLA 154
Cdd:cd06641   12 IGKGSFGeVFKGIDNR-TQKVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLGGGSAL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 155 DFLKSvKTIPESYLSAIFKQVLQGLIYLHHDKHIiHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVGTYNYM 234
Cdd:cd06641   91 DLLEP-GPLDETQIATILREILKGLDYLHSEKKI-HRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIKRN*FVGTPFWM 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 235 SPERIVGNKYGNKSDIWSLGLVVLECATGKfpylPPDQEETWSSVFELmeaIVDQPPPALPSeNFSPELSSFISTCLQKD 314
Cdd:cd06641  169 APEVIKQSAYDSKADIWSLGITAIELARGE----PPHSELHPMKVLFL---IPKNNPPTLEG-NYSKPLKEFVEACLNKE 240
                        250
                 ....*....|....*.
gi 567218350 315 PNSRSSAKELMEHPFL 330
Cdd:cd06641  241 PSFRPTAKELLKHKFI 256
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
76-330 5.34e-48

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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: 163.81  E-value: 5.34e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNIDE------AIRK-SIAQELKinqssqCPYLVNSYQSFYDNGAISLILEYM 148
Cdd:cd07829    7 LGEGTYGVVYKAKDKKTGEIVALKKIRLDNEEegipstALREiSLLKELK------HPNIVKLLDVIHTENKLYLVFEYC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 149 DGgSLADFLKSVKT-IPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFgvstvmtntaGLANTF 227
Cdd:cd07829   81 DQ-DLKKYLDKRPGpLPPNLIKSIMYQLLRGLAYCH-SHRILHRDLKPQNLLINRDGVLKLADF----------GLARAF 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 228 ----------VGTYNYMSPERIVGNK-YGNKSDIWSLGLVVLECATGKfPYLPPDQE----------------ETWSSVF 280
Cdd:cd07829  149 giplrtytheVVTLWYRAPEILLGSKhYSTAVDIWSVGCIFAELITGK-PLFPGDSEidqlfkifqilgtpteESWPGVT 227
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 567218350 281 ELMEAIVDQP--PPALPSENFS---PELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd07829  228 KLPDYKPTFPkwPKNDLEKVLPrldPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
76-346 5.63e-48

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: 163.68  E-value: 5.63e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLAD 155
Cdd:cd06640   12 IGKGSFGEVFKGIDNRTQQVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIMEYLGGGSALD 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 156 FLKSvKTIPESYLSAIFKQVLQGLIYLHHDKHIiHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVGTYNYMS 235
Cdd:cd06640   92 LLRA-GPFDEFQIATMLKEILKGLDYLHSEKKI-HRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRNTFVGTPFWMA 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 236 PERIVGNKYGNKSDIWSLGLVVLECATGKfpylPPDQEETWSSVFELmeaIVDQPPPALPSEnFSPELSSFISTCLQKDP 315
Cdd:cd06640  170 PEVIQQSAYDSKADIWSLGITAIELAKGE----PPNSDMHPMRVLFL---IPKNNPPTLVGD-FSKPFKEFIDACLNKDP 241
                        250       260       270
                 ....*....|....*....|....*....|.
gi 567218350 316 NSRSSAKELMEHPFLNKYNNSeinlASYFTD 346
Cdd:cd06640  242 SFRPTAKELLKHKFIVKNAKK----TSYLTE 268
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
76-329 9.62e-48

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: 162.01  E-value: 9.62e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVI---QLNidEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGS 152
Cdd:cd14009    1 IGRGSFATVWKGRHKQTGEVVAIKEIsrkKLN--KKLQENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGGD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 153 LADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGE---VKITDFGVSTVMtNTAGLANTFVG 229
Cdd:cd14009   79 LSQYIRKRGRLPEAVARHFMQQLASGLKFLR-SKNIIHRDLKPQNLLLSTSGDdpvLKIADFGFARSL-QPASMAETLCG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 230 TYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYlppdqeeTWSSVFELMEAI--VDQPPPALPSENFSPELSSFI 307
Cdd:cd14009  157 SPLYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPF-------RGSNHVQLLRNIerSDAVIPFPIAAQLSPDCKDLL 229
                        250       260
                 ....*....|....*....|..
gi 567218350 308 STCLQKDPNSRSSAKELMEHPF 329
Cdd:cd14009  230 RRLLRRDPAERISFEEFFAHPF 251
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
72-330 2.52e-47

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: 161.44  E-value: 2.52e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  72 MVKFLGKGSSGVVQLVQHKWTGQFFALKVIQ------LNIDEAIRKsiAQELKINQSSQCPYLVNSYQSFYDNGAISLIL 145
Cdd:cd08222    4 VVRKLGSGNFGTVYLVSDLKATADEELKVLKeisvgeLQPDETVDA--NREAKLLSKLDHPAIVKFHDSFVEKESFCIVT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 146 EYMDGGSLADFLKSVK----TIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINhRGEVKITDFGVSTVMTNTA 221
Cdd:cd08222   82 EYCEGGDLDDKISEYKksgtTIDENQILDWFIQLLLAVQYMH-ERRILHRDLKAKNIFLK-NNVIKVGDFGISRILMGTS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 222 GLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYlppdqeeTWSSVFELMEAIVDQPPPALPsENFSP 301
Cdd:cd08222  160 DLATTFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAF-------DGQNLLSVMYKIVEGETPSLP-DKYSK 231
                        250       260
                 ....*....|....*....|....*....
gi 567218350 302 ELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd08222  232 ELNAIYSRMLNKDPALRPSAAEILKIPFI 260
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
69-330 2.59e-47

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: 161.05  E-value: 2.59e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  69 DLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVI---QLNIDEaiRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLIL 145
Cdd:cd08220    1 KYEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIpveQMTKEE--RQAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 146 EYMDGGSLADFLKSVKT--IPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLIN-HRGEVKITDFGVSTVMtNTAG 222
Cdd:cd08220   79 EYAPGGTLFEYIQQRKGslLSEEEILHFFVQILLALHHVH-SKQILHRDLKTQNILLNkKRTVVKIGDFGISKIL-SSKS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 223 LANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYlppDQEETWSSVFELMEAIVDQpppalPSENFSPE 302
Cdd:cd08220  157 KAYTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAF---EAANLPALVLKIMRGTFAP-----ISDRYSEE 228
                        250       260
                 ....*....|....*....|....*...
gi 567218350 303 LSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd08220  229 LRHLILSMLHLDPNKRPTLSEIMAQPII 256
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
71-337 7.53e-47

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: 160.97  E-value: 7.53e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  71 DMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAqELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDG 150
Cdd:cd06644   15 EIIGELGDGAFGKVYKAKNKETGALAAAKVIETKSEEELEDYMV-EIEILATCNHPYIVKLLGAFYWDGKLWIMIEFCPG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 151 GSL-ADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVG 229
Cdd:cd06644   94 GAVdAIMLELDRGLTEPQIQVICRQMLEALQYLH-SMKIIHRDLKAGNVLLTLDGDIKLADFGVSAKNVKTLQRRDSFIG 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 230 TYNYMSPERIV-----GNKYGNKSDIWSLGLVVLECATGKfpylPPDQEETWSSVfeLMEAIVDQPPPALPSENFSPELS 304
Cdd:cd06644  173 TPYWMAPEVVMcetmkDTPYDYKADIWSLGITLIEMAQIE----PPHHELNPMRV--LLKIAKSEPPTLSQPSKWSMEFR 246
                        250       260       270
                 ....*....|....*....|....*....|...
gi 567218350 305 SFISTCLQKDPNSRSSAKELMEHPFLNKYNNSE 337
Cdd:cd06644  247 DFLKTALDKHPETRPSAAQLLEHPFVSSVTSNR 279
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
76-334 1.16e-46

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


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 159.70  E-value: 1.16e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLN--IDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSL 153
Cdd:cd05572    1 LGVGGFGRVELVQLKSKGRTFALKCVKKRhiVQTRQQEHIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLGGEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 154 ADFLKSVKTIPESYLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGlANTFVGTYNY 233
Cdd:cd05572   81 WTILRDRGLFDEYTARFYTACVVLAFEYLHS-RGIIYRDLKPENLLLDSNGYVKLVDFGFAKKLGSGRK-TWTFCGTPEY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 234 MSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEEtwssvFELMEAIVDQPPPALPSENFSPELSSFISTCLQK 313
Cdd:cd05572  159 VAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFGGDDEDP-----MKIYNIILKGIDKIEFPKYIDKNAKNLIKQLLRR 233
                        250       260
                 ....*....|....*....|....*.
gi 567218350 314 DP-----NSRSSAKELMEHPFLNKYN 334
Cdd:cd05572  234 NPeerlgYLKGGIRDIKKHKWFEGFD 259
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
74-330 1.80e-46

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: 159.47  E-value: 1.80e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIR---------KSIAQELKINQSSQCPYLVnSYQSFYD-NGAISL 143
Cdd:cd06629    7 ELIGKGTYGRVYLAMNATTGEMLAVKQVELPKTSSDRadsrqktvvDALKSEIDTLKDLDHPNIV-QYLGFEEtEDYFSI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 144 ILEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAG- 222
Cdd:cd06629   86 FLEYVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLH-SKGILHRDLKADNILVDLEGICKISDFGISKKSDDIYGn 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 223 -LANTFVGTYNYMSPERI--VGNKYGNKSDIWSLGLVVLECATGKFPYlppDQEETWSSVFELMEAivDQPPPALPSENF 299
Cdd:cd06629  165 nGATSMQGSVFWMAPEVIhsQGQGYSAKVDIWSLGCVVLEMLAGRRPW---SDDEAIAAMFKLGNK--RSAPPVPEDVNL 239
                        250       260       270
                 ....*....|....*....|....*....|.
gi 567218350 300 SPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd06629  240 SPEALDFLNACFAIDPRDRPTAAELLSHPFL 270
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
77-330 1.93e-46

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: 158.96  E-value: 1.93e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  77 GKGSSGVVQLVQHKWTGQFFALKVIqlNIDEAIRK----SIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGS 152
Cdd:cd05578    9 GKGSFGKVCIVQKKDTKKMFAMKYM--NKQKCIEKdsvrNVLNELEILQELEHPFLVNLWYSFQDEEDMYMVVDLLLGGD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 153 LADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAgLANTFVGTYN 232
Cdd:cd05578   87 LRYHLQQKVKFSEETVKFYICEIVLALDYLH-SKNIIHRDIKPDNILLDEQGHVHITDFNIATKLTDGT-LATSTSGTKP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 233 YMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYlpPDQEETWSSVFELMEAIVDQPPPALpsenFSPELSSFISTCLQ 312
Cdd:cd05578  165 YMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPY--EIHSRTSIEEIRAKFETASVLYPAG----WSEEAIDLINKLLE 238
                        250
                 ....*....|....*....
gi 567218350 313 KDPNSR-SSAKELMEHPFL 330
Cdd:cd05578  239 RDPQKRlGDLSDLKNHPYF 257
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
69-329 2.58e-46

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


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 158.79  E-value: 2.58e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  69 DLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVI---QLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLIL 145
Cdd:cd14098    1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIvkrKVAGNDKNLQLFQREINILKSLEHPGIVRLIDWYEDDQHIYLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 146 EYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLhHDKHIIHRDLKPSNLLINHRGE--VKITDFGVSTVmTNTAGL 223
Cdd:cd14098   81 EYVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYT-HSMGITHRDLKPENILITQDDPviVKISDFGLAKV-IHTGTF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 224 ANTFVGTYNYMSPERIVG------NKYGNKSDIWSLGLVVLECATGkfpYLPPDQeetwSSVFELMEAIVD----QPPpa 293
Cdd:cd14098  159 LVTFCGTMAYLAPEILMSkeqnlqGGYSNLVDMWSVGCLVYVMLTG---ALPFDG----SSQLPVEKRIRKgrytQPP-- 229
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 567218350 294 LPSENFSPELSSFISTCLQKDPNSRSSAKELMEHPF 329
Cdd:cd14098  230 LVDFNISEEAIDFILRLLDVDPEKRMTAAQALDHPW 265
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
73-330 1.40e-45

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: 156.24  E-value: 1.40e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  73 VKFLGKGSSGVVQLVQHKWTGQFFALKVIQLniDEAIRKSIAQELKI----NQSSQCPYLVNSYQSFYDNGA--ISLILE 146
Cdd:cd05118    4 LRKIGEGAFGTVWLARDKVTGEKVAIKKIKN--DFRHPKAALREIKLlkhlNDVEGHPNIVKLLDVFEHRGGnhLCLVFE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 147 YMdGGSLADFLK-SVKTIPESYLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLINH-RGEVKITDFGVSTVMTNtaGLA 224
Cdd:cd05118   82 LM-GMNLYELIKdYPRGLPLDLIKSYLYQLLQALDFLHSNG-IIHRDLKPENILINLeLGQLKLADFGLARSFTS--PPY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 225 NTFVGTYNYMSPERIVGNK-YGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFELMEaivdqpppalpsenfSPEL 303
Cdd:cd05118  158 TPYVATRWYRAPEVLLGAKpYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIVRLLG---------------TPEA 222
                        250       260
                 ....*....|....*....|....*..
gi 567218350 304 SSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd05118  223 LDLLSKMLKYDPAKRITASQALAHPYF 249
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
58-330 4.36e-45

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: 156.68  E-value: 4.36e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  58 IKPADDELSLSDLdmVKfLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAiRKSIAQELKINQSSQCPYLVNSYQSFYD 137
Cdd:cd06659   14 VDQGDPRQLLENY--VK-IGEGSTGVVCIAREKHSGRQVAVKMMDLRKQQR-RELLFNEVVIMRDYQHPNVVEMYKSYLV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 138 NGAISLILEYMDGGSLADFLKSVKtIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVM 217
Cdd:cd06659   90 GEELWVLMEYLQGGALTDIVSQTR-LNEEQIATVCEAVLQALAYLH-SQGVIHRDIKSDSILLTLDGRVKLSDFGFCAQI 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 218 TNTAGLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPpdqeetwSSVFELMEAIVDQPPPALP-S 296
Cdd:cd06659  168 SKDVPKRKSLVGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFS-------DSPVQAMKRLRDSPPPKLKnS 240
                        250       260       270
                 ....*....|....*....|....*....|....
gi 567218350 297 ENFSPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd06659  241 HKASPVLRDFLERMLVRDPQERATAQELLDHPFL 274
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
76-330 5.75e-45

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: 155.09  E-value: 5.75e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKviQLNIDEAIRKS-IAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLA 154
Cdd:cd06647   15 IGQGASGTVYTAIDVATGQEVAIK--QMNLQQQPKKElIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 155 DFLKSVkTIPESYLSAIFKQVLQGLIYLHHDkHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVGTYNYM 234
Cdd:cd06647   93 DVVTET-CMDEGQIAAVCRECLQALEFLHSN-QVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWM 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 235 SPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLppdQEETWSSVFelmeAIVDQPPPALPS-ENFSPELSSFISTCLQK 313
Cdd:cd06647  171 APEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYL---NENPLRALY----LIATNGTPELQNpEKLSAIFRDFLNRCLEM 243
                        250
                 ....*....|....*..
gi 567218350 314 DPNSRSSAKELMEHPFL 330
Cdd:cd06647  244 DVEKRGSAKELLQHPFL 260
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
71-337 5.87e-45

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: 155.96  E-value: 5.87e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  71 DMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAqELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDG 150
Cdd:cd06643    8 EIVGELGDGAFGKVYKAQNKETGILAAAKVIDTKSEEELEDYMV-EIDILASCDHPNIVKLLDAFYYENNLWILIEFCAG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 151 GSL-ADFLKSVKTIPESYLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVG 229
Cdd:cd06643   87 GAVdAVMLELERPLTEPQIRVVCKQTLEALVYLHENK-IIHRDLKAGNILFTLDGDIKLADFGVSAKNTRTLQRRDSFIG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 230 TYNYMSPERIV-----GNKYGNKSDIWSLGLVVLECATGKfpylPPDQEETWSSVfeLMEAIVDQPPPALPSENFSPELS 304
Cdd:cd06643  166 TPYWMAPEVVMcetskDRPYDYKADVWSLGVTLIEMAQIE----PPHHELNPMRV--LLKIAKSEPPTLAQPSRWSPEFK 239
                        250       260       270
                 ....*....|....*....|....*....|...
gi 567218350 305 SFISTCLQKDPNSRSSAKELMEHPFLNKYNNSE 337
Cdd:cd06643  240 DFLRKCLEKNVDARWTTSQLLQHPFVSVLVSNK 272
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
76-330 6.95e-45

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: 155.00  E-value: 6.95e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQL---NIDEAIRK-----SIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEY 147
Cdd:cd06628    8 IGSGSFGSVYLGMNASSGELMAVKQVELpsvSAENKDRKksmldALQREIALLRELQHENIVQYLGSSSDANHLNIFLEY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 148 MDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVS------TVMTNTA 221
Cdd:cd06628   88 VPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLH-NRGIIHRDIKGANILVDNKGGIKISDFGISkkleanSLSTKNN 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 222 GLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEEtwsSVFELMEAIVDQPPPalpseNFSP 301
Cdd:cd06628  167 GARPSLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFPDCTQMQ---AIFKIGENASPTIPS-----NISS 238
                        250       260
                 ....*....|....*....|....*....
gi 567218350 302 ELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd06628  239 EARDFLEKTFEIDHNKRPTADELLKHPFL 267
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
70-335 2.27e-44

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: 154.88  E-value: 2.27e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  70 LDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEaiRKSIAQELK-INQSSQCPYLVNSYQSFYD------NGAIS 142
Cdd:cd06637    8 FELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDVTGDE--EEEIKQEINmLKKYSHHRNIATYYGAFIKknppgmDDQLW 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 143 LILEYMDGGSLADFLKSVK--TIPESYLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNT 220
Cdd:cd06637   86 LVMEFCGAGSVTDLIKNTKgnTLKEEWIAYICREILRGLSHLHQHK-VIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 221 AGLANTFVGTYNYMSPERIVGNK-----YGNKSDIWSLGLVVLECATGKFPYLppdQEETWSSVFelmeAIVDQPPPALP 295
Cdd:cd06637  165 VGRRNTFIGTPYWMAPEVIACDEnpdatYDFKSDLWSLGITAIEMAEGAPPLC---DMHPMRALF----LIPRNPAPRLK 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 567218350 296 SENFSPELSSFISTCLQKDPNSRSSAKELMEHPFLNKYNN 335
Cdd:cd06637  238 SKKWSKKFQSFIESCLVKNHSQRPSTEQLMKHPFIRDQPN 277
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
72-330 4.43e-44

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: 152.79  E-value: 4.43e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  72 MVKFLGKGSSGVVQLVQHKWTGQFFALKVI--QLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMD 149
Cdd:cd14081    5 LGKTLGKGQTGLVKLAKHCVTGQKVAIKIVnkEKLSKESVLMKVEREIAIMKLIEHPNVLKLYDVYENKKYLYLVLEYVS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 150 GGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAgLANTFVG 229
Cdd:cd14081   85 GGELFDYLVKKGRLTEKEARKFFRQIISALDYCHS-HSICHRDLKPENLLLDEKNNIKIADFGMASLQPEGS-LLETSCG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 230 TYNYMSPERIVGNKY-GNKSDIWSLGLVVLECATGKFPYlppDQEetwsSVFELMEAiVDQPPPALPSeNFSPELSSFIS 308
Cdd:cd14081  163 SPHYACPEVIKGEKYdGRKADIWSCGVILYALLVGALPF---DDD----NLRQLLEK-VKRGVFHIPH-FISPDAQDLLR 233
                        250       260
                 ....*....|....*....|..
gi 567218350 309 TCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14081  234 RMLEVNPEKRITIEEIKKHPWF 255
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
76-330 5.31e-44

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: 152.59  E-value: 5.31e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQ--LVQhkwTGQFFALKVIQLNIDEAIR-----KSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYM 148
Cdd:cd06631    9 LGKGAYGTVYcgLTS---TGQLIAVKQVELDTSDKEKaekeyEKLQEEVDLLKTLKHVNIVGYLGTCLEDNVVSIFMEFV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 149 DGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFG-------VSTVMTNtA 221
Cdd:cd06631   86 PGGSIASILARFGALEEPVFCRYTKQILEGVAYLH-NNNVIHRDIKGNNIMLMPNGVIKLIDFGcakrlciNLSSGSQ-S 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 222 GLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKfpylPPdqeetWSSVfELMEAIV-----DQPPPALPs 296
Cdd:cd06631  164 QLLKSMRGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGK----PP-----WADM-NPMAAIFaigsgRKPVPRLP- 232
                        250       260       270
                 ....*....|....*....|....*....|....
gi 567218350 297 ENFSPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd06631  233 DKFSPEARDFVHACLTRDQDERPSAEQLLKHPFI 266
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
68-332 8.70e-44

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


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 154.75  E-value: 8.70e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  68 SDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIqlnideaiRKSIAqeLKINQSS------------QCPYLVNSYQSF 135
Cdd:cd05573    1 DDFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKIL--------RKSDM--LKREQIAhvraerdiladaDSPWIVRLHYAF 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 136 YDNGAISLILEYMDGGSLADFLKSVKTIPES----YLSAIfkqVLQgliyLH--HDKHIIHRDLKPSNLLINHRGEVKIT 209
Cdd:cd05573   71 QDEDHLYLVMEYMPGGDLMNLLIKYDVFPEEtarfYIAEL---VLA----LDslHKLGFIHRDIKPDNILLDADGHIKLA 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 210 DFGVSTVM-----------------------------TNTAGLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLEC 260
Cdd:cd05573  144 DFGLCTKMnksgdresylndsvntlfqdnvlarrrphKQRRVRAYSAVGTPDYIAPEVLRGTGYGPECDWWSLGVILYEM 223
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 567218350 261 ATGKFPYLPPDQEETWSSVFELMEAIVdqpppaLPSEN-FSPELSSFISTCLqKDPNSR-SSAKELMEHPFLNK 332
Cdd:cd05573  224 LYGFPPFYSDSLVETYSKIMNWKESLV------FPDDPdVSPEAIDLIRRLL-CDPEDRlGSAEEIKAHPFFKG 290
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
69-329 8.88e-44

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: 152.94  E-value: 8.88e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  69 DLDMVKFLGKGSSGVVQLVQHKWTGQFFALKviQLNIDEAIR----KSIAQELKINQSSQCPYLVNSYQSFYDNGAISLI 144
Cdd:cd14209    2 DFDRIKTLGTGSFGRVMLVRHKETGNYYAMK--ILDKQKVVKlkqvEHTLNEKRILQAINFPFLVKLEYSFKDNSNLYMV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 145 LEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLINHRGEVKITDFGVST-VMTNTAgl 223
Cdd:cd14209   80 MEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHS-LDLIYRDLKPENLLIDQQGYIKVTDFGFAKrVKGRTW-- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 224 anTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPpdqeetwSSVFELMEAIVdQPPPALPSeNFSPEL 303
Cdd:cd14209  157 --TLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFA-------DQPIQIYEKIV-SGKVRFPS-HFSSDL 225
                        250       260       270
                 ....*....|....*....|....*....|.
gi 567218350 304 SSFISTCLQKD-----PNSRSSAKELMEHPF 329
Cdd:cd14209  226 KDLLRNLLQVDltkrfGNLKNGVNDIKNHKW 256
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
64-330 9.57e-44

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: 154.80  E-value: 9.57e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  64 ELSLSDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAiRKSIAQELKIN---QSSQCPYLVNSYQSFYDNGA 140
Cdd:cd05594   21 KVTMNDFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVA-KDEVAHTLTENrvlQNSRHPFLTALKYSFQTHDR 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 141 ISLILEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNT 220
Cdd:cd05594  100 LCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKD 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 221 AGLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVfeLMEAIvdQPPPALpsenfS 300
Cdd:cd05594  180 GATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELI--LMEEI--RFPRTL-----S 250
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 567218350 301 PELSSFISTCLQKDPNSR-----SSAKELMEHPFL 330
Cdd:cd05594  251 PEAKSLLSGLLKKDPKQRlgggpDDAKEIMQHKFF 285
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
63-330 9.78e-44

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: 152.47  E-value: 9.78e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  63 DELSLSDL-------DMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEaiRKSIAQELK-INQSSQCPYLVNSYQS 134
Cdd:cd06636    4 DDIDLSALrdpagifELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDE--EEEIKLEINmLKKYSHHRNIATYYGA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 135 FY------DNGAISLILEYMDGGSLADFLKSVK--TIPESYLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLINHRGEV 206
Cdd:cd06636   82 FIkksppgHDDQLWLVMEFCGAGSVTDLVKNTKgnALKEDWIAYICREILRGLAHLHA-HKVIHRDIKGQNVLLTENAEV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 207 KITDFGVSTVMTNTAGLANTFVGTYNYMSPERIVGNK-----YGNKSDIWSLGLVVLECATGKFPYLppdQEETWSSVFe 281
Cdd:cd06636  161 KLVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEMAEGAPPLC---DMHPMRALF- 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 567218350 282 lmeAIVDQPPPALPSENFSPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd06636  237 ---LIPRNPPPKLKSKKWSKKFIDFIEGCLVKNYLSRPSTEQLLKHPFI 282
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
76-330 1.30e-43

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: 151.61  E-value: 1.30e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLN-IDEAIRKSIAQELKINQSSQCPYLVNSYQSFYD--NGAISLILEYMDGGS 152
Cdd:cd13983    9 LGRGSFKTVYRAFDTEEGIEVAWNEIKLRkLPKAERQRFKQEIEILKSLKHPNIIKFYDSWESksKKEVIFITELMTSGT 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 153 LADFLKSVKTIPESYLSAIFKQVLQGLIYLH-HDKHIIHRDLKPSNLLIN-HRGEVKITDFGVSTVMtnTAGLANTFVGT 230
Cdd:cd13983   89 LKQYLKRFKRLKLKVIKSWCRQILEGLNYLHtRDPPIIHRDLKCDNIFINgNTGEVKIGDLGLATLL--RQSFAKSVIGT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 231 YNYMSPErIVGNKYGNKSDIWSLGLVVLECATGKFPYlppdqeETWSSVFELMEAIVDQPPPALPSENFSPELSSFISTC 310
Cdd:cd13983  167 PEFMAPE-MYEEHYDEKVDIYAFGMCLLEMATGEYPY------SECTNAAQIYKKVTSGIKPESLSKVKDPELKDFIEKC 239
                        250       260
                 ....*....|....*....|
gi 567218350 311 LQKdPNSRSSAKELMEHPFL 330
Cdd:cd13983  240 LKP-PDERPSARELLEHPFF 258
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
73-334 1.45e-43

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: 151.48  E-value: 1.45e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  73 VKFLGKGSSGVVQLVQHKWTGQFFALKVIQ---LNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMD 149
Cdd:cd05611    1 LKPISKGAFGSVYLAKKRSTGDYFAIKVLKksdMIAKNQVTNVKAERAIMMIQGESPYVAKLYYSFQSKDYLYLVMEYLN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 150 GGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVmtntaGLAN---- 225
Cdd:cd05611   81 GGDCASLIKTLGGLPEDWAKQYIAEVVLGVEDLH-QRGIIHRDIKPENLLIDQTGHLKLTDFGLSRN-----GLEKrhnk 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 226 TFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGkfpyLPPDQEETWSSVFELMEAIVDQpPPALPSENFSPELSS 305
Cdd:cd05611  155 KFVGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFG----YPPFHAETPDAVFDNILSRRIN-WPEEVKEFCSPEAVD 229
                        250       260       270
                 ....*....|....*....|....*....|..
gi 567218350 306 FISTCLQKDPNSRSSAK---ELMEHPFLNKYN 334
Cdd:cd05611  230 LINRLLCMDPAKRLGANgyqEIKSHPFFKSIN 261
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
69-330 2.45e-43

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: 150.66  E-value: 2.45e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  69 DLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQL-NIDEAIRKSIAQELKINQSSQCPYLVNSYQSF-YDNGAISLILE 146
Cdd:cd08223    1 EYQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLkNASKRERKAAEQEAKLLSKLKHPNIVSYKESFeGEDGFLYIVMG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 147 YMDGGSLADFLKSVKTIP--ESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLA 224
Cdd:cd08223   81 FCEGGDLYTRLKEQKGVLleERQVVEWFVQIAMALQYMH-ERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLESSSDMA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 225 NTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEetwSSVFELMEAIVdqppPALPSEnFSPELS 304
Cdd:cd08223  160 TTLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMN---SLVYKILEGKL----PPMPKQ-YSPELG 231
                        250       260
                 ....*....|....*....|....*.
gi 567218350 305 SFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd08223  232 ELIKAMLHQDPEKRPSVKRILRQPYI 257
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
77-330 4.67e-43

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: 149.71  E-value: 4.67e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  77 GKGSSGVVQLVQHKWTGQFFALKVI-QLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGgSLAD 155
Cdd:cd14002   10 GEGSFGKVYKGRRKYTGQVVALKFIpKRGKSEKELRNLRQEIEILRKLNHPNIIEMLDSFETKKEFVVVTEYAQG-ELFQ 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 156 FLKSVKTIPESYLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVGTYNYMS 235
Cdd:cd14002   89 ILEDDGTLPEEEVRSIAKQLVSALHYLHSNR-IIHRDMKPQNILIGKGGVVKLCDFGFARAMSCNTLVLTSIKGTPLYMA 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 236 PERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPpdqeetwSSVFELMEAIVDQPPPaLPSeNFSPELSSFISTCLQKDP 315
Cdd:cd14002  168 PELVQEQPYDHTADLWSLGCILYELFVGQPPFYT-------NSIYQLVQMIVKDPVK-WPS-NMSPEFKSFLQGLLNKDP 238
                        250
                 ....*....|....*
gi 567218350 316 NSRSSAKELMEHPFL 330
Cdd:cd14002  239 SKRLSWPDLLEHPFV 253
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
68-329 7.52e-43

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: 150.06  E-value: 7.52e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  68 SDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVI--QLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLIL 145
Cdd:cd05581    1 NDFKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLdkRHIIKEKKVKYVTIEKEVLSRLAHPGIVKLYYTFQDESKLYFVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 146 EYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGL-- 223
Cdd:cd05581   81 EYAPNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLH-SKGIIHRDLKPENILLDEDMHIKITDFGTAKVLGPDSSPes 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 224 ---------------ANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYlppdqeeTWSSVFELMEAIV- 287
Cdd:cd05581  160 tkgdadsqiaynqarAASFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPF-------RGSNEYLTFQKIVk 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 567218350 288 ---DQPPpalpseNFSPELSSFISTCLQKDPNSR------SSAKELMEHPF 329
Cdd:cd05581  233 leyEFPE------NFPPDAKDLIQKLLVLDPSKRlgvnenGGYDELKAHPF 277
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
76-328 1.19e-42

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: 148.57  E-value: 1.19e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIqlNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLAD 155
Cdd:cd14006    1 LGRGRFGVVKRCIEKATGREFAAKFI--PKRDKKKEAVLREISILNQLQHPRIIQLHEAYESPTELVLILELCSGGELLD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 156 FLKSVKTIPESYLSAIFKQVLQGLIYLhHDKHIIHRDLKPSNLLINHRGE--VKITDFGVSTVMtNTAGLANTFVGTYNY 233
Cdd:cd14006   79 RLAERGSLSEEEVRTYMRQLLEGLQYL-HNHHILHLDLKPENILLADRPSpqIKIIDFGLARKL-NPGEELKEIFGTPEF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 234 MSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVfelMEAIVDQPPPAlpSENFSPELSSFISTCLQK 313
Cdd:cd14006  157 VAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANI---SACRVDFSEEY--FSSVSQEAKDFIRKLLVK 231
                        250
                 ....*....|....*
gi 567218350 314 DPNSRSSAKELMEHP 328
Cdd:cd14006  232 EPRKRPTAQEALQHP 246
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
92-328 1.47e-42

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: 149.12  E-value: 1.47e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  92 TGQFFALKVI---------QLNIDEAIRKSIAQELKINQssqcPYLVNSYQSFYDNGAISLILEYMDGGSLADFLKSVKT 162
Cdd:cd06630   24 TGTLMAVKQVsfcrnssseQEEVVEAIREEIRMMARLNH----PNIVRMLGATQHKSHFNIFVEWMAGGSVASLLSKYGA 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 163 IPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGE-VKITDFGVSTVMTNTAGLANTF----VGTYNYMSPE 237
Cdd:cd06630  100 FSENVIINYTLQILRGLAYLH-DNQIIHRDLKGANLLVDSTGQrLRIADFGAAARLASKGTGAGEFqgqlLGTIAFMAPE 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 238 RIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFELMEAivdQPPPALPsENFSPELSSFISTCLQKDPNS 317
Cdd:cd06630  179 VLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEKISNHLALIFKIASA---TTPPPIP-EHLSPGLRDVTLRCLELQPED 254
                        250
                 ....*....|.
gi 567218350 318 RSSAKELMEHP 328
Cdd:cd06630  255 RPPARELLKHP 265
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
76-330 1.95e-42

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: 149.49  E-value: 1.95e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKviQLNIDEAIRKS-IAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLA 154
Cdd:cd06656   27 IGQGASGTVYTAIDIATGQEVAIK--QMNLQQQPKKElIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 155 DFLKSVkTIPESYLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVGTYNYM 234
Cdd:cd06656  105 DVVTET-CMDEGQIAAVCRECLQALDFLHSNQ-VIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWM 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 235 SPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLppdQEETWSSVFELMeaiVDQPPPALPSENFSPELSSFISTCLQKD 314
Cdd:cd06656  183 APEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYL---NENPLRALYLIA---TNGTPELQNPERLSAVFRDFLNRCLEMD 256
                        250
                 ....*....|....*.
gi 567218350 315 PNSRSSAKELMEHPFL 330
Cdd:cd06656  257 VDRRGSAKELLQHPFL 272
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
74-334 2.21e-42

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: 150.16  E-value: 2.21e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAiRKSIAQ---ELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDG 150
Cdd:cd05595    1 KLLGKGTFGKVILVREKATGRYYAMKILRKEVIIA-KDEVAHtvtESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 151 GSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVGT 230
Cdd:cd05595   80 GELFFHLSRERVFTEDRARFYGAEIVSALEYLH-SRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGITDGATMKTFCGT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 231 YNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVfeLMEAIvdqpppALPsENFSPELSSFISTC 310
Cdd:cd05595  159 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELI--LMEEI------RFP-RTLSPEAKSLLAGL 229
                        250       260
                 ....*....|....*....|....*....
gi 567218350 311 LQKDPNSR-----SSAKELMEHPFLNKYN 334
Cdd:cd05595  230 LKKDPKQRlgggpSDAKEVMEHRFFLSIN 258
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
73-330 3.88e-42

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: 147.65  E-value: 3.88e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  73 VKFLGKGSSGVVQLVQHKWTGQFFALKVIQLN-IDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGG 151
Cdd:cd08218    5 IKKIGEGSFGKALLVKSKEDGKQYVIKEINISkMSPKEREESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDYCDGG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 152 SLADFLKSVKTI--PESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVG 229
Cdd:cd08218   85 DLYKRINAQRGVlfPEDQILDWFVQLCLALKHVH-DRKILHRDIKSQNIFLTKDGIIKLGDFGIARVLNSTVELARTCIG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 230 TYNYMSPErIVGNK-YGNKSDIWSLGLVVLECATGKFPYlppdqeeTWSSVFELMEAIVDQPPPALPSEnFSPELSSFIS 308
Cdd:cd08218  164 TPYYLSPE-ICENKpYNNKSDIWALGCVLYEMCTLKHAF-------EAGNMKNLVLKIIRGSYPPVPSR-YSYDLRSLVS 234
                        250       260
                 ....*....|....*....|..
gi 567218350 309 TCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd08218  235 QLFKRNPRDRPSINSILEKPFI 256
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
74-330 4.34e-42

Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle 1 (also called TTK); Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TTK/Mps1 is a spindle checkpoint kinase that was first discovered due to its necessity in centrosome duplication in budding yeast. It was later found to function in the spindle assembly checkpoint, which monitors the proper attachment of chromosomes to the mitotic spindle. In yeast, substrates of Mps1 include the spindle pole body components Spc98p, Spc110p, and Spc42p. The TTK/Mps1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 147.75  E-value: 4.34e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKwTGQFFALKVIQL-NIDEAIRKSIAQELKI-NQSSQCPYLVN--SYQSFYDNGAISLILEYMD 149
Cdd:cd14131    7 KQLGKGGSSKVYKVLNP-KKKIYALKRVDLeGADEQTLQSYKNEIELlKKLKGSDRIIQlyDYEVTDEDDYLYMVMECGE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 150 GgSLADFLKS--VKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINhRGEVKITDFGVSTVMTN--TAGLAN 225
Cdd:cd14131   86 I-DLATILKKkrPKPIDPNFIRYYWKQMLEAVHTIH-EEGIVHSDLKPANFLLV-KGRLKLIDFGIAKAIQNdtTSIVRD 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 226 TFVGTYNYMSPERIVGN----------KYGNKSDIWSLGLVVLECATGKFPYlppdQEetWSSVFELMEAIVDqPPPALP 295
Cdd:cd14131  163 SQVGTLNYMSPEAIKDTsasgegkpksKIGRPSDVWSLGCILYQMVYGKTPF----QH--ITNPIAKLQAIID-PNHEIE 235
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 567218350 296 SENFS-PELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14131  236 FPDIPnPDLIDVMKRCLQRDPKKRPSIPELLNHPFL 271
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
76-330 5.88e-42

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: 147.55  E-value: 5.88e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVI-QLNIDEAirKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLA 154
Cdd:cd06624   16 LGKGTFGVVYAARDLSTQVRIAIKEIpERDSREV--QPLHEEIALHSRLSHKNIVQYLGSVSEDGFFKIFMEQVPGGSLS 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 155 DFLKSvKTIP----ESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLIN-HRGEVKITDFGVSTVMtntAGL---ANT 226
Cdd:cd06624   94 ALLRS-KWGPlkdnENTIGYYTKQILEGLKYLH-DNKIVHRDIKGDNVLVNtYSGVVKISDFGTSKRL---AGInpcTET 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 227 FVGTYNYMSPERI-VGNK-YGNKSDIWSLGLVVLECATGKFPYLppDQEETWSSVFEL-MEAIvdqpPPALPsENFSPEL 303
Cdd:cd06624  169 FTGTLQYMAPEVIdKGQRgYGPPADIWSLGCTIIEMATGKPPFI--ELGEPQAAMFKVgMFKI----HPEIP-ESLSEEA 241
                        250       260
                 ....*....|....*....|....*..
gi 567218350 304 SSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd06624  242 KSFILRCFEPDPDKRATASDLLQDPFL 268
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
76-330 6.80e-42

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: 148.33  E-value: 6.80e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKviQLNIDEAIRKS-IAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLA 154
Cdd:cd06655   27 IGQGASGTVFTAIDVATGQEVAIK--QINLQKQPKKElIINEILVMKELKNPNIVNFLDSFLVGDELFVVMEYLAGGSLT 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 155 DFLKSVkTIPESYLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVGTYNYM 234
Cdd:cd06655  105 DVVTET-CMDEAQIAAVCRECLQALEFLHANQ-VIHRDIKSDNVLLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWM 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 235 SPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLppdQEETWSSVFELMeaiVDQPPPALPSENFSPELSSFISTCLQKD 314
Cdd:cd06655  183 APEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYL---NENPLRALYLIA---TNGTPELQNPEKLSPIFRDFLNRCLEMD 256
                        250
                 ....*....|....*.
gi 567218350 315 PNSRSSAKELMEHPFL 330
Cdd:cd06655  257 VEKRGSAKELLQHPFL 272
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
76-329 9.84e-42

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


Pssm-ID: 270832 [Multi-domain]  Cd Length: 291  Bit Score: 147.33  E-value: 9.84e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQL-NIDE-----AIRksiaqELKINQSSQCPYLVN------SYQSFYDNGAISL 143
Cdd:cd07840    7 IGEGTYGQVYKARNKKTGELVALKKIRMeNEKEgfpitAIR-----EIKLLQKLDHPNVVRlkeivtSKGSAKYKGSIYM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 144 ILEYMDGgSLADFL--KSVK-TIPEsyLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNT 220
Cdd:cd07840   82 VFEYMDH-DLTGLLdnPEVKfTESQ--IKCYMKQLLEGLQYLHS-NGILHRDIKGSNILINNDGVLKLADFGLARPYTKE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 221 AGLANTF-VGTYNYMSPERIVG-NKYGNKSDIWSLGLVVLECATGKfPYLP----PDQ------------EETWSSVFEL 282
Cdd:cd07840  158 NNADYTNrVITLWYRPPELLLGaTRYGPEVDMWSVGCILAELFTGK-PIFQgkteLEQlekifelcgsptEENWPGVSDL 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 567218350 283 MEAIVDQPPPALPS-------ENFSPELSSFISTCLQKDPNSRSSAKELMEHPF 329
Cdd:cd07840  237 PWFENLKPKKPYKRrlrevfkNVIDPSALDLLDKLLTLDPKKRISADQALQHEY 290
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
74-329 1.23e-41

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: 148.13  E-value: 1.23e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVIQ---LNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDG 150
Cdd:cd05570    1 KVLGKGSFGKVMLAERKKTDELYAIKVLKkevIIEDDDVECTMTEKRVLALANRHPFLTGLHACFQTEDRLYFVMEYVNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 151 GSLADFLKSVKTIPESylSAIF--KQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTV-MTNtAGLANTF 227
Cdd:cd05570   81 GDLMFHIQRARRFTEE--RARFyaAEICLALQFLH-ERGIIYRDLKLDNVLLDAEGHIKIADFGMCKEgIWG-GNTTSTF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 228 VGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYlPPDQEEtwssvfELMEAIVDQPPPaLPSeNFSPELSSFI 307
Cdd:cd05570  157 CGTPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPF-EGDDED------ELFEAILNDEVL-YPR-WLSREAVSIL 227
                        250       260
                 ....*....|....*....|....*..
gi 567218350 308 STCLQKDPNSR-----SSAKELMEHPF 329
Cdd:cd05570  228 KGLLTKDPARRlgcgpKGEADIKAHPF 254
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
72-330 2.91e-41

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


Pssm-ID: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 145.10  E-value: 2.91e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  72 MVKFLGKGSSGVVQLVQHKWTGQFFALKVI------QLNIDEAIRKsiaqELKINQSSQCPYLVNSYQSFYDNGAISLIL 145
Cdd:cd14079    6 LGKTLGVGSFGKVKLAEHELTGHKVAVKILnrqkikSLDMEEKIRR----EIQILKLFRHPHIIRLYEVIETPTDIFMVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 146 EYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLaN 225
Cdd:cd14079   82 EYVSGGELFDYIVQKGRLSEDEARRFFQQIISGVEYCHR-HMVVHRDLKPENLLLDSNMNVKIADFGLSNIMRDGEFL-K 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 226 TFVGTYNYMSPERIVGNKY-GNKSDIWSLG--LVVLECATgkfpyLPPDQEETwSSVFELMEAIVdqppPALPSeNFSPE 302
Cdd:cd14079  160 TSCGSPNYAAPEVISGKLYaGPEVDVWSCGviLYALLCGS-----LPFDDEHI-PNLFKKIKSGI----YTIPS-HLSPG 228
                        250       260
                 ....*....|....*....|....*...
gi 567218350 303 LSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14079  229 ARDLIKRMLVVDPLKRITIPEIRQHPWF 256
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
66-338 5.65e-41

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: 147.15  E-value: 5.65e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  66 SLSDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAiRKSIAQEL---KINQSSQCPYLVNSYQSFYDNGAIS 142
Cdd:cd05593   13 TMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIA-KDEVAHTLtesRVLKNTRHPFLTSLKYSFQTKDRLC 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 143 LILEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAG 222
Cdd:cd05593   92 FVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGK-IVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAA 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 223 LANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVfeLMEAIvdqpppALPsENFSPE 302
Cdd:cd05593  171 TMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELI--LMEDI------KFP-RTLSAD 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 567218350 303 LSSFISTCLQKDPNSR-----SSAKELMEHPFLNKYNNSEI 338
Cdd:cd05593  242 AKSLLSGLLIKDPNKRlgggpDDAKEIMRHSFFTGVNWQDV 282
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
71-330 6.20e-41

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: 145.52  E-value: 6.20e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  71 DMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQ--LNIDEAIRKsiaqELKINQS-SQCPYLVNSYQSFYD-----NGAIS 142
Cdd:cd06639   25 DIIETIGKGTYGKVYKVTNKKDGSLAAVKILDpiSDVDEEIEA----EYNILRSlPNHPNVVKFYGMFYKadqyvGGQLW 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 143 LILEYMDGGSLADFLKSV----KTIPESYLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKITDFGVSTVMT 218
Cdd:cd06639  101 LVLELCNGGSVTELVKGLlkcgQRLDEAMISYILYGALLGLQHLHNNR-IIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 219 NTAGLANTFVGTYNYMSPERIVGNK-----YGNKSDIWSLGLVVLECATGKfpylPPDQEetWSSVFELMEAIVDQPPPA 293
Cdd:cd06639  180 SARLRRNTSVGTPFWMAPEVIACEQqydysYDARCDVWSLGITAIELADGD----PPLFD--MHPVKALFKIPRNPPPTL 253
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 567218350 294 LPSENFSPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd06639  254 LNPEKWCRGFSHFISQCLIKDFEKRPSVTHLLEHPFI 290
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
69-325 6.25e-41

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: 144.35  E-value: 6.25e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  69 DLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYM 148
Cdd:cd08219    1 QYNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIRLPKSSSAVEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVMEYC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 149 DGGSLADFLKSV--KTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANT 226
Cdd:cd08219   81 DGGDLMQKIKLQrgKLFPEDTILQWFVQMCLGVQHIH-EKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSPGAYACT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 227 FVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYlppdQEETWSSvfeLMEAIVDQPPPALPSEnFSPELSSF 306
Cdd:cd08219  160 YVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPF----QANSWKN---LILKVCQGSYKPLPSH-YSYELRSL 231
                        250
                 ....*....|....*....
gi 567218350 307 ISTCLQKDPNSRSSAKELM 325
Cdd:cd08219  232 IKQMFKRNPRSRPSATTIL 250
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
68-329 9.74e-41

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: 145.03  E-value: 9.74e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  68 SDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKViqLNIDEAIR----KSIAQELKINQSSQCPYLVNSYQSFYDNGAISL 143
Cdd:cd05580    1 DDFEFLKTLGTGSFGRVRLVKHKDSGKYYALKI--LKKAKIIKlkqvEHVLNEKRILSEVRHPFIVNLLGSFQDDRNLYM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 144 ILEYMDGGSLADFLKSVKTIPESYlsAIF--KQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNta 221
Cdd:cd05580   79 VMEYVPGGELFSLLRRSGRFPNDV--AKFyaAEVVLALEYLH-SLDIVYRDLKPENLLLDSDGHIKITDFGFAKRVKD-- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 222 gLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGkfpyLPPDQEETWSSVFEL-MEAIVDQPPPalpsenFS 300
Cdd:cd05580  154 -RTYTLCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAG----YPPFFDENPMKIYEKiLEGKIRFPSF------FD 222
                        250       260       270
                 ....*....|....*....|....*....|....
gi 567218350 301 PELSSFISTCLQKDP-----NSRSSAKELMEHPF 329
Cdd:cd05580  223 PDAKDLIKRLLVVDLtkrlgNLKNGVEDIKNHPW 256
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
67-324 9.93e-41

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


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 144.36  E-value: 9.93e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  67 LSDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILE 146
Cdd:cd13996    5 LNDFEEIELLGSGGFGSVYKVRNKVDGVTYAIKKIRLTEKSSASEKVLREVKALAKLNHPNIVRYYTAWVEEPPLYIQME 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 147 YMDGGSLADFL----KSVKTIPESYLSaIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHR-GEVKITDFGVSTVMTNTA 221
Cdd:cd13996   85 LCEGGTLRDWIdrrnSSSKNDRKLALE-LFKQILKGVSYIH-SKGIVHRDLKPSNIFLDNDdLQVKIGDFGLATSIGNQK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 222 GLAN--------------TFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECatgkfpYLPPdqeetwSSVFELMEAIV 287
Cdd:cd13996  163 RELNnlnnnnngntsnnsVGIGTPLYASPEQLDGENYNEKADIYSLGIILFEM------LHPF------KTAMERSTILT 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 567218350 288 DQPPPALPsENFS---PELSSFISTCLQKDPNSRSSAKEL 324
Cdd:cd13996  231 DLRNGILP-ESFKakhPKEADLIQSLLSKNPEERPSAEQL 269
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
76-330 2.56e-40

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: 144.10  E-value: 2.56e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKviQLNIDEAIRKS-IAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLA 154
Cdd:cd06654   28 IGQGASGTVYTAMDVATGQEVAIR--QMNLQQQPKKElIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 155 DFLKSVkTIPESYLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVGTYNYM 234
Cdd:cd06654  106 DVVTET-CMDEGQIAAVCRECLQALEFLHSNQ-VIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWM 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 235 SPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLppdQEETWSSVFELMeaiVDQPPPALPSENFSPELSSFISTCLQKD 314
Cdd:cd06654  184 APEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYL---NENPLRALYLIA---TNGTPELQNPEKLSAIFRDFLNRCLEMD 257
                        250
                 ....*....|....*.
gi 567218350 315 PNSRSSAKELMEHPFL 330
Cdd:cd06654  258 VEKRGSAKELLQHQFL 273
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
68-334 3.76e-40

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: 143.92  E-value: 3.76e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  68 SDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAiRKSIAQ---ELKINQSSQCPYLVNSYQSFYDNGAISLI 144
Cdd:cd05574    1 DHFKKIKLLGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMIK-RNKVKRvltEREILATLDHPFLPTLYASFQTSTHLCFV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 145 LEYMDGGSLADFLKSV--KTIPES----YLSaifkQVLQGLIYLHHdKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMT 218
Cdd:cd05574   80 MDYCPGGELFRLLQKQpgKRLPEEvarfYAA----EVLLALEYLHL-LGFVYRDLKPENILLHESGHIMLTDFDLSKQSS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 219 NTAGL-----------------------------ANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLP 269
Cdd:cd05574  155 VTPPPvrkslrkgsrrssvksieketfvaepsarSNSFVGTEEYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTTPFKG 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 567218350 270 PDQEETWSSvfelmeaIVDQPPPALPSENFSPELSSFISTCLQKDPNSR----SSAKELMEHPFLNKYN 334
Cdd:cd05574  235 SNRDETFSN-------ILKKELTFPESPPVSSEAKDLIRKLLVKDPSKRlgskRGASEIKRHPFFRGVN 296
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
64-330 4.13e-40

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: 142.70  E-value: 4.13e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  64 ELSLSDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVI---QLNiDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGA 140
Cdd:cd14117    2 KFTIDDFDIGRPLGKGKFGNVYLAREKQSKFIVALKVLfksQIE-KEGVEHQLRREIEIQSHLRHPNILRLYNYFHDRKR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 141 ISLILEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVStvmTNT 220
Cdd:cd14117   81 IYLILEYAPRGELYKELQKHGRFDEQRTATFMEELADALHYCH-EKKVIHRDIKPENLLMGYKGELKIADFGWS---VHA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 221 AGL-ANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFElmeaiVD-QPPPALPSEN 298
Cdd:cd14117  157 PSLrRRTMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVK-----VDlKFPPFLSDGS 231
                        250       260       270
                 ....*....|....*....|....*....|..
gi 567218350 299 fspelSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14117  232 -----RDLISKLLRYHPSERLPLKGVMEHPWV 258
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
76-330 9.23e-40

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: 141.68  E-value: 9.23e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHK--WTGQFFALKVIQLNIDEAIRK----SIAQELKINQSSQCPYLVNSYQSFYDNGA-ISLILEYM 148
Cdd:cd13994    1 IGKGATSVVRIVTKKnpRSGVLYAVKEYRRRDDESKRKdyvkRLTSEYIISSKLHHPNIVKVLDLCQDLHGkWCLVMEYC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 149 DGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAG----LA 224
Cdd:cd13994   81 PGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLH-SHGIAHRDLKPENILLDEDGVLKLTDFGTAEVFGMPAEkespMS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 225 NTFVGTYNYMSPERIVGNKY-GNKSDIWSLGLVVLECATGKFPYLPPDQEEtwSSVFELMEAIVDQPPPALPSENFSPEL 303
Cdd:cd13994  160 AGLCGSEPYMAPEVFTSGSYdGRAVDVWSCGIVLFALFTGRFPWRSAKKSD--SAYKAYEKSGDFTNGPYEPIENLLPSE 237
                        250       260
                 ....*....|....*....|....*...
gi 567218350 304 S-SFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd13994  238 CrRLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
70-332 9.86e-40

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: 142.47  E-value: 9.86e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  70 LDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAiRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMD 149
Cdd:cd06657   22 LDNFIKIGEGSTGIVCIATVKSSGKLVAVKKMDLRKQQR-RELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLE 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 150 GGSLADFLKSVKtIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVG 229
Cdd:cd06657  101 GGALTDIVTHTR-MNEEQIAAVCLAVLKALSVLH-AQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVG 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 230 TYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYL--PPdqeetwssvFELMEAIVDQPPPALPS-ENFSPELSSF 306
Cdd:cd06657  179 TPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFnePP---------LKAMKMIRDNLPPKLKNlHKVSPSLKGF 249
                        250       260
                 ....*....|....*....|....*.
gi 567218350 307 ISTCLQKDPNSRSSAKELMEHPFLNK 332
Cdd:cd06657  250 LDRLLVRDPAQRATAAELLKHPFLAK 275
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
66-330 2.36e-39

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


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 140.48  E-value: 2.36e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  66 SLSDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVI---QLNiDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAIS 142
Cdd:cd14116    3 ALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLfkaQLE-KAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 143 LILEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVStvMTNTAG 222
Cdd:cd14116   82 LILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCH-SKRVIHRDIKPENLLLGSAGELKIADFGWS--VHAPSS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 223 LANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVfelmeAIVDQPPPALPSEnfspE 302
Cdd:cd14116  159 RRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRI-----SRVEFTFPDFVTE----G 229
                        250       260
                 ....*....|....*....|....*...
gi 567218350 303 LSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14116  230 ARDLISRLLKHNPSQRPMLREVLEHPWI 257
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
76-330 2.39e-39

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: 140.28  E-value: 2.39e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRK--SIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGgSL 153
Cdd:cd06607    9 IGHGSFGAVYYARNKRTSEVVAIKKMSYSGKQSTEKwqDIIKEVKFLRQLRHPNTIEYKGCYLREHTAWLVMEYCLG-SA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 154 ADFLKSVKT-IPESYLSAIFKQVLQGLIYLH-HDKhiIHRDLKPSNLLINHRGEVKITDFGVSTVMTNtaglANTFVGTY 231
Cdd:cd06607   88 SDIVEVHKKpLQEVEIAAICHGALQGLAYLHsHNR--IHRDVKAGNILLTEPGTVKLADFGSASLVCP----ANSFVGTP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 232 NYMSPERIVG---NKYGNKSDIWSLGLVVLECATGKFPYlppdqeetwssvFEL--MEA---IVDQPPPALPSENFSPEL 303
Cdd:cd06607  162 YWMAPEVILAmdeGQYDGKVDVWSLGITCIELAERKPPL------------FNMnaMSAlyhIAQNDSPTLSSGEWSDDF 229
                        250       260
                 ....*....|....*....|....*..
gi 567218350 304 SSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd06607  230 RNFVDSCLQKIPQDRPSAEDLLKHPFV 256
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
69-329 3.31e-39

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


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 140.62  E-value: 3.31e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  69 DLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVI-QLNIdeAIRKSIAQ---ELKINQSSQCPYLVNSYQSFYDNGAISLI 144
Cdd:cd05609    1 DFETIKLISNGAYGAVYLVRHRETRQRFAMKKInKQNL--ILRNQIQQvfvERDILTFAENPFVVSMYCSFETKRHLCMV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 145 LEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTV--MTNTAG 222
Cdd:cd05609   79 MEYVEGGDCATLLKNIGPLPVDMARMYFAETVLALEYLH-SYGIVHRDLKPDNLLITSMGHIKLTDFGLSKIglMSLTTN 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 223 LANTF-------------VGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSV----FELMEA 285
Cdd:cd05609  158 LYEGHiekdtrefldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVisdeIEWPEG 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 567218350 286 ivDQPPPalpsenfsPELSSFISTCLQKDPNSR---SSAKELMEHPF 329
Cdd:cd05609  238 --DDALP--------DDAQDLITRLLQQNPLERlgtGGAEEVKQHPF 274
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
74-329 5.56e-39

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: 140.95  E-value: 5.56e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVIQlniDEAI--RKSIAQELKIN---QSSQCPYLVNSYQSFYDNGAISLILEYM 148
Cdd:cd05571    1 KVLGKGTFGKVILCREKATGELYAIKILK---KEVIiaKDEVAHTLTENrvlQNTRHPFLTSLKYSFQTNDRLCFVMEYV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 149 DGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFV 228
Cdd:cd05571   78 NGGELFFHLSRERVFSEDRTRFYGAEIVLALGYLH-SQGIVYRDLKLENLLLDKDGHIKITDFGLCKEEISYGATTKTFC 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 229 GTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEEtwssVFEL--MEAIVdqpppaLPSeNFSPELSSF 306
Cdd:cd05571  157 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEV----LFELilMEEVR------FPS-TLSPEAKSL 225
                        250       260
                 ....*....|....*....|....*...
gi 567218350 307 ISTCLQKDPNSR-----SSAKELMEHPF 329
Cdd:cd05571  226 LAGLLKKDPKKRlgggpRDAKEIMEHPF 253
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
71-330 5.58e-39

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


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 139.47  E-value: 5.58e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  71 DMVKFLGKGSSGVVQLVQHKWTGQFFALKVI-QLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMD 149
Cdd:cd14074    6 DLEETLGRGHFAVVKLARHVFTGEKVAVKVIdKTKLDDVSKAHLFQEVRCMKLVQHPNVVRLYEVIDTQTKLYLILELGD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 150 GGSLADF-LKSVKTIPESYLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLI-NHRGEVKITDFGVSTVMTNTAGLaNTF 227
Cdd:cd14074   86 GGDMYDYiMKHENGLNEDLARKYFRQIVSAISYCHK-LHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQPGEKL-ETS 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 228 VGTYNYMSPERIVGNKY-GNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVfelMEAIVDQPPpalpseNFSPELSSF 306
Cdd:cd14074  164 CGSLAYSAPEILLGDEYdAPAVDIWSLGVILYMLVCGQPPFQEANDSETLTMI---MDCKYTVPA------HVSPECKDL 234
                        250       260
                 ....*....|....*....|....
gi 567218350 307 ISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14074  235 IRRMLIRDPKKRASLEEIENHPWL 258
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
76-329 6.71e-39

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: 139.35  E-value: 6.71e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKviqlNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLAD 155
Cdd:cd14010    8 IGRGKHSVVYKGRRKGTIEFVAIK----CVDKSKRPEVLNEVRLTHELKHPNVLKFYEWYETSNHLWLVVEYCTGGDLET 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 156 FLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMT----------------N 219
Cdd:cd14010   84 LLRQDGNLPESSVRKFGRDLVRGLHYIH-SKGIIYCDLKPSNILLDGNGTLKLSDFGLARREGeilkelfgqfsdegnvN 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 220 TAGLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKfpylPPDQEETWSsvfELMEAIVDQPPPALP---S 296
Cdd:cd14010  163 KVSKKQAKRGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGK----PPFVAESFT---ELVEKILNEDPPPPPpkvS 235
                        250       260       270
                 ....*....|....*....|....*....|...
gi 567218350 297 ENFSPELSSFISTCLQKDPNSRSSAKELMEHPF 329
Cdd:cd14010  236 SKPSPDFKSLLKGLLEKDPAKRLSWDELVKHPF 268
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
69-329 1.24e-38

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: 138.31  E-value: 1.24e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  69 DLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVI------QLNIDEAIRKSIAQELKINQssqcPYLVNSYQSFYDNGAIS 142
Cdd:cd14663    1 RYELGRTLGEGTFAKVKFARNTKTGESVAIKIIdkeqvaREGMVEQIKREIAIMKLLRH----PNIVELHEVMATKTKIF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 143 LILEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMT--NT 220
Cdd:cd14663   77 FVMELVTGGELFSKIAKNGRLKEDKARKYFQQLIDAVDYCH-SRGVFHRDLKPENLLLDEDGNLKISDFGLSALSEqfRQ 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 221 AGLANTFVGTYNYMSPERIVGNKY-GNKSDIWSLGLVVLECATGkfpYLPPDQEETWSSVFELMEAIVDQPPpalpseNF 299
Cdd:cd14663  156 DGLLHTTCGTPNYVAPEVLARRGYdGAKADIWSCGVILFVLLAG---YLPFDDENLMALYRKIMKGEFEYPR------WF 226
                        250       260       270
                 ....*....|....*....|....*....|
gi 567218350 300 SPELSSFISTCLQKDPNSRSSAKELMEHPF 329
Cdd:cd14663  227 SPGAKSLIKRILDPNPSTRITVEQIMASPW 256
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
71-330 1.37e-38

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: 139.38  E-value: 1.37e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  71 DMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQ--LNIDEAIRksiAQELKINQSSQCPYLVNSYQSFYDNGAIS-----L 143
Cdd:cd06638   21 EIIETIGKGTYGKVFKVLNKKNGSKAAVKILDpiHDIDEEIE---AEYNILKALSDHPNVVKFYGMYYKKDVKNgdqlwL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 144 ILEYMDGGSLAD----FLKSVKTIPESYLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKITDFGVSTVMTN 219
Cdd:cd06638   98 VLELCNGGSVTDlvkgFLKRGERMEEPIIAYILHEALMGLQHLHVNK-TIHRDVKGNNILLTTEGGVKLVDFGVSAQLTS 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 220 TAGLANTFVGTYNYMSPERI-----VGNKYGNKSDIWSLGLVVLECATGKfpylPPDQE-ETWSSVFElmeaIVDQPPPA 293
Cdd:cd06638  177 TRLRRNTSVGTPFWMAPEVIaceqqLDSTYDARCDVWSLGITAIELGDGD----PPLADlHPMRALFK----IPRNPPPT 248
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 567218350 294 LPS-ENFSPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd06638  249 LHQpELWSNEFNDFIRKCLTKDYEKRPTVSDLLQHVFI 286
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
71-330 1.97e-38

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: 137.90  E-value: 1.97e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  71 DMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLN--IDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYM 148
Cdd:cd14073    4 ELLETLGKGTYGKVKLAIERATGREVAIKSIKKDkiEDEQDMVRIRREIEIMSSLNHPHIIRIYEVFENKDKIVIVMEYA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 149 DGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAgLANTFV 228
Cdd:cd14073   84 SGGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNG-VVHRDLKLENILLDQNGNAKIADFGLSNLYSKDK-LLQTFC 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 229 GTYNYMSPERIVGNKY-GNKSDIWSLGLVVLECATGKFPYlppDQEETWSSVFELMEAIVDQPPPalPSENfspelSSFI 307
Cdd:cd14073  162 GSPLYASPEIVNGTPYqGPEVDCWSLGVLLYTLVYGTMPF---DGSDFKRLVKQISSGDYREPTQ--PSDA-----SGLI 231
                        250       260
                 ....*....|....*....|...
gi 567218350 308 STCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14073  232 RWMLTVNPKRRATIEDIANHWWV 254
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
71-328 2.53e-38

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: 137.46  E-value: 2.53e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  71 DMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDG 150
Cdd:cd14095    3 DIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGKEHMIENEVAILRRVKHPNIVQLIEEYDTDTELYLVMELVKG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 151 GSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGE----VKITDFGVSTVMTNtagLANT 226
Cdd:cd14095   83 GDLFDAITSSTKFTERDASRMVTDLAQALKYLH-SLSIVHRDIKPENLLVVEHEDgsksLKLADFGLATEVKE---PLFT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 227 FVGTYNYMSPERIVGNKYGNKSDIWSLGLV--VLECatGKFPYLPPDQEETwssvfELMEAI----VDQPPPALpsENFS 300
Cdd:cd14095  159 VCGTPTYVAPEILAETGYGLKVDIWAAGVItyILLC--GFPPFRSPDRDQE-----ELFDLIlageFEFLSPYW--DNIS 229
                        250       260
                 ....*....|....*....|....*...
gi 567218350 301 PELSSFISTCLQKDPNSRSSAKELMEHP 328
Cdd:cd14095  230 DSAKDLISRMLVVDPEKRYSAGQVLDHP 257
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
76-330 2.61e-38

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: 137.87  E-value: 2.61e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNID-------EAIRKSIAQELKI-NQSSQCPYLVNSYQSFYDNGAISLILEY 147
Cdd:cd14093   11 LGRGVSSTVRRCIEKETGQEFAVKIIDITGEksseneaEELREATRREIEIlRQVSGHPNIIELHDVFESPTFIFLVFEL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 148 MDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANtF 227
Cdd:cd14093   91 CRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLH-SLNIVHRDLKPENILLDDNLNVKISDFGFATRLDEGEKLRE-L 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 228 VGTYNYMSPERIVGN------KYGNKSDIWSLGLVVLECATGKFPYlppdqeetWSSVFELMEAIVDQPPPALPS---EN 298
Cdd:cd14093  169 CGTPGYLAPEVLKCSmydnapGYGKEVDMWACGVIMYTLLAGCPPF--------WHRKQMVMLRNIMEGKYEFGSpewDD 240
                        250       260       270
                 ....*....|....*....|....*....|..
gi 567218350 299 FSPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14093  241 ISDTAKDLISKLLVVDPKKRLTAEEALEHPFF 272
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
71-346 2.98e-38

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: 138.97  E-value: 2.98e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  71 DMVKFLGKGSSG--VVQLVQHKWTGQFFALKVIqlNIDEAIRKS---IAQELKINQSSQCPYLVNSYQSFYDNGAISLIL 145
Cdd:cd08216    1 ELLYEIGKCFKGggVVHLAKHKPTNTLVAVKKI--NLESDSKEDlkfLQQEILTSRQLQHPNILPYVTSFVVDNDLYVVT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 146 EYMDGGSLADFLKSVKT--IPESYLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNtAGL 223
Cdd:cd08216   79 PLMAYGSCRDLLKTHFPegLPELAIAFILRDVLNALEYIHS-KGYIHRSVKASHILISGDGKVVLSGLRYAYSMVK-HGK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 224 ANTFVGTY--------NYMSPERIVGN--KYGNKSDIWSLGLVVLECATGKFP--------------------------Y 267
Cdd:cd08216  157 RQRVVHDFpksseknlPWLSPEVLQQNllGYNEKSDIYSVGITACELANGVVPfsdmpatqmllekvrgttpqlldcstY 236
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 567218350 268 LPPDQEETWSSVFELMEAIVDQPPPALPSENFSPELSSFISTCLQKDPNSRSSAKELMEHPFLNKYNNSEINLASYFTD 346
Cdd:cd08216  237 PLEEDSMSQSEDSSTEHPNNRDTRDIPYQRTFSEAFHQFVELCLQRDPELRPSASQLLAHSFFKQCRRSNTSLLDLLKP 315
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
67-318 7.09e-38

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: 136.70  E-value: 7.09e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  67 LSDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQL--NIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLI 144
Cdd:cd08228    1 LANFQIEKKIGRGQFSEVYRATCLLDRKPVALKKVQIfeMMDAKARQDCVKEIDLLKQLNHPNVIKYLDSFIEDNELNIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 145 LEYMDGGSLADFLKSVKT----IPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNT 220
Cdd:cd08228   81 LELADAGDLSQMIKYFKKqkrlIPERTVWKYFVQLCSAVEHMH-SRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 221 AGLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQeetwsSVFELMEAIVDQPPPALPSENFS 300
Cdd:cd08228  160 TTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKM-----NLFSLCQKIEQCDYPPLPTEHYS 234
                        250
                 ....*....|....*...
gi 567218350 301 PELSSFISTCLQKDPNSR 318
Cdd:cd08228  235 EKLRELVSMCIYPDPDQR 252
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
76-330 8.87e-38

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: 137.06  E-value: 8.87e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALK-VIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLA 154
Cdd:cd07833    9 VGEGAYGVVLKCRNKATGEIVAIKkFKESEDDEDVKKTALREVKVLRQLRHENIVNLKEAFRRKGRLYLVFEYVERTLLE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 155 DFLKSVKTIPESYLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANT-FVGTYNY 233
Cdd:cd07833   89 LLEASPGGLPPDAVRSYIWQLLQAIAYCHSHN-IIHRDIKPENILVSESGVLKLCDFGFARALTARPASPLTdYVATRWY 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 234 MSPERIVGN-KYGNKSDIWSLGLVVLECATGK--FP--------Y--------LPPDQEETWSS--VFeLMEAIVDQPPP 292
Cdd:cd07833  168 RAPELLVGDtNYGKPVDVWAIGCIMAELLDGEplFPgdsdidqlYliqkclgpLPPSHQELFSSnpRF-AGVAFPEPSQP 246
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 567218350 293 ----ALPSENFSPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd07833  247 esleRRYPGKVSSPALDFLKACLRMDPKERLTCDELLQHPYF 288
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
76-327 1.01e-37

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: 136.03  E-value: 1.01e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVqhKWTGQFFALKVIQLnidEAIRKSIAQELKinQSSQC--PYLVNSYQSFYDNGAISLILEYMDGGSL 153
Cdd:cd14058    1 VGRGSFGVVCKA--RWRNQIVAVKIIES---ESEKKAFEVEVR--QLSRVdhPNIIKLYGACSNQKPVCLVMEYAEGGSL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 154 ADFLKSVKTIPE-SYLSAI--FKQVLQGLIYLH--HDKHIIHRDLKPSNLLINHRGEV-KITDFG----VSTVMTNTAGL 223
Cdd:cd14058   74 YNVLHGKEPKPIyTAAHAMswALQCAKGVAYLHsmKPKALIHRDLKPPNLLLTNGGTVlKICDFGtacdISTHMTNNKGS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 224 ANtfvgtynYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYlppdqEETWSSVFELMEAIVDQPPPalPSENFSPE- 302
Cdd:cd14058  154 AA-------WMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPF-----DHIGGPAFRIMWAVHNGERP--PLIKNCPKp 219
                        250       260
                 ....*....|....*....|....*...
gi 567218350 303 LSSFISTCLQKDPNSRSSAKEL---MEH 327
Cdd:cd14058  220 IESLMTRCWSKDPEKRPSMKEIvkiMSH 247
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
76-327 1.46e-37

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: 135.86  E-value: 1.46e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKwTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLAD 155
Cdd:cd14066    1 IGSGGFGTVYKGVLE-NGTVVAVKRLNEMNCAASKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNGSLED 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 156 FLKSVKTIPEsyLS-----AIFKQVLQGLIYLHH--DKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANT-- 226
Cdd:cd14066   80 RLHCHKGSPP--LPwpqrlKIAKGIARGLEYLHEecPPPIIHGDIKSSNILLDEDFEPKLTDFGLARLIPPSESVSKTsa 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 227 FVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFP--YLPPDQ------EETWSSVFELMEAIVDQ-PPPALPSE 297
Cdd:cd14066  158 VKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAvdENRENAsrkdlvEWVESKGKEELEDILDKrLVDDDGVE 237
                        250       260       270
                 ....*....|....*....|....*....|...
gi 567218350 298 NfsPELSSFIST---CLQKDPNSRSSAKELMEH 327
Cdd:cd14066  238 E--EEVEALLRLallCTRSDPSLRPSMKEVVQM 268
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
72-330 1.88e-37

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: 135.98  E-value: 1.88e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  72 MVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKS-------IAQELKINQSSQCPYLVNSYQSFYDNGAISLI 144
Cdd:cd14084   10 MSRTLGSGACGEVKLAYDKSTCKKVAIKIINKRKFTIGSRReinkprnIETEIEILKKLSHPCIIKIEDFFDAEDDYYIV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 145 LEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLhHDKHIIHRDLKPSNLLINHRGE---VKITDFGVSTVMTNTA 221
Cdd:cd14084   90 LELMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYL-HSNGIIHRDLKPENVLLSSQEEeclIKITDFGLSKILGETS 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 222 gLANTFVGTYNYMSPE--RIVG-NKYGNKSDIWSLGLVVLECATGkfpYLPPDQEETWSSvfeLMEAIVDQPPPALPSE- 297
Cdd:cd14084  169 -LMKTLCGTPTYLAPEvlRSFGtEGYTRAVDCWSLGVILFICLSG---YPPFSEEYTQMS---LKEQILSGKYTFIPKAw 241
                        250       260       270
                 ....*....|....*....|....*....|....
gi 567218350 298 -NFSPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14084  242 kNVSEEAKDLVKKMLVVDPSRRPSIEEALEHPWL 275
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
70-331 2.20e-37

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


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 135.89  E-value: 2.20e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  70 LDMVKFLGKGSSGVVQLVQHKWTGQFFALKVI---QLNIDEAIRKSIAQELKINQSSqcpylVNSYQSFYDNGA-ISLIL 145
Cdd:cd14166    5 FIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIkksPLSRDSSLENEIAVLKRIKHEN-----IVTLEDIYESTThYYLVM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 146 EYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLhHDKHIIHRDLKPSNLLI---NHRGEVKITDFGVSTVMTNtaG 222
Cdd:cd14166   80 QLVSGGELFDRILERGVYTEKDASRVINQVLSAVKYL-HENGIVHRDLKPENLLYltpDENSKIMITDFGLSKMEQN--G 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 223 LANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLV--VLECAtgkfpyLPPDQEETWSSVFE-LMEAIVDQPPPALpsENF 299
Cdd:cd14166  157 IMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVItyILLCG------YPPFYEETESRLFEkIKEGYYEFESPFW--DDI 228
                        250       260       270
                 ....*....|....*....|....*....|..
gi 567218350 300 SPELSSFISTCLQKDPNSRSSAKELMEHPFLN 331
Cdd:cd14166  229 SESAKDFIRHLLEKNPSKRYTCEKALSHPWII 260
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
76-329 2.35e-37

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: 134.72  E-value: 2.35e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHK-WTGQFFALKVIQL-NIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSL 153
Cdd:cd14121    3 LGSGTYATVYKAYRKsGAREVVAVKCVSKsSLNKASTENLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYCSGGDL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 154 ADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEV--KITDFGVSTVMTNTAgLANTFVGTY 231
Cdd:cd14121   83 SRFIRSRRTLPESTVRRFLQQLASALQFLR-EHNISHMDLKPQNLLLSSRYNPvlKLADFGFAQHLKPND-EAHSLRGSP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 232 NYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYlppdqeeTWSSVFELMEAIVDQPPPALPSenfSPELSS----FI 307
Cdd:cd14121  161 LYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPF-------ASRSFEELEEKIRSSKPIEIPT---RPELSAdcrdLL 230
                        250       260
                 ....*....|....*....|..
gi 567218350 308 STCLQKDPNSRSSAKELMEHPF 329
Cdd:cd14121  231 LRLLQRDPDRRISFEEFFAHPF 252
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
71-330 2.40e-37

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: 135.09  E-value: 2.40e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  71 DMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQ-ELKINQSSQCPYLVNSYQSFYDNGAISLILEYMD 149
Cdd:cd08225    3 EIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKEKEASKkEVILLAKMKHPNIVTFFASFQENGRLFIVMEYCD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 150 GGSLADFLKSVKTI--PESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEV-KITDFGVSTVMTNTAGLANT 226
Cdd:cd08225   83 GGDLMKRINRQRGVlfSEDQILSWFVQISLGLKHIH-DRKILHRDIKSQNIFLSKNGMVaKLGDFGIARQLNDSMELAYT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 227 FVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYlppdqeeTWSSVFELMEAIVdQPPPALPSENFSPELSSF 306
Cdd:cd08225  162 CVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPF-------EGNNLHQLVLKIC-QGYFAPISPNFSRDLRSL 233
                        250       260
                 ....*....|....*....|....
gi 567218350 307 ISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd08225  234 ISQLFKVSPRDRPSITSILKRPFL 257
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
70-326 3.24e-37

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 134.58  E-value: 3.24e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350    70 LDMVKFLGKGSSGVVQL----VQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLIL 145
Cdd:smart00219   1 LTLGKKLGEGAFGEVYKgklkGKGGKKKVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350   146 EYMDGGSLADFLKSVK-TIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVS-----TVMTN 219
Cdd:smart00219  81 EYMEGGDLLSYLRKNRpKLSLSDLLSFALQIARGMEYLE-SKNFIHRDLAARNCLVGENLVVKISDFGLSrdlydDDYYR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350   220 TAGLAntfvGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPYlpPDQeetwsSVFELMEAIVD---QPPPalp 295
Cdd:smart00219 160 KRGGK----LPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEQPY--PGM-----SNEEVLEYLKNgyrLPQP--- 225
                          250       260       270
                   ....*....|....*....|....*....|.
gi 567218350   296 sENFSPELSSFISTCLQKDPNSRSSAKELME 326
Cdd:smart00219 226 -PNCPPELYDLMLQCWAEDPEDRPTFSELVE 255
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
74-324 3.73e-37

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: 134.59  E-value: 3.73e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVqlvqhkWTGQFF---------ALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLI 144
Cdd:cd00192    1 KKLGEGAFGEV------YKGKLKggdgktvdvAVKTLKEDASESERKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 145 LEYMDGGSLADFLKSVK---------TIPESYLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLINHRGEVKITDFGVST 215
Cdd:cd00192   75 MEYMEGGDLLDFLRKSRpvfpspepsTLSLKDLLSFAIQIAKGMEYLAS-KKFVHRDLAARNCLVGEDLVVKISDFGLSR 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 216 vmtntaglaNTFVGTYNY-----------MSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPYlpPDQeetwsSVFELM 283
Cdd:cd00192  154 ---------DIYDDDYYRkktggklpirwMAPESLKDGIFTSKSDVWSFGVLLWEIFTlGATPY--PGL-----SNEEVL 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 567218350 284 EAIVD---QPPPalpsENFSPELSSFISTCLQKDPNSRSSAKEL 324
Cdd:cd00192  218 EYLRKgyrLPKP----ENCPDELYELMLSCWQLDPEDRPTFSEL 257
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
76-329 4.48e-37

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: 135.19  E-value: 4.48e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALK-VIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLA 154
Cdd:cd07847    9 IGEGSYGVVFKCRNRETGQIVAIKkFVESEDDPVIKKIALREIRMLKQLKHPNLVNLIEVFRRKRKLHLVFEYCDHTVLN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 155 DFLKSVKTIPESYLSAIFKQVLQGLIYLHhdKH-IIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVGTYNY 233
Cdd:cd07847   89 ELEKNPRGVPEHLIKKIIWQTLQAVNFCH--KHnCIHRDVKPENILITKQGQIKLCDFGFARILTGPGDDYTDYVATRWY 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 234 MSPERIVGN-KYGNKSDIWSLGLVVLECATGKfPYLP-------------------PDQEETWSSVFELMEAIVDQPPPA 293
Cdd:cd07847  167 RAPELLVGDtQYGPPVDVWAIGCVFAELLTGQ-PLWPgksdvdqlylirktlgdliPRHQQIFSTNQFFKGLSIPEPETR 245
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 567218350 294 LPSENFSPELSS----FISTCLQKDPNSRSSAKELMEHPF 329
Cdd:cd07847  246 EPLESKFPNISSpalsFLKGCLQMDPTERLSCEELLEHPY 285
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
76-331 5.81e-37

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: 134.44  E-value: 5.81e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQH---KWTGQFFALKVIQlnideaiRKSIAQELKINQSS-----------QCPYLVNSYQSFYDNGAI 141
Cdd:cd05583    2 LGTGAYGKVFLVRKvggHDAGKLYAMKVLK-------KATIVQKAKTAEHTmterqvleavrQSPFLVTLHYAFQTDAKL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 142 SLILEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKITDFGVSTVMTN-T 220
Cdd:cd05583   75 HLILDYVNGGELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLG-IIYRDIKLENILLDSEGHVVLTDFGLSKEFLPgE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 221 AGLANTFVGTYNYMSPERIVGNKYGNKS--DIWSLGLVVLECATGKFPYLPPDQEETWSsvfELMEAIVDQPPPaLPSEn 298
Cdd:cd05583  154 NDRAYSFCGTIEYMAPEVVRGGSDGHDKavDWWSLGVLTYELLTGASPFTVDGERNSQS---EISKRILKSHPP-IPKT- 228
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 567218350 299 FSPELSSFISTCLQKDPNSR-----SSAKELMEHPFLN 331
Cdd:cd05583  229 FSAEAKDFILKLLEKDPKKRlgagpRGAHEIKEHPFFK 266
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
69-330 8.66e-37

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


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 133.73  E-value: 8.66e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  69 DLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVI--------------QLNIDEAIRKSIAQELKINQSSQCPYLVNSYQS 134
Cdd:cd14077    2 NWEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIprasnaglkkerekRLEKEISRDIRTIREAALSSLLNHPHICRLRDF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 135 FYDNGAISLILEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHDkHIIHRDLKPSNLLINHRGEVKITDFGVS 214
Cdd:cd14077   82 LRTPNHYYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRN-SIVHRDLKIENILISKSGNIKIIDFGLS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 215 TVMTNTAGLaNTFVGTYNYMSPERIVGNKY-GNKSDIWSLGLVVLECATGKFPYlppDQEETWSSVFELMEAIVDQPppa 293
Cdd:cd14077  161 NLYDPRRLL-RTFCGSLYFAAPELLQAQPYtGPEVDVWSFGVVLYVLVCGKVPF---DDENMPALHAKIKKGKVEYP--- 233
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 567218350 294 lpsENFSPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14077  234 ---SYLSSECKSLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
71-329 8.76e-37

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


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 134.62  E-value: 8.76e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  71 DMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLN----IDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILE 146
Cdd:cd07841    3 EKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGerkeAKDGINFTALREIKLLQELKHPNIIGLLDVFGHKSNINLVFE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 147 YMDGgslaDFLKSVK----TIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAG 222
Cdd:cd07841   83 FMET----DLEKVIKdksiVLTPADIKSYMLMTLRGLEYLH-SNWILHRDLKPNNLLIASDGVLKLADFGLARSFGSPNR 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 223 LANTFVGTYNYMSPERIVG-NKYGNKSDIWSLGLVVLECATGKfPYLPP----DQ------------EETWSSVFELMEA 285
Cdd:cd07841  158 KMTHQVVTRWYRAPELLFGaRHYGVGVDMWSVGCIFAELLLRV-PFLPGdsdiDQlgkifealgtptEENWPGVTSLPDY 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 567218350 286 IVDQPPPALPSENFSPELSS----FISTCLQKDPNSRSSAKELMEHPF 329
Cdd:cd07841  237 VEFKPFPPTPLKQIFPAASDdaldLLQRLLTLNPNKRITARQALEHPY 284
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
76-330 1.02e-36

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: 134.40  E-value: 1.02e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAiRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLAD 155
Cdd:cd06658   30 IGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQR-RELLFNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGGALTD 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 156 FLKSVKtIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVGTYNYMS 235
Cdd:cd06658  109 IVTHTR-MNEEQIATVCLSVLRALSYLH-NQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQVSKEVPKRKSLVGTPYWMA 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 236 PERIVGNKYGNKSDIWSLGLVVLECATGKFPYL--PPDQEetwssvfelMEAIVDQPPPALP-SENFSPELSSFISTCLQ 312
Cdd:cd06658  187 PEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFnePPLQA---------MRRIRDNLPPRVKdSHKVSSVLRGFLDLMLV 257
                        250
                 ....*....|....*...
gi 567218350 313 KDPNSRSSAKELMEHPFL 330
Cdd:cd06658  258 REPSQRATAQELLQHPFL 275
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
76-331 1.07e-36

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: 133.99  E-value: 1.07e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQL-NIDEAIRKSIAQELKINQSSQ-CPYLVNSYQSFYDNGAISLILEYMDGgSL 153
Cdd:cd07832    8 IGEGAHGIVFKAKDRETGETVALKKVALrKLEGGIPNQALREIKALQACQgHPYVVKLRDVFPHGTGFVLVFEYMLS-SL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 154 ADFLK-SVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTF-VGTY 231
Cdd:cd07832   87 SEVLRdEERPLTEAQVKRYMRMLLKGVAYMH-ANRIMHRDLKPANLLISSTGVLKIADFGLARLFSEEDPRLYSHqVATR 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 232 NYMSPERIVGN-KYGNKSDIWSLGLVVLECATGKfPYLP-----------------PDqEETWSSVFELMEA--IVDQPP 291
Cdd:cd07832  166 WYRAPELLYGSrKYDEGVDLWAVGCIFAELLNGS-PLFPgendieqlaivlrtlgtPN-EKTWPELTSLPDYnkITFPES 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 567218350 292 PALPSENFSPELSS----FISTCLQKDPNSRSSAKELMEHPFLN 331
Cdd:cd07832  244 KGIRLEEIFPDCSPeaidLLKGLLVYNPKKRLSAEEALRHPYFF 287
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
72-330 1.10e-36

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: 133.81  E-value: 1.10e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  72 MVKFLGKGSSGVVQLVQHKWTGQFFALKVIQ---LNIDEAIR----KSIaqeLKINQSsqcPYLVNSYQSFYDNGAISLI 144
Cdd:cd07830    3 VIKQLGDGTFGSVYLARNKETGELVAIKKMKkkfYSWEECMNlrevKSL---RKLNEH---PNIVKLKEVFRENDELYFV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 145 LEYMDGgSLADFLKS--VKTIPESYLSAIFKQVLQGLIYLHhdKH-IIHRDLKPSNLLINHRGEVKITDFgvstvmtnta 221
Cdd:cd07830   77 FEYMEG-NLYQLMKDrkGKPFSESVIRSIIYQILQGLAHIH--KHgFFHRDLKPENLLVSGPEVVKIADF---------- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 222 GLA---------NTFVGTYNYMSPERIVGNKYGNKS-DIWSLGLVVLECATGK--FP-------------YLPPDQEETW 276
Cdd:cd07830  144 GLAreirsrppyTDYVSTRWYRAPEILLRSTSYSSPvDIWALGCIMAELYTLRplFPgsseidqlykicsVLGTPTKQDW 223
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 277 SSVFELMEAI---VDQPPPALPSE---NFSPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd07830  224 PEGYKLASKLgfrFPQFAPTSLHQlipNASPEAIDLIKDMLRWDPKKRPTASQALQHPYF 283
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
74-329 1.49e-36

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: 134.43  E-value: 1.49e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVIQLNI---DEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDG 150
Cdd:cd05592    1 KVLGKGSFGKVMLAELKGTNQYFAIKALKKDVvleDDDVECTMIERRVLALASQHPFLTHLFCTFQTESHLFFVMEYLNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 151 GSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVGT 230
Cdd:cd05592   81 GDLMFHIQQSGRFDEDRARFYGAEIICGLQFLH-SRGIIYRDLKLDNVLLDREGHIKIADFGMCKENIYGENKASTFCGT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 231 YNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVfelmeaIVDQP--PPALpsenfSPELSSFIS 308
Cdd:cd05592  160 PDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSI------CNDTPhyPRWL-----TKEAASCLS 228
                        250       260
                 ....*....|....*....|....*.
gi 567218350 309 TCLQKDPNSR-----SSAKELMEHPF 329
Cdd:cd05592  229 LLLERNPEKRlgvpeCPAGDIRDHPF 254
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
74-329 1.64e-36

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: 133.28  E-value: 1.64e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVIQLNID--EAIRKSIAQELKIN--QSSQCPYLVNSYQSFYDNG--AISLILEY 147
Cdd:cd06651   13 KLLGQGAFGRVYLCYDVDTGRELAAKQVQFDPEspETSKEVSALECEIQllKNLQHERIVQYYGCLRDRAekTLTIFMEY 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 148 MDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKITDFGVS----TVMTNTAGL 223
Cdd:cd06651   93 MPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNM-IVHRDIKGANILRDSAGNVKLGDFGASkrlqTICMSGTGI 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 224 aNTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLppdQEETWSSVFElmeaIVDQPP-PALPSeNFSPE 302
Cdd:cd06651  172 -RSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWA---EYEAMAAIFK----IATQPTnPQLPS-HISEH 242
                        250       260
                 ....*....|....*....|....*..
gi 567218350 303 LSSFIStCLQKDPNSRSSAKELMEHPF 329
Cdd:cd06651  243 ARDFLG-CIFVEARHRPSAEELLRHPF 268
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
68-330 1.72e-36

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: 132.84  E-value: 1.72e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  68 SDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIqlNIDEA---IRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLI 144
Cdd:cd14069    1 EDWDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFV--DMKRApgdCPENIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 145 LEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTN--TAG 222
Cdd:cd14069   79 LEYASGGELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLH-SCGITHRDIKPENLLLDENDNLKISDFGLATVFRYkgKER 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 223 LANTFVGTYNYMSPERIVGNKY-GNKSDIWSLGLVVLECATGKFPYlppdqEETWSSVFELMEAIVDQPPPALPSENFSP 301
Cdd:cd14069  158 LLNKMCGTLPYVAPELLAKKKYrAEPVDVWSCGIVLFAMLAGELPW-----DQPSDSCQEYSDWKENKKTYLTPWKKIDT 232
                        250       260
                 ....*....|....*....|....*....
gi 567218350 302 ELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14069  233 AALSLLRKILTENPNKRITIEDIKKHPWY 261
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
76-328 1.88e-36

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: 132.38  E-value: 1.88e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQlniDEAIRK------SIAQELKINQSSQCPYLVNSYQSFYDN--GAISLILEY 147
Cdd:cd14119    1 LGEGSYGKVKEVLDTETLCRRAVKILK---KRKLRRipngeaNVKREIQILRRLNHRNVIKLVDVLYNEekQKLYMVMEY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 148 MdGGSLADFLKSV--KTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTA--GL 223
Cdd:cd14119   78 C-VGGLQEMLDSApdKRLPIWQAHGYFVQLIDGLEYLH-SQGIIHKDIKPGNLLLTTDGTLKISDFGVAEALDLFAedDT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 224 ANTFVGTYNYMSPERIVGNKY--GNKSDIWSLGLVVLECATGKFPYlppdqeeTWSSVFELMEAIVDQP---PPALPsen 298
Cdd:cd14119  156 CTTSQGSPAFQPPEIANGQDSfsGFKVDIWSAGVTLYNMTTGKYPF-------EGDNIYKLFENIGKGEytiPDDVD--- 225
                        250       260       270
                 ....*....|....*....|....*....|
gi 567218350 299 fsPELSSFISTCLQKDPNSRSSAKELMEHP 328
Cdd:cd14119  226 --PDLQDLLRGMLEKDPEKRFTIEQIRQHP 253
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
70-326 2.28e-36

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: 132.29  E-value: 2.28e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350    70 LDMVKFLGKGSSGVV---QLVQHKWTGQFF-ALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLIL 145
Cdd:smart00221   1 LTLGKKLGEGAFGEVykgTLKGKGDGKEVEvAVKTLKEDASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350   146 EYMDGGSLADFLKS--VKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTN---- 219
Cdd:smart00221  81 EYMPGGDLLDYLRKnrPKELSLSDLLSFALQIARGMEYLE-SKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDddyy 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350   220 TAGLANtfvGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPYLPPdqeetwsSVFELMEAIVD---QPPPalp 295
Cdd:smart00221 160 KVKGGK---LPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEEPYPGM-------SNAEVLEYLKKgyrLPKP--- 226
                          250       260       270
                   ....*....|....*....|....*....|.
gi 567218350   296 sENFSPELSSFISTCLQKDPNSRSSAKELME 326
Cdd:smart00221 227 -PNCPPELYKLMLQCWAEDPEDRPTFSELVE 256
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
70-327 3.34e-36

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: 131.85  E-value: 3.34e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350   70 LDMVKFLGKGSSGVVqlVQHKWTGQFF------ALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISL 143
Cdd:pfam07714   1 LTLGEKLGEGAFGEV--YKGTLKGEGEntkikvAVKTLKEGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  144 ILEYMDGGSLADFLKSVK-TIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNtag 222
Cdd:pfam07714  79 VTEYMPGGDLLDFLRKHKrKLTLKDLLSMALQIAKGMEYLE-SKNFVHRDLAARNCLVSENLVVKISDFGLSRDIYD--- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  223 lantfvgTYNY------------MSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPYlpPDQeetwsSVFELMEAIVDQ 289
Cdd:pfam07714 155 -------DDYYrkrgggklpikwMAPESLKDGKFTSKSDVWSFGVLLWEIFTlGEQPY--PGM-----SNEEVLEFLEDG 220
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 567218350  290 PPPALPsENFSPELSSFISTCLQKDPNSRSSAKELMEH 327
Cdd:pfam07714 221 YRLPQP-ENCPDELYDLMKQCWAYDPEDRPTFSELVED 257
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
72-329 3.64e-36

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: 132.44  E-value: 3.64e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  72 MVKFLGKGSSGVV----QLVQHKWTgqffALKVIQLNID------EAIRKSIAQELKINQSSQCPYLVNSYQSF-YDNGA 140
Cdd:cd13990    4 LLNLLGKGGFSEVykafDLVEQRYV----ACKIHQLNKDwseekkQNYIKHALREYEIHKSLDHPRIVKLYDVFeIDTDS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 141 ISLILEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLH-HDKHIIHRDLKPSNLLINHR---GEVKITDFGVSTV 216
Cdd:cd13990   80 FCTVLEYCDGNDLDFYLKQHKSIPEREARSIIMQVVSALKYLNeIKPPIIHYDLKPGNILLHSGnvsGEIKITDFGLSKI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 217 MTNTAG------LANTFVGTYNYMSPERIVGN----KYGNKSDIWSLGLVVLECATGKFPYlppdqEETWSSVFELME-A 285
Cdd:cd13990  160 MDDESYnsdgmeLTSQGAGTYWYLPPECFVVGktppKISSKVDVWSVGVIFYQMLYGRKPF-----GHNQSQEAILEEnT 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 567218350 286 IVDQPPPALPSEN-FSPELSSFISTCLQKDPNSRSSAKELMEHPF 329
Cdd:cd13990  235 ILKATEVEFPSKPvVSSEAKDFIRRCLTYRKEDRPDVLQLANDPY 279
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
67-327 5.06e-36

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: 132.11  E-value: 5.06e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  67 LSDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILE 146
Cdd:cd14046    5 LTDFEELQVLGKGAFGQVVKVRNKLDGRYYAIKKIKLRSESKNNSRILREVMLLSRLNHQHVVRYYQAWIERANLYIQME 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 147 YMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLhHDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANT 226
Cdd:cd14046   85 YCEKSTLRDLIDSGLFQDTDRLWRLFRQILEGLAYI-HSQGIIHRDLKPVNIFLDSNGNVKIGDFGLATSNKLNVELATQ 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 227 F------------------VGTYNYMSPERIVGNK--YGNKSDIWSLGLVVLECatgkfpYLPPDQeeTWSSVFELMeaI 286
Cdd:cd14046  164 DinkstsaalgssgdltgnVGTALYVAPEVQSGTKstYNEKVDMYSLGIIFFEM------CYPFST--GMERVQILT--A 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 567218350 287 VDQPPPALPS---ENFSPELSSFISTCLQKDPNSRSSAKELMEH 327
Cdd:cd14046  234 LRSVSIEFPPdfdDNKHSKQAKLIRWLLNHDPAKRPSAQELLKS 277
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
73-334 6.42e-36

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: 133.16  E-value: 6.42e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  73 VKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNI--DEAIRKSIAQELKIN-QSSQCPYLVNSYQSFYDNGAISLILEYMD 149
Cdd:cd05604    1 LKVIGKGSFGKVLLAKRKRDGKYYAVKVLQKKVilNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTDKLYFVLDFVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 150 GGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVG 229
Cdd:cd05604   81 GGELFFHLQRERSFPEPRARFYAAEIASALGYLHSIN-IVYRDLKPENILLDSQGHIVLTDFGLCKEGISNSDTTTTFCG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 230 TYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVfeLMEAIVDQPPPALPSenfspelSSFIST 309
Cdd:cd05604  160 TPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENI--LHKPLVLRPGISLTA-------WSILEE 230
                        250       260
                 ....*....|....*....|....*....
gi 567218350 310 CLQKDPNSRSSAK----ELMEHPFLNKYN 334
Cdd:cd05604  231 LLEKDRQLRLGAKedflEIKNHPFFESIN 259
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
64-331 8.39e-36

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: 131.29  E-value: 8.39e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  64 ELSLSDLdmvkfLGKGSSGVVQLVQHKWTGQF-FALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAIS 142
Cdd:cd14202    3 EFSRKDL-----IGHGAFAVVFKGRHKEKHDLeVAVKCINKKNLAKSQTLLGKEIKILKELKHENIVALYDFQEIANSVY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 143 LILEYMDGGSLADFLKSVKTIPESYLSaIFKQVLQGLIYLHHDKHIIHRDLKPSNLLINHRG---------EVKITDFGV 213
Cdd:cd14202   78 LVMEYCNGGDLADYLHTMRTLSEDTIR-LFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGgrksnpnniRIKIADFGF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 214 STVMTNTAgLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETwSSVFELMEAIVdqppPA 293
Cdd:cd14202  157 ARYLQNNM-MAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQDL-RLFYEKNKSLS----PN 230
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 567218350 294 LPSENFSPeLSSFISTCLQKDPNSRSSAKELMEHPFLN 331
Cdd:cd14202  231 IPRETSSH-LRQLLLGLLQRNQKDRMDFDEFFHHPFLD 267
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
59-334 1.63e-35

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 132.25  E-value: 1.63e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  59 KPADDELSLSDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKViqLNIDEAIR----KSIAQELKINQSSQCPYLVNSYQS 134
Cdd:PTZ00263   9 KPDTSSWKLSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKC--LKKREILKmkqvQHVAQEKSILMELSHPFIVNMMCS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 135 FYDNGAISLILEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVS 214
Cdd:PTZ00263  87 FQDENRVYFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLH-SKDIIYRDLKPENLLLDNKGHVKVTDFGFA 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 215 TVMTNTaglANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGkfpyLPPDQEETWSSVFE-LMEAIVDQPppa 293
Cdd:PTZ00263 166 KKVPDR---TFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAG----YPPFFDDTPFRIYEkILAGRLKFP--- 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 567218350 294 lpsENFSPELSSFISTCLQKDPNSR-----SSAKELMEHPFLNKYN 334
Cdd:PTZ00263 236 ---NWFDGRARDLVKGLLQTDHTKRlgtlkGGVADVKNHPYFHGAN 278
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
74-329 1.98e-35

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: 131.76  E-value: 1.98e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQH---KWTGQFFALKVIQ-LNI-----DEAIRKSiaqELKINQSSQCPYLVNSYQSFYDNGAISLI 144
Cdd:cd05584    2 KVLGKGGYGKVFQVRKttgSDKGKIFAMKVLKkASIvrnqkDTAHTKA---ERNILEAVKHPFIVDLHYAFQTGGKLYLI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 145 LEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLA 224
Cdd:cd05584   79 LEYLSGGELFMHLEREGIFMEDTACFYLAEITLALGHLH-SLGIIYRDLKPENILLDAQGHVKLTDFGLCKESIHDGTVT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 225 NTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETwssvfelMEAIVD---QPPPALpsenfSP 301
Cdd:cd05584  158 HTFCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKT-------IDKILKgklNLPPYL-----TN 225
                        250       260       270
                 ....*....|....*....|....*....|...
gi 567218350 302 ELSSFISTCLQKDPNSR-----SSAKELMEHPF 329
Cdd:cd05584  226 EARDLLKKLLKRNVSSRlgsgpGDAEEIKAHPF 258
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
74-329 2.06e-35

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: 130.07  E-value: 2.06e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSL 153
Cdd:cd14185    6 RTIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGKEDMIESEILIIKSLSHPNIVKLFEVYETEKEIYLILEYVRGGDL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 154 AD-FLKSVKtIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGE----VKITDFGVSTVMTntaGLANTFV 228
Cdd:cd14185   86 FDaIIESVK-FTEHDAALMIIDLCEALVYIH-SKHIVHRDLKPENLLVQHNPDksttLKLADFGLAKYVT---GPIFTVC 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 229 GTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPP--DQEETWSSV----FELMeaivdqpPPALpsENFSPE 302
Cdd:cd14185  161 GTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRSPerDQEELFQIIqlghYEFL-------PPYW--DNISEA 231
                        250       260
                 ....*....|....*....|....*..
gi 567218350 303 LSSFISTCLQKDPNSRSSAKELMEHPF 329
Cdd:cd14185  232 AKDLISRLLVVDPEKRYTAKQVLQHPW 258
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
71-329 2.81e-35

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: 130.23  E-value: 2.81e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  71 DMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIA-QELKINQSSQCPYLVNSYQSFYDNGAISLILEYMD 149
Cdd:cd07846    4 ENLGLVGEGSYGMVMKCRHKETGQIVAIKKFLESEDDKMVKKIAmREIKMLKQLRHENLVNLIEVFRRKKRWYLVFEFVD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 150 GGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHDkHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVG 229
Cdd:cd07846   84 HTVLDDLEKYPNGLDESRVRKYLFQILRGIDFCHSH-NIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDYVA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 230 TYNYMSPERIVGN-KYGNKSDIWSLGLVVLECATGKfPYLPPDQE--------ETWSSVFELMEAIVDQPPP----ALPS 296
Cdd:cd07846  163 TRWYRAPELLVGDtKYGKAVDVWAVGCLVTEMLTGE-PLFPGDSDidqlyhiiKCLGNLIPRHQELFQKNPLfagvRLPE 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 567218350 297 -----------ENFSPELSSFISTCLQKDPNSRSSAKELMEHPF 329
Cdd:cd07846  242 vkeveplerryPKLSGVVIDLAKKCLHIDPDKRPSCSELLHHEF 285
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
74-330 3.22e-35

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: 129.78  E-value: 3.22e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVIQL---NIDeaIRKSIAQELKI-NQSSQCPYLVNSYQSFYDNGAISLILEYMD 149
Cdd:cd14106   14 TPLGRGKFAVVRKCIHKETGKEYAAKFLRKrrrGQD--CRNEILHEIAVlELCKDCPRVVNLHEVYETRSELILILELAA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 150 GGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLhHDKHIIHRDLKPSNLLINHR---GEVKITDFGVSTVMTNTAGLaNT 226
Cdd:cd14106   92 GGELQTLLDEEECLTEADVRRLMRQILEGVQYL-HERNIVHLDLKPQNILLTSEfplGDIKLCDFGISRVIGEGEEI-RE 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 227 FVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSvfelmeaiVDQPPPALPSENF---SPEL 303
Cdd:cd14106  170 ILGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLN--------ISQCNLDFPEELFkdvSPLA 241
                        250       260
                 ....*....|....*....|....*..
gi 567218350 304 SSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14106  242 IDFIKRLLVKDPEKRLTAKECLEHPWL 268
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
65-350 3.26e-35

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: 132.46  E-value: 3.26e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  65 LSLSDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAI--RKSIAQELKINQSSQCPYLVNSYQSFYDNGAIS 142
Cdd:cd05600    8 LKLSDFQILTQVGQGGYGSVFLARKKDTGEICALKIMKKKVLFKLneVNHVLTERDILTTTNSPWLVKLLYAFQDPENVY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 143 LILEYMDGGSLADFLKSVKTIPES----YLSAIFKQVlQGLiylhHDKHIIHRDLKPSNLLINHRGEVKITDFGVST--- 215
Cdd:cd05600   88 LAMEYVPGGDFRTLLNNSGILSEEharfYIAEMFAAI-SSL----HQLGYIHRDLKPENFLIDSSGHIKLTDFGLASgtl 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 216 ------VM-------TNTAGL---------------------ANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECA 261
Cdd:cd05600  163 spkkieSMkirleevKNTAFLeltakerrniyramrkedqnyANSVVGSPDYMAPEVLRGEGYDLTVDYWSLGCILFECL 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 262 TGKFPYLPPDQEETWSSVF---ELMEAIVDQPPPALPseNFSPELSSFISTCLQKDPNSRSSAKELMEHPFLNKYN---- 334
Cdd:cd05600  243 VGFPPFSGSTPNETWANLYhwkKTLQRPVYTDPDLEF--NLSDEAWDLITKLITDPQDRLQSPEQIKNHPFFKNIDwdrl 320
                        330       340
                 ....*....|....*....|....*...
gi 567218350 335 ------------NSEINlASYFTDAGSP 350
Cdd:cd05600  321 regskppfipelESEID-TSYFDDFNDE 347
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
51-332 5.34e-35

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


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 130.54  E-value: 5.34e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  51 EPEVLSPIKPADDELSLSDLDMVkflGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRK--SIAQELKINQSSQCPYL 128
Cdd:cd06633    7 DPEIADLFYKDDPEEIFVDLHEI---GHGSFGAVYFATNSHTNEVVAIKKMSYSGKQTNEKwqDIIKEVKFLQQLKHPNT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 129 VNSYQSFYDNGAISLILEYMDGgSLADFLK-SVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVK 207
Cdd:cd06633   84 IEYKGCYLKDHTAWLVMEYCLG-SASDLLEvHKKPLQEVEIAAITHGALQGLAYLH-SHNMIHRDIKAGNILLTEPGQVK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 208 ITDFGVSTVmtntAGLANTFVGTYNYMSPERIVG---NKYGNKSDIWSLGLVVLECATGKFPYLppdQEETWSSVFElme 284
Cdd:cd06633  162 LADFGSASI----ASPANSFVGTPYWMAPEVILAmdeGQYDGKVDIWSLGITCIELAERKPPLF---NMNAMSALYH--- 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 567218350 285 aIVDQPPPALPSENFSPELSSFISTCLQKDPNSRSSAKELMEHPFLNK 332
Cdd:cd06633  232 -IAQNDSPTLQSNEWTDSFRGFVDYCLQKIPQERPSSAELLRHDFVRR 278
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
76-330 6.03e-35

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


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 129.46  E-value: 6.03e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQL-NIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLA 154
Cdd:cd14086    9 LGKGAFSVVRRCVQKSTGQEFAAKIINTkKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFDLVTGGELF 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 155 DFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGE---VKITDFGVSTVMTNTAGLANTFVGTY 231
Cdd:cd14086   89 EDIVAREFYSEADASHCIQQILESVNHCH-QNGIVHRDLKPENLLLASKSKgaaVKLADFGLAIEVQGDQQAWFGFAGTP 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 232 NYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSsvfELMEAIVDQPPPALPSenFSPELSSFISTCL 311
Cdd:cd14086  168 GYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYA---QIKAGAYDYPSPEWDT--VTPEAKDLINQML 242
                        250
                 ....*....|....*....
gi 567218350 312 QKDPNSRSSAKELMEHPFL 330
Cdd:cd14086  243 TVNPAKRITAAEALKHPWI 261
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
69-332 6.05e-35

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


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 129.01  E-value: 6.05e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  69 DLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIrKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYM 148
Cdd:cd06645   12 DFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEPGEDF-AVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICMEFC 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 149 DGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFV 228
Cdd:cd06645   91 GGGSLQDIYHVTGPLSESQIAYVSRETLQGLYYLH-SKGKMHRDIKGANILLTDNGHVKLADFGVSAQITATIAKRKSFI 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 229 GTYNYMSPERIVGNK---YGNKSDIWSLGLVVLECATGKfpylPPDQEETWSSVFELMEAIVDQPPPALPSENFSPELSS 305
Cdd:cd06645  170 GTPYWMAPEVAAVERkggYNQLCDIWAVGITAIELAELQ----PPMFDLHPMRALFLMTKSNFQPPKLKDKMKWSNSFHH 245
                        250       260
                 ....*....|....*....|....*..
gi 567218350 306 FISTCLQKDPNSRSSAKELMEHPFLNK 332
Cdd:cd06645  246 FVKMALTKNPKKRPTAEKLLQHPFVTQ 272
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
74-329 6.10e-35

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: 129.01  E-value: 6.10e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVIQLNID--EAIRKSIAQELKINQSSQCPY--LVNSYQSFYD--NGAISLILEY 147
Cdd:cd06652    8 KLLGQGAFGRVYLCYDADTGRELAVKQVQFDPEspETSKEVNALECEIQLLKNLLHerIVQYYGCLRDpqERTLSIFMEY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 148 MDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKITDFGVS----TVMTNTAGL 223
Cdd:cd06652   88 MPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNM-IVHRDIKGANILRDSVGNVKLGDFGASkrlqTICLSGTGM 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 224 aNTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKfpylPPdqeetWSSvFELMEA---IVDQPP-PALPsenf 299
Cdd:cd06652  167 -KSVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEK----PP-----WAE-FEAMAAifkIATQPTnPQLP---- 231
                        250       260       270
                 ....*....|....*....|....*....|...
gi 567218350 300 sPELSSFISTCLQK---DPNSRSSAKELMEHPF 329
Cdd:cd06652  232 -AHVSDHCRDFLKRifvEAKLRPSADELLRHTF 263
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
76-318 7.62e-35

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: 128.77  E-value: 7.62e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQ-FFALKVIQLN----------IDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLI 144
Cdd:cd08528    8 LGSGAFGCVYKVRKKSNGQtLLALKEINMTnpafgrteqeRDKSVGDIISEVNIIKEQLRHPNIVRYYKTFLENDRLYIV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 145 LEYMDGGSLADFLKSVKT----IPESYLSAIFKQVLQGLIYLHHDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNT 220
Cdd:cd08528   88 MELIEGAPLGEHFSSLKEknehFTEDRIWNIFVQMVLALRYLHKEKQIVHRDLKPNNIMLGEDDKVTITDFGLAKQKGPE 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 221 AGLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATgkfpYLPPDQEEtwsSVFELMEAIVDQPPPALPSENFS 300
Cdd:cd08528  168 SSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCT----LQPPFYST---NMLTLATKIVEAEYEPLPEGMYS 240
                        250
                 ....*....|....*...
gi 567218350 301 PELSSFISTCLQKDPNSR 318
Cdd:cd08528  241 DDITFVIRSCLTPDPEAR 258
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
74-334 8.88e-35

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: 130.13  E-value: 8.88e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVIQlniDEAIRKS-----IAQE---LKINQSSqcPYLVNSYQSFYDNGAISLIL 145
Cdd:cd05575    1 KVIGKGSFGKVLLARHKAEGKLYAVKVLQ---KKAILKRnevkhIMAErnvLLKNVKH--PFLVGLHYSFQTKDKLYFVL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 146 EYMDGGSLADFLKSVKTIPES---YLSAifkQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAG 222
Cdd:cd05575   76 DYVNGGELFFHLQRERHFPEPrarFYAA---EIASALGYLH-SLNIIYRDLKPENILLDSQGHVVLTDFGLCKEGIEPSD 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 223 LANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGkfpyLPPdqeeTWS-SVFELMEAIVDQpPPALPsENFSP 301
Cdd:cd05575  152 TTSTFCGTPEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYG----LPP----FYSrDTAEMYDNILHK-PLRLR-TNVSP 221
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 567218350 302 ELSSFISTCLQKDPNSRSSAK----ELMEHPFLNKYN 334
Cdd:cd05575  222 SARDLLEGLLQKDRTKRLGSGndflEIKNHSFFRPIN 258
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
73-335 1.16e-34

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


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 129.57  E-value: 1.16e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  73 VKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIR-KSIAQELKINQSSQCPYLVN--------SYQSFYDngaISL 143
Cdd:cd07834    5 LKPIGSGAYGVVCSAYDKRTGRKVAIKKISNVFDDLIDaKRILREIKILRHLKHENIIGlldilrppSPEEFND---VYI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 144 ILEYMDggslADF---LKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVS-TVMTN 219
Cdd:cd07834   82 VTELME----TDLhkvIKSPQPLTDDHIQYFLYQILRGLKYLH-SAGVIHRDLKPSNILVNSNCDLKICDFGLArGVDPD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 220 TAGLANT-FVGTYNYMSPERIVG-NKYGNKSDIWSLGLVVLECATGK--FP---YL------------PPDQEETWSSVF 280
Cdd:cd07834  157 EDKGFLTeYVVTRWYRAPELLLSsKKYTKAIDIWSVGCIFAELLTRKplFPgrdYIdqlnlivevlgtPSEEDLKFISSE 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 281 ELMEAIVDQPP-PALPSENFSPELSS----FISTCLQKDPNSRSSAKELMEHPFLNKYNN 335
Cdd:cd07834  237 KARNYLKSLPKkPKKPLSEVFPGASPeaidLLEKMLVFNPKKRITADEALAHPYLAQLHD 296
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
66-318 1.87e-34

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: 128.23  E-value: 1.87e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  66 SLSDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLN--IDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISL 143
Cdd:cd08229   22 TLANFRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIFdlMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNI 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 144 ILEYMDGGSLADFLKSVKT----IPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTN 219
Cdd:cd08229  102 VLELADAGDLSRMIKHFKKqkrlIPEKTVWKYFVQLCSALEHMH-SRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSS 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 220 TAGLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQeetwsSVFELMEAIVDQPPPALPSENF 299
Cdd:cd08229  181 KTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKM-----NLYSLCKKIEQCDYPPLPSDHY 255
                        250
                 ....*....|....*....
gi 567218350 300 SPELSSFISTCLQKDPNSR 318
Cdd:cd08229  256 SEELRQLVNMCINPDPEKR 274
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
76-329 2.57e-34

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: 127.10  E-value: 2.57e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHK-WTGQFFALKVIQlniDEAIRKS---IAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGG 151
Cdd:cd14120    1 IGHGAFAVVFKGRHRkKPDLPVAIKCIT---KKNLSKSqnlLGKEIKILKELSHENVVALLDCQETSSSVYLVMEYCNGG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 152 SLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGE---------VKITDFGVSTVMTNTAg 222
Cdd:cd14120   78 DLADYLQAKGTLSEDTIRVFLQQIAAAMKALH-SKGIVHRDLKPQNILLSHNSGrkpspndirLKIADFGFARFLQDGM- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 223 LANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYL---PPDQEETWSSVFELMeaivdqppPALPSENf 299
Cdd:cd14120  156 MAATLCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQaqtPQELKAFYEKNANLR--------PNIPSGT- 226
                        250       260       270
                 ....*....|....*....|....*....|
gi 567218350 300 SPELSSFISTCLQKDPNSRSSAKELMEHPF 329
Cdd:cd14120  227 SPALKDLLLGLLKRNPKDRIDFEDFFSHPF 256
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
64-338 4.14e-34

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: 128.50  E-value: 4.14e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  64 ELSLSDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNI---DEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGA 140
Cdd:cd05619    1 KLTIEDFVLHKMLGKGSFGKVFLAELKGTNQFFAIKALKKDVvlmDDDVECTMVEKRVLSLAWEHPFLTHLFCTFQTKEN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 141 ISLILEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTvmTNT 220
Cdd:cd05619   81 LFFVMEYLNGGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLH-SKGIVYRDLKLDNILLDKDGHIKIADFGMCK--ENM 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 221 AGLA--NTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFelmeaiVDQP--PPALPS 296
Cdd:cd05619  158 LGDAktSTFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSIR------MDNPfyPRWLEK 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 567218350 297 ENFSPELSSFIstclqKDPNSRSSAK-ELMEHPFLNKYNNSEI 338
Cdd:cd05619  232 EAKDILVKLFV-----REPERRLGVRgDIRQHPFFREINWEAL 269
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
74-329 4.30e-34

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: 126.68  E-value: 4.30e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVIQLNID-EAIRKSIAQ---ELKINQSSQCPYLVNSYQSFYDNGA--ISLILEY 147
Cdd:cd06653    8 KLLGRGAFGEVYLCYDADTGRELAVKQVPFDPDsQETSKEVNAlecEIQLLKNLRHDRIVQYYGCLRDPEEkkLSIFVEY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 148 MDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVS----TVMTNTAGL 223
Cdd:cd06653   88 MPGGSVKDQLKAYGALTENVTRRYTRQILQGVSYLH-SNMIVHRDIKGANILRDSAGNVKLGDFGASkriqTICMSGTGI 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 224 aNTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKfpylPPdqeetWSSvFELMEA---IVDQPP-PALPsENF 299
Cdd:cd06653  167 -KSVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEK----PP-----WAE-YEAMAAifkIATQPTkPQLP-DGV 234
                        250       260       270
                 ....*....|....*....|....*....|
gi 567218350 300 SPELSSFISTCLQKDpNSRSSAKELMEHPF 329
Cdd:cd06653  235 SDACRDFLRQIFVEE-KRRPTAEFLLRHPF 263
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
73-330 4.51e-34

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: 126.39  E-value: 4.51e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  73 VKFLGKGSSGVVQLVQHKWTGQFFALKVIQLN-IDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGG 151
Cdd:cd08221    5 VRVLGRGAFGEAVLYRKTEDNSLVVWKEVNLSrLSEKERRDALNEIDILSLLNHDNIITYYNHFLDGESLFIEMEYCNGG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 152 SLADFLKSVKT--IPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVG 229
Cdd:cd08221   85 NLHDKIAQQKNqlFPEEVVLWYLYQIVSAVSHIH-KAGILHRDIKTLNIFLTKADLVKLGDFGISKVLDSESSMAESIVG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 230 TYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQeetwssvFELMEAIVdQPPPALPSENFSPELSSFIST 309
Cdd:cd08221  164 TPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFDATNP-------LRLAVKIV-QGEYEDIDEQYSEEIIQLVHD 235
                        250       260
                 ....*....|....*....|.
gi 567218350 310 CLQKDPNSRSSAKELMEHPFL 330
Cdd:cd08221  236 CLHQDPEDRPTAEELLERPLL 256
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
44-332 6.10e-34

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: 127.47  E-value: 6.10e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  44 VRIVSQSEPEVLSPIKPADDELSLSDLdmvKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRK--SIAQELKINQ 121
Cdd:cd06635    4 SRAGSLKDPDIAELFFKEDPEKLFSDL---REIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEKwqDIIKEVKFLQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 122 SSQCPYLVNSYQSFYDNGAISLILEYMDGgSLADFLK-SVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLI 200
Cdd:cd06635   81 RIKHPNSIEYKGCYLREHTAWLVMEYCLG-SASDLLEvHKKPLQEIEIAAITHGALQGLAYLH-SHNMIHRDIKAGNILL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 201 NHRGEVKITDFGVSTVmtntAGLANTFVGTYNYMSPERIVG---NKYGNKSDIWSLGLVVLECATGKFPYLppdQEETWS 277
Cdd:cd06635  159 TEPGQVKLADFGSASI----ASPANSFVGTPYWMAPEVILAmdeGQYDGKVDVWSLGITCIELAERKPPLF---NMNAMS 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 567218350 278 SVFElmeaIVDQPPPALPSENFSPELSSFISTCLQKDPNSRSSAKELMEHPFLNK 332
Cdd:cd06635  232 ALYH----IAQNESPTLQSNEWSDYFRNFVDSCLQKIPQDRPTSEELLKHMFVLR 282
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
76-330 7.37e-34

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: 126.62  E-value: 7.37e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEA-IRKSIAQE---LKINQSSQCPYLVN----SYQSFYDNG-AISLILE 146
Cdd:cd07838    7 IGEGAYGTVYKARDLQDGRFVALKKVRVPLSEEgIPLSTIREialLKQLESFEHPNVVRlldvCHGPRTDRElKLTLVFE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 147 YMDGgSLADFLKSV--KTIPESYLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLa 224
Cdd:cd07838   87 HVDQ-DLATYLDKCpkPGLPPETIKDLMRQLLRGLDFLHSHR-IVHRDLKPQNILVTSDGQVKLADFGLARIYSFEMAL- 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 225 NTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKfPYLPPDQE-ETWSSVFELM-EAIVDQPPP--ALPSENFS 300
Cdd:cd07838  164 TSVVVTLWYRAPEVLLQSSYATPVDMWSVGCIFAELFNRR-PLFRGSSEaDQLGKIFDVIgLPSEEEWPRnsALPRSSFP 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 567218350 301 -----------PELSS----FISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd07838  243 sytprpfksfvPEIDEegldLLKKMLTFNPHKRISAFEALQHPYF 287
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
69-330 1.62e-33

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: 124.81  E-value: 1.62e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  69 DLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVI---QLNIDEAIR----KSIAQELKI----NQSSQcPYLVNSYQSFYD 137
Cdd:cd14004    1 DYTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIfkeRILVDTWVRdrklGTVPLEIHIldtlNKRSH-PNIVKLLDFFED 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 138 NGAISLILE-YMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTV 216
Cdd:cd14004   80 DEFYYLVMEkHGSGMDLFDFIERKPNMDEKEAKYIFRQVADAVKHLH-DQGIVHRDIKDENVILDGNGTIKLIDFGSAAY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 217 MTNtaGLANTFVGTYNYMSPERIVGNKYGNKS-DIWSLGLVVLECATGKFPYlppdqeetwSSVFELMEAivDQPPPALP 295
Cdd:cd14004  159 IKS--GPFDTFVGTIDYAAPEVLRGNPYGGKEqDIWALGVLLYTLVFKENPF---------YNIEEILEA--DLRIPYAV 225
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 567218350 296 SEnfspELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14004  226 SE----DLIDLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
76-330 1.77e-33

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: 125.13  E-value: 1.77e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRK-----SIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDG 150
Cdd:cd14194   13 LGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRRgvsreDIEREVSILKEIQHPNVITLHEVYENKTDVILILELVAG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 151 GSLADFLKSVKTIPESYLSAIFKQVLQGLIYLhHDKHIIHRDLKPSNLLINHRG----EVKITDFGVSTVMTNTAGLANT 226
Cdd:cd14194   93 GELFDFLAEKESLTEEEATEFLKQILNGVYYL-HSLQIAHFDLKPENIMLLDRNvpkpRIKIIDFGLAHKIDFGNEFKNI 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 227 FvGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSV----FELMEAIVdqpppalpsENFSPE 302
Cdd:cd14194  172 F-GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVsavnYEFEDEYF---------SNTSAL 241
                        250       260
                 ....*....|....*....|....*...
gi 567218350 303 LSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14194  242 AKDFIRRLLVKDPKKRMTIQDSLQHPWI 269
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
69-330 2.11e-33

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: 124.76  E-value: 2.11e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  69 DLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIrKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYM 148
Cdd:cd06646   10 DYELIQRVGSGTYGDVYKARNLHTGELAAVKIIKLEPGDDF-SLIQQEIFMVKECKHCNIVAYFGSYLSREKLWICMEYC 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 149 DGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFV 228
Cdd:cd06646   89 GGGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLH-SKGKMHRDIKGANILLTDNGDVKLADFGVAAKITATIAKRKSFI 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 229 GTYNYMSPERIVGNK---YGNKSDIWSLGLVVLECATGKfpylPPDQEETWSSVFELMEAIVDQPPPALPSENFSPELSS 305
Cdd:cd06646  168 GTPYWMAPEVAAVEKnggYNQLCDIWAVGITAIELAELQ----PPMFDLHPMRALFLMSKSNFQPPKLKDKTKWSSTFHN 243
                        250       260
                 ....*....|....*....|....*
gi 567218350 306 FISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd06646  244 FVKISLTKNPKKRPTAERLLTHLFV 268
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
71-330 2.33e-33

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: 124.43  E-value: 2.33e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  71 DMVKFLGKGSSGVVQLVQHKWTGQFFALKVI-QLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMD 149
Cdd:cd14071    3 DIERTIGKGNFAVVKLARHRITKTEVAIKIIdKSQLDEENLKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEYAS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 150 GGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLaNTFVG 229
Cdd:cd14071   83 NGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCH-KRHIVHRDLKAENLLLDANMNIKIADFGFSNFFKPGELL-KTWCG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 230 TYNYMSPERIVGNKY-GNKSDIWSLGLV--VLECatGKFPY----LPPDQEETWSSVFELmeaivdqppPALPSEnfspE 302
Cdd:cd14071  161 SPPYAAPEVFEGKEYeGPQLDIWSLGVVlyVLVC--GALPFdgstLQTLRDRVLSGRFRI---------PFFMST----D 225
                        250       260
                 ....*....|....*....|....*...
gi 567218350 303 LSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14071  226 CEHLIRRMLVLDPSKRLTIEQIKKHKWM 253
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
76-325 3.15e-33

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: 124.38  E-value: 3.15e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVI------QLNIDEAIRKSIAQELKIN-QSSQCPYLVNSYQSFYDNGAISLILEYM 148
Cdd:cd13993    8 IGEGAYGVVYLAVDLRTGRKYAIKCLyksgpnSKDGNDFQKLPQLREIDLHrRVSRHPNIITLHDVFETEVAIYIVLEYC 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 149 DGGSLADFLKSVKTIPESYLSA--IFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGE-VKITDFGVSTV--MTNTAGl 223
Cdd:cd13993   88 PNGDLFEAITENRIYVGKTELIknVFLQLIDAVKHCH-SLGIYHRDIKPENILLSQDEGtVKLCDFGLATTekISMDFG- 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 224 antfVGTYNYMSPERIVGNKYGNKS------DIWSLGLVVLECATGKFPYLPPDQEE-TWSSVFELMEAIVDQPPPalps 296
Cdd:cd13993  166 ----VGSEFYMAPECFDEVGRSLKGypcaagDIWSLGIILLNLTFGRNPWKIASESDpIFYDYYLNSPNLFDVILP---- 237
                        250       260
                 ....*....|....*....|....*....
gi 567218350 297 enFSPELSSFISTCLQKDPNSRSSAKELM 325
Cdd:cd13993  238 --MSDDFYNLLRQIFTVNPNNRILLPELQ 264
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
74-330 4.39e-33

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: 124.26  E-value: 4.39e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVIQ-LNIDEAIRKSIAQELKINQSSQ-CPYLVNSYQSFYDNGAISLILEYMDGG 151
Cdd:cd14198   14 KELGRGKFAVVRQCISKSTGQEYAAKFLKkRRRGQDCRAEILHEIAVLELAKsNPRVVNLHEVYETTSEIILILEYAAGG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 152 SLADFLKS--VKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLL---INHRGEVKITDFGVSTVMTNtAGLANT 226
Cdd:cd14198   94 EIFNLCVPdlAEMVSENDIIRLIRQILEGVYYLH-QNNIVHLDLKPQNILlssIYPLGDIKIVDFGMSRKIGH-ACELRE 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 227 FVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFELMeaiVDqpppaLPSENFS--PELS 304
Cdd:cd14198  172 IMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNISQVN---VD-----YSEETFSsvSQLA 243
                        250       260
                 ....*....|....*....|....*..
gi 567218350 305 S-FISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14198  244 TdFIQKLLVKNPEKRPTAEICLSHSWL 270
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
76-330 4.52e-33

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


Pssm-ID: 270982 [Multi-domain]  Cd Length: 262  Bit Score: 123.83  E-value: 4.52e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHK--WTGQFFALKVIQLNI--DEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGG 151
Cdd:cd14080    8 IGEGSYSKVKLAEYTksGLKEKVACKIIDKKKapKDFLEKFLPRELEILRKLRHPNIIQVYSIFERGSKVFIFMEYAEHG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 152 SLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAG--LANTFVG 229
Cdd:cd14080   88 DLLEYIQKRGALSESQARIWFRQLALAVQYLH-SLDIAHRDLKCENILLDSNNNVKLSDFGFARLCPDDDGdvLSKTFCG 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 230 TYNYMSPERIVGNKY-GNKSDIWSLGLVVLECATGKFPYlppDQeetwSSVFELMEAIVDQP---PPALpsENFSPELSS 305
Cdd:cd14080  167 SAAYAAPEILQGIPYdPKKYDIWSLGVILYIMLCGSMPF---DD----SNIKKMLKDQQNRKvrfPSSV--KKLSPECKD 237
                        250       260
                 ....*....|....*....|....*
gi 567218350 306 FISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14080  238 LIDQLLEPDPTKRATIEEILNHPWL 262
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
73-330 5.14e-33

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


Pssm-ID: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 123.53  E-value: 5.14e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  73 VKFLGKGSSG-VVQLVQHKwTGQFFALKVIQlNIDEAIRKSIaQELKI----NQSSQC--PYLVNSYQSFYDNGAISLIL 145
Cdd:cd14133    4 LEVLGKGTFGqVVKCYDLL-TGEEVALKIIK-NNKDYLDQSL-DEIRLlellNKKDKAdkYHIVRLKDVFYFKNHLCIVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 146 EyMDGGSLADFLKSVKTIPES--YLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLI--NHRGEVKITDFGVSTVMTNTA 221
Cdd:cd14133   81 E-LLSQNLYEFLKQNKFQYLSlpRIRKIAQQILEALVFLHSLG-LIHCDLKPENILLasYSRCQIKIIDFGSSCFLTQRL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 222 glaNTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKfPYLPPDqeetwsSVFELMEAIVD---QPPPALPSEN 298
Cdd:cd14133  159 ---YSYIQSRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGE-PLFPGA------SEVDQLARIIGtigIPPAHMLDQG 228
                        250       260       270
                 ....*....|....*....|....*....|....
gi 567218350 299 FS--PELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14133  229 KAddELFVDFLKKLLEIDPKERPTASQALSHPWL 262
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
69-328 5.15e-33

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


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 123.26  E-value: 5.15e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  69 DLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNI-DEAIRKSIAQELKINQS-SQCPYLVNSYQSFYDNGAISLILE 146
Cdd:cd13997    1 HFHELEQIGSGSFSEVFKVRSKVDGCLYAVKKSKKPFrGPKERARALREVEAHAAlGQHPNIVRYYSSWEEGGHLYIQME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 147 YMDGGSLADFLKsvKTIPESYLS-----AIFKQVLQGLIYLHHdKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTnTA 221
Cdd:cd13997   81 LCENGSLQDALE--ELSPISKLSeaevwDLLLQVALGLAFIHS-KGIVHLDIKPDNIFISNKGTCKIGDFGLATRLE-TS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 222 GLANTfvGTYNYMSPERIVGNK-YGNKSDIWSLGLVVLECATGkfpYLPPDQEETWSsvfELMEAIvdqpPPALPSENFS 300
Cdd:cd13997  157 GDVEE--GDSRYLAPELLNENYtHLPKADIFSLGVTVYEAATG---EPLPRNGQQWQ---QLRQGK----LPLPPGLVLS 224
                        250       260
                 ....*....|....*....|....*...
gi 567218350 301 PELSSFISTCLQKDPNSRSSAKELMEHP 328
Cdd:cd13997  225 QELTRLLKVMLDPDPTRRPTADQLLAHD 252
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
76-330 5.79e-33

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: 123.93  E-value: 5.79e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNID-------EAIRKSIAQELKI-NQSSQCPYLVNSYQSFYDNGAISLILEY 147
Cdd:cd14181   18 IGRGVSSVVRRCVHRHTGQEFAVKIIEVTAErlspeqlEEVRSSTLKEIHIlRQVSGHPSIITLIDSYESSTFIFLVFDL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 148 MDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHDkHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLaNTF 227
Cdd:cd14181   98 MRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHAN-NIVHRDLKPENILLDDQLHIKLSDFGFSCHLEPGEKL-REL 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 228 VGTYNYMSPERI------VGNKYGNKSDIWSLGLVVLECATGKFPYlppdqeetWSSVFELMEAIVDQPPPALPS---EN 298
Cdd:cd14181  176 CGTPGYLAPEILkcsmdeTHPGYGKEVDLWACGVILFTLLAGSPPF--------WHRRQMLMLRMIMEGRYQFSSpewDD 247
                        250       260       270
                 ....*....|....*....|....*....|..
gi 567218350 299 FSPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14181  248 RSSTVKDLISRLLVVDPEIRLTAEQALQHPFF 279
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
61-330 6.54e-33

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: 125.92  E-value: 6.54e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  61 ADDELSLSDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQ---LNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYD 137
Cdd:cd05618   13 ASSSLGLQDFDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKkelVNDDEDIDWVQTEKHVFEQASNHPFLVGLHSCFQT 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 138 NGAISLILEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVM 217
Cdd:cd05618   93 ESRLFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLH-ERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEG 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 218 TNTAGLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPY------LPPDQeETWSSVFE-LMEAIVDQP 290
Cdd:cd05618  172 LRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFdivgssDNPDQ-NTEDYLFQvILEKQIRIP 250
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 567218350 291 ppalpsENFSPELSSFISTCLQKDPNSR------SSAKELMEHPFL 330
Cdd:cd05618  251 ------RSLSVKAASVLKSFLNKDPKERlgchpqTGFADIQGHPFF 290
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
74-330 7.62e-33

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


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 123.20  E-value: 7.62e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVIQLN--IDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGG 151
Cdd:cd14188    7 KVLGKGGFAKCYEMTDLTTNKVYAAKIIPHSrvSKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRR 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 152 SLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVGTY 231
Cdd:cd14188   87 SMAHILKARKVLTEPEVRYYLRQIVSGLKYLH-EQEILHRDLKLGNFFINENMELKVGDFGLAARLEPLEHRRRTICGTP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 232 NYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFELMEaivdqpppALPSENFSPElSSFISTCL 311
Cdd:cd14188  166 NYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARY--------SLPSSLLAPA-KHLIASML 236
                        250
                 ....*....|....*....
gi 567218350 312 QKDPNSRSSAKELMEHPFL 330
Cdd:cd14188  237 SKNPEDRPSLDEIIRHDFF 255
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
65-318 8.14e-33

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: 125.52  E-value: 8.14e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  65 LSLSDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNI---DEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAI 141
Cdd:cd05617   12 LGLQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELvhdDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 142 SLILEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTA 221
Cdd:cd05617   92 FLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLH-ERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPG 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 222 GLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFELMEAIVDQpPPALPsENFSP 301
Cdd:cd05617  171 DTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNTEDYLFQVILEK-PIRIP-RFLSV 248
                        250
                 ....*....|....*..
gi 567218350 302 ELSSFISTCLQKDPNSR 318
Cdd:cd05617  249 KASHVLKGFLNKDPKER 265
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
73-328 9.33e-33

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: 122.42  E-value: 9.33e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  73 VKFLGKGSSGVVQLVQHKWTGQFFALKVI-QLNIDEAIRKSIAQEL-KINQSSQCPYLVNSYQSFYDNGAISLILEYMDG 150
Cdd:cd14050    6 LSKLGEGSFGEVFKVRSREDGKLYAVKRSrSRFRGEKDRKRKLEEVeRHEKLGEHPNCVRFIKAWEEKGILYIQTELCDT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 151 gSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVsTVMTNTAGLANTFVGT 230
Cdd:cd14050   86 -SLQQYCEETHSLPESEVWNILLDLLKGLKHLH-DHGLIHLDIKPANIFLSKDGVCKLGDFGL-VVELDKEDIHDAQEGD 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 231 YNYMSPERIVGnKYGNKSDIWSLGLVVLECATgkfpYLP-PDQEETWssvfelmEAIVDQPPPALPSENFSPELSSFIST 309
Cdd:cd14050  163 PRYMAPELLQG-SFTKAADIFSLGITILELAC----NLElPSGGDGW-------HQLRQGYLPEEFTAGLSPELRSIIKL 230
                        250
                 ....*....|....*....
gi 567218350 310 CLQKDPNSRSSAKELMEHP 328
Cdd:cd14050  231 MMDPDPERRPTAEDLLALP 249
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
76-330 2.62e-32

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: 122.40  E-value: 2.62e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNIDE------AIRK-SIAQELKinqssqCPYLVNSYQSFYDNGAISLILEYM 148
Cdd:cd07835    7 IGEGTYGVVYKARDKLTGEIVALKKIRLETEDegvpstAIREiSLLKELN------HPNIVRLLDVVHSENKLYLVFEFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 149 DggslADFLKSVKTIPESYLSA-IFK----QVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKITDFgvstvmtntaGL 223
Cdd:cd07835   81 D----LDLKKYMDSSPLTGLDPpLIKsylyQLLQGIAFCHSHR-VLHRDLKPQNLLIDTEGALKLADF----------GL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 224 ANTF---VGTYN-------YMSPERIVGNK-YGNKSDIWSLGLVVLECATGKfPYLPPDQE----------------ETW 276
Cdd:cd07835  146 ARAFgvpVRTYThevvtlwYRAPEILLGSKhYSTPVDIWSVGCIFAEMVTRR-PLFPGDSEidqlfrifrtlgtpdeDVW 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 567218350 277 SSVFELME---AIVDQPPPALPS--ENFSPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd07835  225 PGVTSLPDykpTFPKWARQDLSKvvPSLDEDGLDLLSQMLVYDPAKRISAKAALQHPYF 283
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
73-331 2.67e-32

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: 122.61  E-value: 2.67e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  73 VKFLGKGSSGVVQLVQHKWTGQFFALK-VIQlniDeaiRKSIAQELKINQSSQCPYLVNSYQSFYDNGA------ISLIL 145
Cdd:cd14137    9 EKVIGSGSFGVVYQAKLLETGEVVAIKkVLQ---D---KRYKNRELQIMRRLKHPNIVKLKYFFYSSGEkkdevyLNLVM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 146 EYMDGgSLADFL----KSVKTIPESYLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLINHR-GEVKITDFGVSTVMtnT 220
Cdd:cd14137   83 EYMPE-TLYRVIrhysKNKQTIPIIYVKLYSYQLFRGLAYLHS-LGICHRDIKPQNLLVDPEtGVLKLCDFGSAKRL--V 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 221 AGLAN-TFVGTYNYMSPERIVGNK-YGNKSDIWSLGLVVLECATGKfPYLPPDqeetwSSVFELMEAI------------ 286
Cdd:cd14137  159 PGEPNvSYICSRYYRAPELIFGATdYTTAIDIWSAGCVLAELLLGQ-PLFPGE-----SSVDQLVEIIkvlgtptreqik 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 567218350 287 ------VDQPPPALPSENFS--------PELSSFISTCLQKDPNSRSSAKELMEHPFLN 331
Cdd:cd14137  233 amnpnyTEFKFPQIKPHPWEkvfpkrtpPDAIDLLSKILVYNPSKRLTALEALAHPFFD 291
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
76-328 3.09e-32

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: 122.08  E-value: 3.09e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQlniDEAIRKSIA---QELKINQSSQCPYLVNSYQSFYDNGAI----------- 141
Cdd:cd14118    2 IGKGSYGIVKLAYNEEDNTLYAMKILS---KKKLLKQAGffrRPPPRRKPGALGKPLDPLDRVYREIAIlkkldhpnvvk 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 142 -------------SLILEYMDGGSLADfLKSVKTIPESYLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKI 208
Cdd:cd14118   79 lvevlddpnednlYMVFELVDKGAVME-VPTDNPLSEETARSYFRDIVLGIEYLHYQK-IIHRDIKPSNLLLGDDGHVKI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 209 TDFGVSTVMTNTAGLANTFVGTYNYMSPERIVG--NKYGNKS-DIWSLGlVVLEC-ATGKFPYLPPdqeetwsSVFELME 284
Cdd:cd14118  157 ADFGVSNEFEGDDALLSSTAGTPAFMAPEALSEsrKKFSGKAlDIWAMG-VTLYCfVFGRCPFEDD-------HILGLHE 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 567218350 285 AIVDQPPPALPSENFSPELSSFISTCLQKDPNSRSSAKELMEHP 328
Cdd:cd14118  229 KIKTDPVVFPDDPVVSEQLKDLILRMLDKNPSERITLPEIKEHP 272
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
71-330 3.30e-32

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


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 121.83  E-value: 3.30e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  71 DMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRK-----SIAQELKINQSSQCPYLVNSYQSFYDNGAISLIL 145
Cdd:cd14105    8 DIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKASRRgvsreDIEREVSILRQVLHPNIITLHDVFENKTDVVLIL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 146 EYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLhHDKHIIHRDLKPSNLLINHRGE----VKITDFGVSTVMTNTA 221
Cdd:cd14105   88 ELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYL-HTKNIAHFDLKPENIMLLDKNVpiprIKLIDFGLAHKIEDGN 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 222 GLANTFvGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSV----FELMEAIVDQpppalpse 297
Cdd:cd14105  167 EFKNIF-GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANItavnYDFDDEYFSN-------- 237
                        250       260       270
                 ....*....|....*....|....*....|....
gi 567218350 298 nfSPELSS-FISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14105  238 --TSELAKdFIRQLLVKDPRKRMTIQESLRHPWI 269
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
76-330 3.87e-32

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: 120.79  E-value: 3.87e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLnIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLAD 155
Cdd:cd14103    1 LGRGKFGTVYRCVEKATGKELAAKFIKC-RKAKDREDVRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAGGELFE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 156 flksvKTIPESY----LSAIF--KQVLQGLIYLHHdKHIIHRDLKPSNLL-INHRG-EVKITDFGVSTVMTNTAGLANTF 227
Cdd:cd14103   80 -----RVVDDDFelteRDCILfmRQICEGVQYMHK-QGILHLDLKPENILcVSRTGnQIKIIDFGLARKYDPDKKLKVLF 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 228 vGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSV--------FELMEAIvdqpppalpsenf 299
Cdd:cd14103  154 -GTPEFVAPEVVNYEPISYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVtrakwdfdDEAFDDI------------- 219
                        250       260       270
                 ....*....|....*....|....*....|.
gi 567218350 300 SPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14103  220 SDEAKDFISKLLVKDPRKRMSAAQCLQHPWL 250
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
74-267 4.24e-32

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: 121.25  E-value: 4.24e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVI--QLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGG 151
Cdd:cd14162    6 KTLGHGSYAVVKKAYSTKHKCKVAIKIVskKKAPEDYLQKFLPREIEVIKGLKHPNLICFYEAIETTSRVYIIMELAENG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 152 SLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLINHRGEVKITDFGVS-TVMTNTAG---LANTF 227
Cdd:cd14162   86 DLLDYIRKNGALPEPQARRWFRQLVAGVEYCHS-KGVVHRDLKCENLLLDKNNNLKITDFGFArGVMKTKDGkpkLSETY 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 567218350 228 VGTYNYMSPERIVGNKY-GNKSDIWSLGLVVLECATGKFPY 267
Cdd:cd14162  165 CGSYAYASPEILRGIPYdPFLSDIWSMGVVLYTMVYGRLPF 205
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
76-327 4.72e-32

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: 120.89  E-value: 4.72e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKviQLNIDEAIRKSIAQELKINQS-SQCPYLVNSYQ-SFYDNGAISLILEYMDGGSL 153
Cdd:cd13987    1 LGEGTYGKVLLAVHKGSGTKMALK--FVPKPSTKLKDFLREYNISLElSVHPHIIKTYDvAFETEDYYVFAQEYAPYGDL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 154 ADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLI--NHRGEVKITDFGvstvMTNTAGLANTFV-GT 230
Cdd:cd13987   79 FSIIPPQVGLPEERVKRCAAQLASALDFMH-SKNLVHRDIKPENVLLfdKDCRRVKLCDFG----LTRRVGSTVKRVsGT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 231 YNYMSPE--------RIVGNKygnKSDIWSLGLVVLECATGKFPYlppdQEETWS-SVFELMEAIVDQPPPALPS--ENF 299
Cdd:cd13987  154 IPYTAPEvceakkneGFVVDP---SIDVWAFGVLLFCCLTGNFPW----EKADSDdQFYEEFVRWQKRKNTAVPSqwRRF 226
                        250       260
                 ....*....|....*....|....*...
gi 567218350 300 SPELSSFISTCLQKDPNSRSSAKELMEH 327
Cdd:cd13987  227 TPKALRMFKKLLAPEPERRCSIKEVFKY 254
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
76-320 4.79e-32

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: 121.02  E-value: 4.79e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQ-LNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLA 154
Cdd:cd13978    1 LGSGGFGTVSKARHVSWFGMVAIKCLHsSPNCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSLK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 155 DFLKSVKT-IPESYLSAIFKQVLQGLIYLHH-DKHIIHRDLKPSNLLINHRGEVKITDFGVSTV--MTNTAGLANT---F 227
Cdd:cd13978   81 SLLEREIQdVPWSLRFRIIHEIALGMNFLHNmDPPLLHHDLKPENILLDNHFHVKISDFGLSKLgmKSISANRRRGtenL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 228 VGTYNYMSPERI--VGNKYGNKSDIWSLGLVVLECATGKFPYlpPDQEETwssvFELMEAIVDQPPPALPSEN------F 299
Cdd:cd13978  161 GGTPIYMAPEAFddFNKKPTSKSDVYSFAIVIWAVLTRKEPF--ENAINP----LLIMQIVSKGDRPSLDDIGrlkqieN 234
                        250       260
                 ....*....|....*....|.
gi 567218350 300 SPELSSFISTCLQKDPNSRSS 320
Cdd:cd13978  235 VQELISLMIRCWDGNPDARPT 255
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
74-330 5.08e-32

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: 120.80  E-value: 5.08e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVI-QLNIDEA-IRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGG 151
Cdd:cd14189    7 RLLGKGGFARCYEMTDLATNKTYAVKVIpHSRVAKPhQREKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLELCSRK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 152 SLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVGTY 231
Cdd:cd14189   87 SLAHIWKARHTLLEPEVRYYLKQIISGLKYLHL-KGILHRDLKLGNFFINENMELKVGDFGLAARLEPPEQRKKTICGTP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 232 NYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFElmeaiVDQPPPAlpseNFSPELSSFISTCL 311
Cdd:cd14189  166 NYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQ-----VKYTLPA----SLSLPARHLLAGIL 236
                        250
                 ....*....|....*....
gi 567218350 312 QKDPNSRSSAKELMEHPFL 330
Cdd:cd14189  237 KRNPGDRLTLDQILEHEFF 255
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
62-330 6.89e-32

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: 121.49  E-value: 6.89e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  62 DDELSLSDldmvkFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEA----IRKSIAQELKINQSSQCPYLVNSYQSFYD 137
Cdd:cd14094    2 EDVYELCE-----VIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFTSspglSTEDLKREASICHMLKHPHIVELLETYSS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 138 NGAISLILEYMDGGSL---------ADFLKSvktipESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLI---NHRGE 205
Cdd:cd14094   77 DGMLYMVFEFMDGADLcfeivkradAGFVYS-----EAVASHYMRQILEALRYCH-DNNIIHRDVKPHCVLLaskENSAP 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 206 VKITDFGVSTVMTNTAGLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLppdqeETWSSVFE-LME 284
Cdd:cd14094  151 VKLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFY-----GTKERLFEgIIK 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 567218350 285 AIVDQPPPALPseNFSPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14094  226 GKYKMNPRQWS--HISESAKDLVRRMLMLDPAERITVYEALNHPWI 269
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
64-362 7.67e-32

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: 121.64  E-value: 7.67e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  64 ELSLSDldmvKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDeairksIAQELKINQSSQC-PYLVNSYQSFYDNGAIS 142
Cdd:cd14092    6 ELDLRE----EALGDGSFSVCRKCVHKKTGQEFAVKIVSRRLD------TSREVQLLRLCQGhPNIVKLHEVFQDELHTY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 143 LILEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLL---INHRGEVKITDFGVSTVMTN 219
Cdd:cd14092   76 LVMELLRGGELLERIRKKKRFTESEASRIMRQLVSAVSFMH-SKGVVHRDLKPENLLftdEDDDAEIKIVDFGFARLKPE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 220 TAGLaNTFVGTYNYMSPERI----VGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEEtwsSVFELMEAI----VDQPP 291
Cdd:cd14092  155 NQPL-KTPCFTLPYAAPEVLkqalSTQGYDESCDLWSLGVILYTMLSGQVPFQSPSRNE---SAAEIMKRIksgdFSFDG 230
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 567218350 292 PALpsENFSPELSSFISTCLQKDPNSRSSAKELMEHPFLNKynnseinlASYFTDAgsPLATLGNLSGTFS 362
Cdd:cd14092  231 EEW--KNVSSEAKSLIQGLLTVDPSKRLTMSELRNHPWLQG--------SSSPSST--PLMTPGVLSSSAA 289
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
68-287 8.27e-32

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: 121.39  E-value: 8.27e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  68 SDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKViqLNIDEAIR----KSIAQELKINQSSQCPYLVNSYQSFYDNGAISL 143
Cdd:cd05612    1 DDFERIKTIGTGTFGRVHLVRDRISEHYYALKV--MAIPEVIRlkqeQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 144 ILEYMDGGSLADFLKSVKTIPESylSAIF--KQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTA 221
Cdd:cd05612   79 LMEYVPGGELFSYLRNSGRFSNS--TGLFyaSEIVCALEYLH-SKEIVYRDLKPENILLDKEGHIKLTDFGFAKKLRDRT 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 567218350 222 GlanTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKfpylPPDQEETwssVFELMEAIV 287
Cdd:cd05612  156 W---TLCGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGY----PPFFDDN---PFGIYEKIL 211
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
64-318 9.03e-32

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: 121.69  E-value: 9.03e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  64 ELSLSDldmvKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQeLKINQSSqcPYLVNSYQSFYDNGAISL 143
Cdd:cd14179    7 ELDLKD----KPLGEGSFSICRKCLHKKTNQEYAVKIVSKRMEANTQREIAA-LKLCEGH--PNIVKLHEVYHDQLHTFL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 144 ILEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLI---NHRGEVKITDFGVSTVMTNT 220
Cdd:cd14179   80 VMELLKGGELLERIKKKQHFSETEASHIMRKLVSAVSHMH-DVGVVHRDLKPENLLFtdeSDNSEIKIIDFGFARLKPPD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 221 AGLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFELMEAIvDQPPPALPSE--- 297
Cdd:cd14179  159 NQPLKTPCFTLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQCHDKSLTCTSAEEIMKKI-KQGDFSFEGEawk 237
                        250       260
                 ....*....|....*....|.
gi 567218350 298 NFSPELSSFISTCLQKDPNSR 318
Cdd:cd14179  238 NVSQEAKDLIQGLLTVDPNKR 258
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
61-331 9.11e-32

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: 120.50  E-value: 9.11e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  61 ADDELSLSDLdmvkfLGKGSSGVVQLVQH-KWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNG 139
Cdd:cd14201    4 GDFEYSRKDL-----VGHGAFAVVFKGRHrKKTDWEVAIKSINKKNLSKSQILLGKEIKILKELQHENIVALYDVQEMPN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 140 AISLILEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGE---------VKITD 210
Cdd:cd14201   79 SVFLVMEYCNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILH-SKGIIHRDLKPQNILLSYASRkkssvsgirIKIAD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 211 FGVSTVMTNTAgLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYL---PPDQEETWSSVFELMeaiv 287
Cdd:cd14201  158 FGFARYLQSNM-MAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQansPQDLRMFYEKNKNLQ---- 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 567218350 288 dqppPALPSENfSPELSSFISTCLQKDPNSRSSAKELMEHPFLN 331
Cdd:cd14201  233 ----PSIPRET-SPYLADLLLGLLQRNQKDRMDFEAFFSHPFLE 271
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
69-330 9.42e-32

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


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 122.03  E-value: 9.42e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  69 DLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNI---DEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLIL 145
Cdd:cd05616    1 DFNFLMVLGKGSFGKVMLAERKGTDELYAVKILKKDVviqDDDVECTMVEKRVLALSGKPPFLTQLHSCFQTMDRLYFVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 146 EYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLAN 225
Cdd:cd05616   81 EYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQ-SKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 226 TFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVfelMEAIVDQPppalpsENFSPELSS 305
Cdd:cd05616  160 TFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSI---MEHNVAYP------KSMSKEAVA 230
                        250       260       270
                 ....*....|....*....|....*....|
gi 567218350 306 FISTCLQKDPNSR-----SSAKELMEHPFL 330
Cdd:cd05616  231 ICKGLMTKHPGKRlgcgpEGERDIKEHAFF 260
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
71-328 9.44e-32

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


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 120.17  E-value: 9.44e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  71 DMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDG 150
Cdd:cd14083    6 EFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKALKGKEDSLENEIAVLRKIKHPNIVQLLDIYESKSHLYLVMELVTG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 151 GSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGE---VKITDFGVSTVMTNtaGLANTF 227
Cdd:cd14083   86 GELFDRIVEKGSYTEKDASHLIRQVLEAVDYLH-SLGIVHRDLKPENLLYYSPDEdskIMISDFGLSKMEDS--GVMSTA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 228 VGTYNYMSPERIVGNKYGNKSDIWSLGLV--VLECAtgkfpYlPPDQEETWSSVFE-LMEAIVDQPPPALpsENFSPELS 304
Cdd:cd14083  163 CGTPGYVAPEVLAQKPYGKAVDCWSIGVIsyILLCG-----Y-PPFYDENDSKLFAqILKAEYEFDSPYW--DDISDSAK 234
                        250       260
                 ....*....|....*....|....
gi 567218350 305 SFISTCLQKDPNSRSSAKELMEHP 328
Cdd:cd14083  235 DFIRHLMEKDPNKRYTCEQALEHP 258
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
65-329 9.46e-32

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: 122.49  E-value: 9.46e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  65 LSLSDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKViqLNIDEAIRKSIA----QELKINQSSQCPYLVNSYQSFYDNGA 140
Cdd:cd05596   23 MNAEDFDVIKVIGRGAFGEVQLVRHKSTKKVYAMKL--LSKFEMIKRSDSaffwEERDIMAHANSEWIVQLHYAFQDDKY 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 141 ISLILEYMDGGSLADfLKSVKTIPESYlsAIF--KQVLQGLIYLhHDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMt 218
Cdd:cd05596  101 LYMVMDYMPGGDLVN-LMSNYDVPEKW--ARFytAEVVLALDAI-HSMGFVHRDVKPDNMLLDASGHLKLADFGTCMKM- 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 219 NTAGL--ANTFVGTYNYMSPERI----VGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSvfelmeaIVDQ--- 289
Cdd:cd05596  176 DKDGLvrSDTAVGTPDYISPEVLksqgGDGVYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYGK-------IMNHkns 248
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 567218350 290 ---PPPALPSENFSPELSSFISTCLQKdpNSRSSAKELMEHPF 329
Cdd:cd05596  249 lqfPDDVEISKDAKSLICAFLTDREVR--LGRNGIEEIKAHPF 289
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
37-330 9.47e-32

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: 123.19  E-value: 9.47e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  37 LRVNKDGVRIVSQSEpEVLSPIKPAddELSLSDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKViqLNIDEAIRKSIA-- 114
Cdd:cd05621   24 LRKNKNIDNFLNRYE-KIVNKIREL--QMKAEDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKL--LSKFEMIKRSDSaf 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 115 --QELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLADfLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRD 192
Cdd:cd05621   99 fwEERDIMAFANSPWVVQLFCAFQDDKYLYMVMEYMPGGDLVN-LMSNYDVPEKWAKFYTAEVVLALDAIH-SMGLIHRD 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 193 LKPSNLLINHRGEVKITDFGVSTVMTNTAGL-ANTFVGTYNYMSPERIVGNK----YGNKSDIWSLGLVVLECATGKFPY 267
Cdd:cd05621  177 VKPDNMLLDKYGHLKLADFGTCMKMDETGMVhCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLFEMLVGDTPF 256
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 567218350 268 LPPDQEETWSSVFELMEAIvDQPPPALPSENFSPELSSFISTclQKDPNSRSSAKELMEHPFL 330
Cdd:cd05621  257 YADSLVGTYSKIMDHKNSL-NFPDDVEISKHAKNLICAFLTD--REVRLGRNGVEEIKQHPFF 316
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
51-332 1.03e-31

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: 121.28  E-value: 1.03e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  51 EPEVLSPIKPADDELSLSDLdmvKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRK--SIAQELKINQSSQCPYL 128
Cdd:cd06634    1 DPEVAELFFKDDPEKLFSDL---REIGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNEKwqDIIKEVKFLQKLRHPNT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 129 VNSYQSFYDNGAISLILEYMDGgSLADFLK-SVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVK 207
Cdd:cd06634   78 IEYRGCYLREHTAWLVMEYCLG-SASDLLEvHKKPLQEVEIAAITHGALQGLAYLH-SHNMIHRDVKAGNILLTEPGLVK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 208 ITDFGVSTVMTNtaglANTFVGTYNYMSPERIVG---NKYGNKSDIWSLGLVVLECATGKFPYLppdQEETWSSVFElme 284
Cdd:cd06634  156 LGDFGSASIMAP----ANSFVGTPYWMAPEVILAmdeGQYDGKVDVWSLGITCIELAERKPPLF---NMNAMSALYH--- 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 567218350 285 aIVDQPPPALPSENFSPELSSFISTCLQKDPNSRSSAKELMEHPFLNK 332
Cdd:cd06634  226 -IAQNESPALQSGHWSEYFRNFVDSCLQKIPQDRPTSDVLLKHRFLLR 272
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
72-330 1.12e-31

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: 121.11  E-value: 1.12e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  72 MVKFLGKGSSG-VVQLVQHKwTGQFFALKVIQlNiDEAIRKSIAQELKI------NQSSQCPYLVNSYQSFYDNGAISLI 144
Cdd:cd14210   17 VLSVLGKGSFGqVVKCLDHK-TGQLVAIKIIR-N-KKRFHQQALVEVKIlkhlndNDPDDKHNIVRYKDSFIFRGHLCIV 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 145 LEyMDGGSLADFLKS--VKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLI--NHRGEVKITDFGVSTvmtnt 220
Cdd:cd14210   94 FE-LLSINLYELLKSnnFQGLSLSLIRKFAKQILQALQFLH-KLNIIHCDLKPENILLkqPSKSSIKVIDFGSSC----- 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 221 aglantFVG----TY----NYMSPERIVGNKYGNKSDIWSLGLVVLECATGKfPYLPPDQEEtwssvfELMEAIV---DQ 289
Cdd:cd14210  167 ------FEGekvyTYiqsrFYRAPEVILGLPYDTAIDMWSLGCILAELYTGY-PLFPGENEE------EQLACIMevlGV 233
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 567218350 290 PPPAL-----------------------------PSE--------NFSPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14210  234 PPKSLidkasrrkkffdsngkprpttnskgkkrrPGSkslaqvlkCDDPSFLDFLKKCLRWDPSERMTPEEALQHPWI 311
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
72-267 1.45e-31

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: 119.55  E-value: 1.45e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  72 MVKFLGKGSSGVVQLVQHKWTGQFFALKVI---QLNiDEAIRKsIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYM 148
Cdd:cd14072    4 LLKTIGKGNFAKVKLARHVLTGREVAIKIIdktQLN-PSSLQK-LFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEYA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 149 DGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLaNTFV 228
Cdd:cd14072   82 SGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQ-KRIVHRDLKAENLLLDADMNIKIADFGFSNEFTPGNKL-DTFC 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 567218350 229 GTYNYMSPERIVGNKY-GNKSDIWSLGLVVLECATGKFPY 267
Cdd:cd14072  160 GSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPF 199
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
69-334 1.61e-31

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: 120.49  E-value: 1.61e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  69 DLDMVKFLGKGSSGVVQLVQ----HKwTGQFFALKVIQlnideaiRKSIAQELKINQSS-----------QCPYLVNSYQ 133
Cdd:cd05613    1 NFELLKVLGTGAYGKVFLVRkvsgHD-AGKLYAMKVLK-------KATIVQKAKTAEHTrterqvlehirQSPFLVTLHY 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 134 SFYDNGAISLILEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLINHRGEVKITDFGV 213
Cdd:cd05613   73 AFQTDTKLHLILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHK-LGIIYRDIKLENILLDSSGHVVLTDFGL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 214 ST-VMTNTAGLANTFVGTYNYMSPERIVGNKYGNKS--DIWSLGLVVLECATGKFPYlPPDQEEtwSSVFELMEAIVDQP 290
Cdd:cd05613  152 SKeFLLDENERAYSFCGTIEYMAPEIVRGGDSGHDKavDWWSLGVLMYELLTGASPF-TVDGEK--NSQAEISRRILKSE 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 567218350 291 PPaLPSEnFSPELSSFISTCLQKDPNSR-----SSAKELMEHPFLNKYN 334
Cdd:cd05613  229 PP-YPQE-MSALAKDIIQRLLMKDPKKRlgcgpNGADEIKKHPFFQKIN 275
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
68-331 1.76e-31

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: 121.18  E-value: 1.76e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  68 SDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKViqLNIDEAIRKS----IAQELKINQSSQCPYLVNSYQSFYDNGAISL 143
Cdd:cd05599    1 EDFEPLKVIGRGAFGEVRLVRKKDTGHVYAMKK--LRKSEMLEKEqvahVRAERDILAEADNPWVVKLYYSFQDEENLYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 144 ILEYMDGGSLADFLKSVKTIPES----YlsaIFKQVLQglIYLHHDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMtN 219
Cdd:cd05599   79 IMEFLPGGDMMTLLMKKDTLTEEetrfY---IAETVLA--IESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGLCTGL-K 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 220 TAGLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEET------WSSVFELmeaivdqpPPA 293
Cdd:cd05599  153 KSHLAYSTVGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETcrkimnWRETLVF--------PPE 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 567218350 294 LPsenFSPELSSFIST--CLQKDPNSRSSAKELMEHPFLN 331
Cdd:cd05599  225 VP---ISPEAKDLIERllCDAEHRLGANGVEEIKSHPFFK 261
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
76-330 1.85e-31

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: 120.18  E-value: 1.85e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNIDE-----AIRK-SIAQELKINQssqcpyLVNSYQSFYDNGAISLILEYMD 149
Cdd:cd07844    8 LGEGSYATVYKGRSKLTGQLVALKEIRLEHEEgapftAIREaSLLKDLKHAN------IVTLHDIIHTKKTLTLVFEYLD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 150 ggsladflKSVKTIPESYLSAI--------FKQVLQGLIYLHHdKHIIHRDLKPSNLLINHRGEVKITDFGVS---TVMT 218
Cdd:cd07844   82 --------TDLKQYMDDCGGGLsmhnvrlfLFQLLRGLAYCHQ-RRVLHRDLKPQNLLISERGELKLADFGLArakSVPS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 219 NTagLANTFVgTYNYMSPERIVGN-KYGNKSDIWSLGLVVLECATGK--FPYL--PPDQ------------EETWSSVFE 281
Cdd:cd07844  153 KT--YSNEVV-TLWYRPPDVLLGStEYSTSLDMWGVGCIFYEMATGRplFPGStdVEDQlhkifrvlgtptEETWPGVSS 229
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 567218350 282 LME----AIVDQPPPAL----PSENFSPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd07844  230 NPEfkpySFPFYPPRPLinhaPRLDRIPHGEELALKFLQYEPKKRISAAEAMKHPYF 286
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
76-329 1.89e-31

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: 119.89  E-value: 1.89e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNIDE-----AIRK-SIAQELKinqssqCPYLVNSYQSFYDNGAISLILEYMD 149
Cdd:cd07836    8 LGEGTYATVYKGRNRTTGEIVALKEIHLDAEEgtpstAIREiSLMKELK------HENIVRLHDVIHTENKLMLVFEYMD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 150 GgslaDFLKSVKT------IPESYLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKITDFGVSTVMtntaGL 223
Cdd:cd07836   82 K----DLKKYMDThgvrgaLDPNTVKSFTYQLLKGIAFCHENR-VLHRDLKPQNLLINKRGELKLADFGLARAF----GI 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 224 -ANTF---VGTYNYMSPERIVGNK-YGNKSDIWSLGLVVLECATGKfPYLP----PDQ------------EETWSSVFEL 282
Cdd:cd07836  153 pVNTFsneVVTLWYRAPDVLLGSRtYSTSIDIWSVGCIMAEMITGR-PLFPgtnnEDQllkifrimgtptESTWPGISQL 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 567218350 283 MEAIVDQPP-PALPSENFSPELS----SFISTCLQKDPNSRSSAKELMEHPF 329
Cdd:cd07836  232 PEYKPTFPRyPPQDLQQLFPHADplgiDLLHRLLQLNPELRISAHDALQHPW 283
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
76-334 1.97e-31

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


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 119.94  E-value: 1.97e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQlniDEAIRKSIAQELKINQSS-----QCPYLVNSYQSFYDNGAISLILEYMDG 150
Cdd:cd05577    1 LGRGGFGEVCACQVKATGKMYACKKLD---KKRIKKKKGETMALNEKIilekvSSPFIVSLAYAFETKDKLCLVLTLMNG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 151 GSLADFLKSVKTIPESYLSAIF--KQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLaNTFV 228
Cdd:cd05577   78 GDLKYHIYNVGTRGFSEARAIFyaAEIICGLEHLH-NRFIVYRDLKPENILLDDHGHVRISDLGLAVEFKGGKKI-KGRV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 229 GTYNYMSPERIVGN-KYGNKSDIWSLGLVVLECATGKFPYlppDQEETWSSVFELmEAIVDQPPPALPsENFSPELSSFI 307
Cdd:cd05577  156 GTHGYMAPEVLQKEvAYDFSVDWFALGCMLYEMIAGRSPF---RQRKEKVDKEEL-KRRTLEMAVEYP-DSFSPEARSLC 230
                        250       260       270
                 ....*....|....*....|....*....|..
gi 567218350 308 STCLQKDPNSR-----SSAKELMEHPFLNKYN 334
Cdd:cd05577  231 EGLLQKDPERRlgcrgGSADEVKEHPFFRSLN 262
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
63-338 2.10e-31

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: 121.26  E-value: 2.10e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  63 DELSLSDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNI---DEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNG 139
Cdd:cd05615    5 DRVRLTDFNFLMVLGKGSFGKVMLAERKGSDELYAIKILKKDVviqDDDVECTMVEKRVLALQDKPPFLTQLHSCFQTVD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 140 AISLILEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTN 219
Cdd:cd05615   85 RLYFVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHK-KGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 220 TAGLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVfelMEAIVDQPppalpsENF 299
Cdd:cd05615  164 EGVTTRTFCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSI---MEHNVSYP------KSL 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 567218350 300 SPELSSFISTCLQKDPNSR-----SSAKELMEHPFL-----NKYNNSEI 338
Cdd:cd05615  235 SKEAVSICKGLMTKHPAKRlgcgpEGERDIREHAFFrridwDKLENREI 283
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
76-330 3.64e-31

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: 118.88  E-value: 3.64e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVI-QLNIDEAIRKSIAQELKINQSSQ-CPYLVNSYQSFYDNGAISLILEYMDGGSL 153
Cdd:cd14197   17 LGRGKFAVVRKCVEKDSGKEFAAKFMrKRRKGQDCRMEIIHEIAVLELAQaNPWVINLHEVYETASEMILVLEYAAGGEI 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 154 adFLKSVKTIPESY----LSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLINHR---GEVKITDFGVSTVMTNTAGLaNT 226
Cdd:cd14197   97 --FNQCVADREEAFkekdVKRLMKQILEGVSFLHN-NNVVHLDLKPQNILLTSEsplGDIKIVDFGLSRILKNSEEL-RE 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 227 FVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFELMEAIVDQpppalPSENFSPELSSF 306
Cdd:cd14197  173 IMGTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQMNVSYSEE-----EFEHLSESAIDF 247
                        250       260
                 ....*....|....*....|....
gi 567218350 307 ISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14197  248 IKTLLIKKPENRATAEDCLKHPWL 271
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
69-329 3.84e-31

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: 121.49  E-value: 3.84e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  69 DLDMVKFLGKGSSGVVQLVQHKWTGQFFALKviQLNIDEAIRKS----IAQELKINQSSQCPYLVNSYQSFYDNGAISLI 144
Cdd:cd05629    2 DFHTVKVIGKGAFGEVRLVQKKDTGKIYAMK--TLLKSEMFKKDqlahVKAERDVLAESDSPWVVSLYYSFQDAQYLYLI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 145 LEYMDGGSLADFLKSVKTIPES----YLSAIfkqVLQglIYLHHDKHIIHRDLKPSNLLINHRGEVKITDFGVST----- 215
Cdd:cd05629   80 MEFLPGGDLMTMLIKYDTFSEDvtrfYMAEC---VLA--IEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGLSTgfhkq 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 216 ------------------------VMTNTAGL------------------ANTFVGTYNYMSPERIVGNKYGNKSDIWSL 253
Cdd:cd05629  155 hdsayyqkllqgksnknridnrnsVAVDSINLtmsskdqiatwkknrrlmAYSTVGTPDYIAPEIFLQQGYGQECDWWSL 234
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 567218350 254 GLVVLECATGKFPYLPPDQEETWSSVFELMEAIvdQPPPALpseNFSPELSSFISTCLQKDPN--SRSSAKELMEHPF 329
Cdd:cd05629  235 GAIMFECLIGWPPFCSENSHETYRKIINWRETL--YFPDDI---HLSVEAEDLIRRLITNAENrlGRGGAHEIKSHPF 307
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
74-329 3.98e-31

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: 120.19  E-value: 3.98e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVIQLNI---DEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDG 150
Cdd:cd05587    2 MVLGKGSFGKVMLAERKGTDELYAIKILKKDViiqDDDVECTMVEKRVLALSGKPPFLTQLHSCFQTMDRLYFVMEYVNG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 151 GSLADFLKSVKTIPESYlsAIF--KQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFV 228
Cdd:cd05587   82 GDLMYHIQQVGKFKEPV--AVFyaAEIAVGLFFLH-SKGIIYRDLKLDNVMLDAEGHIKIADFGMCKEGIFGGKTTRTFC 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 229 GTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVfelMEAIVDQPppalpsENFSPELSSFIS 308
Cdd:cd05587  159 GTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSI---MEHNVSYP------KSLSKEAVSICK 229
                        250       260
                 ....*....|....*....|....*.
gi 567218350 309 TCLQKDPNSR-----SSAKELMEHPF 329
Cdd:cd05587  230 GLLTKHPAKRlgcgpTGERDIKEHPF 255
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
71-330 5.75e-31

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: 118.21  E-value: 5.75e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  71 DMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDG 150
Cdd:cd14167    6 DFREVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGKETSIENEIAVLHKIKHPNIVALDDIYESGGHLYLIMQLVSG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 151 GSLADFLKSVKTIPESYLSAIFKQVLQGLIYLhHDKHIIHRDLKPSNLL---INHRGEVKITDFGVSTvMTNTAGLANTF 227
Cdd:cd14167   86 GELFDRIVEKGFYTERDASKLIFQILDAVKYL-HDMGIVHRDLKPENLLyysLDEDSKIMISDFGLSK-IEGSGSVMSTA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 228 VGTYNYMSPERIVGNKYGNKSDIWSLGLV--VLECAtgkfpyLPPDQEETWSSVFE-LMEAIVDQPPPALpsENFSPELS 304
Cdd:cd14167  164 CGTPGYVAPEVLAQKPYSKAVDCWSIGVIayILLCG------YPPFYDENDAKLFEqILKAEYEFDSPYW--DDISDSAK 235
                        250       260
                 ....*....|....*....|....*.
gi 567218350 305 SFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14167  236 DFIQHLMEKDPEKRFTCEQALQHPWI 261
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
76-330 8.46e-31

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: 119.60  E-value: 8.46e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAiRKSIAQ---ELKINQ---SSQCPYLVNSYQSFYDNGAISLILEYMD 149
Cdd:cd05586    1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVA-KKEVAHtigERNILVrtaLDESPFIVGLKFSFQTPTDLYLVTDYMS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 150 GGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVG 229
Cdd:cd05586   80 GGELFWHLQKEGRFSEDRAKFYIAELVLALEHLH-KNDIVYRDLKPENILLDANGHIALCDFGLSKADLTDNKTTNTFCG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 230 TYNYMSPERIVGNK-YGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSV-FELMEaivdqpppaLPSENFSPELSSFI 307
Cdd:cd05586  159 TTEYLAPEVLLDEKgYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIaFGKVR---------FPKDVLSDEGRSFV 229
                        250       260
                 ....*....|....*....|....*..
gi 567218350 308 STCLQKDPNSR----SSAKELMEHPFL 330
Cdd:cd05586  230 KGLLNRNPKHRlgahDDAVELKEHPFF 256
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
76-330 1.16e-30

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: 117.38  E-value: 1.16e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEaiRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLAD 155
Cdd:cd14113   15 LGRGRFSVVKKCDQRGTKRAVATKFVNKKLMK--RDQVTHELGVLQSLQHPQLVGLLDTFETPTSYILVLEMADQGRLLD 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 156 FLKSVKTIPESYLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLINH---RGEVKITDFGvSTVMTNTAGLANTFVGTYN 232
Cdd:cd14113   93 YVVRWGNLTEEKIRFYLREILEALQYLHNCR-IAHLDLKPENILVDQslsKPTIKLADFG-DAVQLNTTYYIHQLLGSPE 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 233 YMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFELmeaivdqpPPALPSENF---SPELSSFIST 309
Cdd:cd14113  171 FAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNICRL--------DFSFPDDYFkgvSQKAKDFVCF 242
                        250       260
                 ....*....|....*....|.
gi 567218350 310 CLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14113  243 LLQMDPAKRPSAALCLQEQWL 263
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
69-330 1.72e-30

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: 116.88  E-value: 1.72e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  69 DLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQlniDEAIRKS-----IAQELKINQSSQCPYLVNSYQSFYDNGAISL 143
Cdd:cd14186    2 DFKVLNLLGKGSFACVYRARSLHTGLEVAIKMID---KKAMQKAgmvqrVRNEVEIHCQLKHPSILELYNYFEDSNYVYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 144 ILEYMDGGSLADFLKS-VKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAG 222
Cdd:cd14186   79 VLEMCHNGEMSRYLKNrKKPFTEDEARHFMHQIVTGMLYLH-SHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKMPHE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 223 LANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVfelmeAIVDQPPPALpsenFSPE 302
Cdd:cd14186  158 KHFTMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKV-----VLADYEMPAF----LSRE 228
                        250       260
                 ....*....|....*....|....*...
gi 567218350 303 LSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14186  229 AQDLIHQLLRKNPADRLSLSSVLDHPFM 256
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
72-329 2.21e-30

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: 118.17  E-value: 2.21e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  72 MVKFLGKGSSGVVQLVQHKWTGQFFALKVIQ----LNIDEAirKSIAQELKINQ---SSQCPYLVNSYQSFYDNGAISLI 144
Cdd:cd05589    3 CIAVLGRGHFGKVLLAEYKPTGELFAIKALKkgdiIARDEV--ESLMCEKRIFEtvnSARHPFLVNLFACFQTPEHVCFV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 145 LEYMDGGSL-----ADFLKSVKTIpesYLSAIfkqVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTN 219
Cdd:cd05589   81 MEYAAGGDLmmhihEDVFSEPRAV---FYAAC---VVLGLQFLH-EHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 220 TAGLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYlPPDQEEtwssvfELMEAIVDQP---PPALps 296
Cdd:cd05589  154 FGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPF-PGDDEE------EVFDSIVNDEvryPRFL-- 224
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 567218350 297 enfSPELSSFISTCLQKDPNSR--SS---AKELMEHPF 329
Cdd:cd05589  225 ---STEAISIMRRLLRKNPERRlgASerdAEDVKKQPF 259
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
68-339 4.22e-30

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: 117.81  E-value: 4.22e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  68 SDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLN--IDEAIRKSIAQELKIN-QSSQCPYLVNSYQSFYDNGAISLI 144
Cdd:cd05602    7 SDFHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQKKaiLKKKEEKHIMSERNVLlKNVKHPFLVGLHFSFQTTDKLYFV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 145 LEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLA 224
Cdd:cd05602   87 LDYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLH-SLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIEPNGTT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 225 NTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGkfpyLPPDQEETWSsvfELMEAIVDQPPPALPseNFSPELS 304
Cdd:cd05602  166 STFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYG----LPPFYSRNTA---EMYDNILNKPLQLKP--NITNSAR 236
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 567218350 305 SFISTCLQKDPNSRSSAK----ELMEHPFLNKYNNSEIN 339
Cdd:cd05602  237 HLLEGLLQKDRTKRLGAKddftEIKNHIFFSPINWDDLI 275
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
72-334 5.35e-30

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: 116.30  E-value: 5.35e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  72 MVKFLGKGSSGVVQLVQHKWTGQFFALKVIQlniDEAIRKSIAQELKIN-----QSSQCPYLVNSYQSFYDNGAISLILE 146
Cdd:cd05605    4 QYRVLGKGGFGEVCACQVRATGKMYACKKLE---KKRIKKRKGEAMALNekqilEKVNSRFVVSLAYAYETKDALCLVLT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 147 YMDGGSLADFLKSV--KTIPESylSAIF--KQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVStVMTNTAG 222
Cdd:cd05605   81 IMNGGDLKFHIYNMgnPGFEEE--RAVFyaAEITCGLEHLH-SERIVYRDLKPENILLDDHGHVRISDLGLA-VEIPEGE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 223 LANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLP----PDQEETWSSVFELMEAIvdqpppalpSEN 298
Cdd:cd05605  157 TIRGRVGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRArkekVKREEVDRRVKEDQEEY---------SEK 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 567218350 299 FSPELSSFISTCLQKDPNSR-----SSAKELMEHPFLNKYN 334
Cdd:cd05605  228 FSEEAKSICSQLLQKDPKTRlgcrgEGAEDVKSHPFFKSIN 268
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
69-340 5.52e-30

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: 117.33  E-value: 5.52e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  69 DLDMVKFLGKGSSGVVQLVQ----HKwTGQFFALKVIQlnideaiRKSIAQELKINQSS-----------QCPYLVNSYQ 133
Cdd:cd05614    1 NFELLKVLGTGAYGKVFLVRkvsgHD-ANKLYAMKVLR-------KAALVQKAKTVEHTrternvlehvrQSPFLVTLHY 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 134 SFYDNGAISLILEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLINHRGEVKITDFGV 213
Cdd:cd05614   73 AFQTDAKLHLILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHK-LGIVYRDIKLENILLDSEGHVVLTDFGL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 214 ST-VMTNTAGLANTFVGTYNYMSPERIVGNK-YGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSsvfELMEAIVDQPP 291
Cdd:cd05614  152 SKeFLTEEKERTYSFCGTIEYMAPEIIRGKSgHGKAVDWWSLGILMFELLTGASPFTLEGEKNTQS---EVSRRILKCDP 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 567218350 292 PaLPSEnFSPELSSFISTCLQKDPNSR-----SSAKELMEHPFLNKYNNSEINL 340
Cdd:cd05614  229 P-FPSF-IGPVARDLLQKLLCKDPKKRlgagpQGAQEIKEHPFFKGLDWEALAL 280
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
73-332 6.01e-30

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: 115.89  E-value: 6.01e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  73 VKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNiDEAIRKSIAQELKINQS-SQCPYLVNSYQS-FYDNGAISLILEYMD- 149
Cdd:cd13985    5 TKQLGEGGFSYVYLAHDVNTGRRYALKRMYFN-DEEQLRVAIKEIEIMKRlCGHPNIVQYYDSaILSSEGRKEVLLLMEy 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 150 -GGSLADFL-KSVKT-IPESYLSAIFKQVLQGLIYLHHDK-HIIHRDLKPSNLLINHRGEVKITDFGVST------VMTN 219
Cdd:cd13985   84 cPGSLVDILeKSPPSpLSEEEVLRIFYQICQAVGHLHSQSpPIIHRDIKIENILFSNTGRFKLCDFGSATtehyplERAE 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 220 TAGLANTFVGTYN---YMSPERIvgNKYGN-----KSDIWSLGLVVLECATGKFPYLPpdqeetwSSVFelmeAIVDQPP 291
Cdd:cd13985  164 EVNIIEEEIQKNTtpmYRAPEMI--DLYSKkpigeKADIWALGCLLYKLCFFKLPFDE-------SSKL----AIVAGKY 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 567218350 292 PALPSENFSPELSSFISTCLQKDPNSRSSAKELMEhpFLNK 332
Cdd:cd13985  231 SIPEQPRYSPELHDLIRHMLTPDPAERPDIFQVIN--IITK 269
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
71-330 7.51e-30

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: 115.32  E-value: 7.51e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  71 DMVKFLGKGSSGVVQLVQHKWTGQFFALKVIqlNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDG 150
Cdd:cd14087    4 DIKALIGRGSFSRVVRVEHRVTRQPYAIKMI--ETKCRGREVCESELNVLRRVRHTNIIQLIEVFETKERVYMVMELATG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 151 GSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRG---EVKITDFGVSTVMTNTAG-LANT 226
Cdd:cd14087   82 GELFDRIIAKGSFTERDATRVLQMVLDGVKYLH-GLGITHRDLKPENLLYYHPGpdsKIMITDFGLASTRKKGPNcLMKT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 227 FVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFELMEAIVDQPPPALpsenfSPELSSF 306
Cdd:cd14087  161 TCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSYSGEPWPSV-----SNLAKDF 235
                        250       260
                 ....*....|....*....|....
gi 567218350 307 ISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14087  236 IDRLLTVNPGERLSATQALKHPWI 259
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
74-334 1.06e-29

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: 116.20  E-value: 1.06e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVIQLN---IDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDG 150
Cdd:cd05620    1 KVLGKGSFGKVLLAELKGKGEYFAVKALKKDvvlIDDDVECTMVEKRVLALAWENPFLTHLYCTFQTKEHLFFVMEFLNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 151 GSLADFLKSvKTIPESYLSAIF-KQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVG 229
Cdd:cd05620   81 GDLMFHIQD-KGRFDLYRATFYaAEIVCGLQFLH-SKGIIYRDLKLDNVMLDRDGHIKIADFGMCKENVFGDNRASTFCG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 230 TYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSvfelmeaiVDQPPPALPSEnFSPELSSFIST 309
Cdd:cd05620  159 TPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFES--------IRVDTPHYPRW-ITKESKDILEK 229
                        250       260
                 ....*....|....*....|....*.
gi 567218350 310 CLQKDPNSR-SSAKELMEHPFLNKYN 334
Cdd:cd05620  230 LFERDPTRRlGVVGNIRGHPFFKTIN 255
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
66-329 1.13e-29

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: 115.87  E-value: 1.13e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  66 SLSDLDMVKFLGKGSSGVVQLVQHKWTGQFFALK-VIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDN------ 138
Cdd:cd07866    6 KLRDYEILGKLGEGTFGEVYKARQIKTGRVVALKkILMHNEKDGFPITALREIKILKKLKHPNVVPLIDMAVERpdkskr 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 139 --GAISLILEYMDGgSLADFLK--SVKtIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVS 214
Cdd:cd07866   86 krGSVYMVTPYMDH-DLSGLLEnpSVK-LTESQIKCYMLQLLEGINYLH-ENHILHRDIKAANILIDNQGILKIADFGLA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 215 TV------MTNTAGLANT-----FVGTYNYMSPERIVGNK-YGNKSDIWSLGLVVLECATGKfPYLP------------- 269
Cdd:cd07866  163 RPydgpppNPKGGGGGGTrkytnLVVTRWYRPPELLLGERrYTTAVDIWGIGCVFAEMFTRR-PILQgksdidqlhlifk 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 567218350 270 ---PDQEETWSSVFEL--MEAIVDQP--PPALPS--ENFSPELSSFISTCLQKDPNSRSSAKELMEHPF 329
Cdd:cd07866  242 lcgTPTEETWPGWRSLpgCEGVHSFTnyPRTLEErfGKLGPEGLDLLSKLLSLDPYKRLTASDALEHPY 310
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
76-347 1.50e-29

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: 115.04  E-value: 1.50e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNideaiRKSIAQELKI-NQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLA 154
Cdd:cd14091    8 IGKGSYSVCKRCIHKATGKEYAVKIIDKS-----KRDPSEEIEIlLRYGQHPNIITLRDVYDDGNSVYLVTELLRGGELL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 155 DFLKSVKTIPESYLSAIFKQVLQGLIYLhHDKHIIHRDLKPSNLL-INHRGE---VKITDFGVSTVMTNTAGLANTFVGT 230
Cdd:cd14091   83 DRILRQKFFSEREASAVMKTLTKTVEYL-HSQGVVHRDLKPSNILyADESGDpesLRICDFGFAKQLRAENGLLMTPCYT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 231 YNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYL--PPDQEE----------------TWSSVfelmeaivdqppp 292
Cdd:cd14091  162 ANFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPFAsgPNDTPEvilarigsgkidlsggNWDHV------------- 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 567218350 293 alpsenfSPELSSFISTCLQKDPNSRSSAKELMEHPFLNKYNNSEINLASYFTDA 347
Cdd:cd14091  229 -------SDSAKDLVRKMLHVDPSQRPTAAQVLQHPWIRNRDSLPQRQLTDPQDA 276
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
73-329 1.56e-29

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: 114.91  E-value: 1.56e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  73 VKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDE------AIRK-SIAQELKINQSSQCPYLVNSYQSFYdngaisLIL 145
Cdd:cd07860    5 VEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETegvpstAIREiSLLKELNHPNIVKLLDVIHTENKLY------LVF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 146 EYMDGgSLADFLKS--VKTIPESYLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKITDFgvstvmtntaGL 223
Cdd:cd07860   79 EFLHQ-DLKKFMDAsaLTGIPLPLIKSYLFQLLQGLAFCHSHR-VLHRDLKPQNLLINTEGAIKLADF----------GL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 224 ANTF---VGTYN-------YMSPERIVGNK-YGNKSDIWSLGLVVLECATGK--FP-------------YLPPDQEETWS 277
Cdd:cd07860  147 ARAFgvpVRTYThevvtlwYRAPEILLGCKyYSTAVDIWSLGCIFAEMVTRRalFPgdseidqlfrifrTLGTPDEVVWP 226
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 567218350 278 SVFELMEAIVDQPP-PALPSENFSPELS----SFISTCLQKDPNSRSSAKELMEHPF 329
Cdd:cd07860  227 GVTSMPDYKPSFPKwARQDFSKVVPPLDedgrDLLSQMLHYDPNKRISAKAALAHPF 283
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
79-332 1.60e-29

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 114.57  E-value: 1.60e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  79 GSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINqssqcPYLVNSYQSFYDNGAISLILEYMDGGSLADFLK 158
Cdd:PHA03390  27 GKFGKVSVLKHKPTQKLFVQKIIKAKNFNAIEPMVHQLMKDN-----PNFIKLYYSVTTLKGHVLIMDYIKDGDLFDLLK 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 159 SVKTIPESYLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLIN-HRGEVKITDFGVSTVMtntaGLANTFVGTYNYMSPE 237
Cdd:PHA03390 102 KEGKLSEAEVKKIIRQLVEALNDLHK-HNIIHNDIKLENVLYDrAKDRIYLCDYGLCKII----GTPSCYDGTLDYFSPE 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 238 RIVGNKYGNKSDIWSLGLVVLECATGKFPYlPPDQEETWSsvFELMEAIVDQPPPALpsENFSPELSSFISTCLQKDPNS 317
Cdd:PHA03390 177 KIKGHNYDVSFDWWAVGVLTYELLTGKHPF-KEDEDEELD--LESLLKRQQKKLPFI--KNVSKNANDFVQSMLKYNINY 251
                        250
                 ....*....|....*.
gi 567218350 318 R-SSAKELMEHPFLNK 332
Cdd:PHA03390 252 RlTNYNEIIKHPFLKI 267
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
66-330 1.76e-29

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: 116.13  E-value: 1.76e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  66 SLSDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNidEAIRKSIAQELKINQS----SQCPYLVNSYQSFYDNGAI 141
Cdd:cd05610    2 SIEEFVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKA--DMINKNMVHQVQAERDalalSKSPFIVHLYYSLQSANNV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 142 SLILEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhdKH-IIHRDLKPSNLLINHRGEVKITDFGVSTV---- 216
Cdd:cd05610   80 YLVMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLH--RHgIIHRDLKPDNMLISNEGHIKLTDFGLSKVtlnr 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 217 ------MTNTAGLA----------------------NT---------------------FVGTYNYMSPERIVGNKYGNK 247
Cdd:cd05610  158 elnmmdILTTPSMAkpkndysrtpgqvlslisslgfNTptpyrtpksvrrgaarvegerILGTPDYLAPELLLGKPHGPA 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 248 SDIWSLGLVVLECATGkfpyLPPDQEETWSSVFelmEAIV--DQPPPAlPSENFSPELSSFISTCLQKDPNSRSSAKELM 325
Cdd:cd05610  238 VDWWALGVCLFEFLTG----IPPFNDETPQQVF---QNILnrDIPWPE-GEEELSVNAQNAIEILLTMDPTKRAGLKELK 309

                 ....*
gi 567218350 326 EHPFL 330
Cdd:cd05610  310 QHPLF 314
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
76-330 1.83e-29

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: 114.22  E-value: 1.83e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNidEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLAD 155
Cdd:cd14107   10 IGRGTFGFVKRVTHKGNGECCAAKFIPLR--SSTRARAFQERDILARLSHRRLTCLLDQFETRKTLILILELCSSEELLD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 156 --FLKSVKTipESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINH--RGEVKITDFGVSTVMTNTAGLANTFvGTY 231
Cdd:cd14107   88 rlFLKGVVT--EAEVKLYIQQVLEGIGYLH-GMNILHLDIKPDNILMVSptREDIKICDFGFAQEITPSEHQFSKY-GSP 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 232 NYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLppdQEETWSSVFELMEAIVDQPPPALPSenFSPELSSFISTCL 311
Cdd:cd14107  164 EFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFA---GENDRATLLNVAEGVVSWDTPEITH--LSEDAKDFIKRVL 238
                        250
                 ....*....|....*....
gi 567218350 312 QKDPNSRSSAKELMEHPFL 330
Cdd:cd14107  239 QPDPEKRPSASECLSHEWF 257
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
74-334 1.93e-29

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: 115.45  E-value: 1.93e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVIQlnideaiRKSIAQELKIN----------QSSQCPYLVNSYQSFYDNGAISL 143
Cdd:cd05603    1 KVIGKGSFGKVLLAKRKCDGKFYAVKVLQ-------KKTILKKKEQNhimaernvllKNLKHPFLVGLHYSFQTSEKLYF 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 144 ILEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGL 223
Cdd:cd05603   74 VLDYVNGGELFFHLQRERCFLEPRARFYAAEVASAIGYLH-SLNIIYRDLKPENILLDCQGHVVLTDFGLCKEGMEPEET 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 224 ANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDqeetwssVFELMEAIVDQPPPALPSENFSPel 303
Cdd:cd05603  153 TSTFCGTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRD-------VSQMYDNILHKPLHLPGGKTVAA-- 223
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 567218350 304 SSFISTCLQKDPNSRSSAK----ELMEHPFLNKYN 334
Cdd:cd05603  224 CDLLQGLLHKDQRRRLGAKadflEIKNHVFFSPIN 258
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
76-330 1.99e-29

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: 114.82  E-value: 1.99e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQL-NIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEY--MDGGS 152
Cdd:cd07861    8 IGEGTYGVVYKGRNKKTGQIVAMKKIRLeSEEEGVPSTAIREISLLKELQHPNIVCLEDVLMQENRLYLVFEFlsMDLKK 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 153 LADFLKSVKTIPESYLSAIFKQVLQGlIYLHHDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVGTYN 232
Cdd:cd07861   88 YLDSLPKGKYMDAELVKSYLYQILQG-ILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARAFGIPVRVYTHEVVTLW 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 233 YMSPERIVGN-KYGNKSDIWSLGLVVLECATGK---------------FPYLPPDQEETWSSVFELMEAIVDQP---PPA 293
Cdd:cd07861  167 YRAPEVLLGSpRYSTPVDIWSIGTIFAEMATKKplfhgdseidqlfriFRILGTPTEDIWPGVTSLPDYKNTFPkwkKGS 246
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 567218350 294 LPS--ENFSPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd07861  247 LRTavKNLDEDGLDLLEKMLIYDPAKRISAKKALVHPYF 285
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
76-330 2.35e-29

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: 113.63  E-value: 2.35e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVI---QLNIDeaiRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGS 152
Cdd:cd14078   11 IGSGGFAKVKLATHILTGEKVAIKIMdkkALGDD---LPRVKTEIEALKNLSHQHICRLYHVIETDNKIFMVLEYCPGGE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 153 LADFLKSVKTIPESYLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLINHRGEVKITDFGVstVMTNTAGLA---NTFVG 229
Cdd:cd14078   88 LFDYIVAKDRLSEDEARVFFRQIVSAVAYVHS-QGYAHRDLKPENLLLDEDQNLKLIDFGL--CAKPKGGMDhhlETCCG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 230 TYNYMSPERIVGNKY-GNKSDIWSLG--LVVLECAtgkfpYLPPDQEETWSSVFELMEAIVDQPppalpsENFSPELSSF 306
Cdd:cd14078  165 SPAYAAPELIQGKPYiGSEADVWSMGvlLYALLCG-----FLPFDDDNVMALYRKIQSGKYEEP------EWLSPSSKLL 233
                        250       260
                 ....*....|....*....|....
gi 567218350 307 ISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14078  234 LDQMLQVDPKKRITVKELLNHPWV 257
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
76-329 2.57e-29

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: 114.45  E-value: 2.57e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQL-NIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGgSLA 154
Cdd:cd07839    8 IGEGTYGTVFKAKNRETHEIVALKRVRLdDDDEGVPSSALREICLLKELKHKNIVRLYDVLHSDKKLTLVFEYCDQ-DLK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 155 DFLKSVK-TIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFgvstvmtntaGLANTF------ 227
Cdd:cd07839   87 KYFDSCNgDIDPEIVKSFMFQLLKGLAFCH-SHNVLHRDLKPQNLLINKNGELKLADF----------GLARAFgipvrc 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 228 ----VGTYNYMSPERIVGNK-YGNKSDIWSLGLVVLECATGKFPYLP----PDQ------------EETWSSVFELMEai 286
Cdd:cd07839  156 ysaeVVTLWYRPPDVLFGAKlYSTSIDMWSAGCIFAELANAGRPLFPgndvDDQlkrifrllgtptEESWPGVSKLPD-- 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 567218350 287 vDQPPPALPS----ENFSPELSSFISTCLQK----DPNSRSSAKELMEHPF 329
Cdd:cd07839  234 -YKPYPMYPAttslVNVVPKLNSTGRDLLQNllvcNPVQRISAEEALQHPY 283
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
37-330 2.65e-29

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: 116.64  E-value: 2.65e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  37 LRVNKDGVRIVSQSEpEVLSPIKpaDDELSLSDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKViqLNIDEAIRKSIA-- 114
Cdd:cd05622   45 LRKNKNIDNFLSRYK-DTINKIR--DLRMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKL--LSKFEMIKRSDSaf 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 115 --QELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLADfLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRD 192
Cdd:cd05622  120 fwEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIH-SMGFIHRD 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 193 LKPSNLLINHRGEVKITDFGVSTVMtNTAGLA--NTFVGTYNYMSPERIVGNK----YGNKSDIWSLGLVVLECATGKFP 266
Cdd:cd05622  198 VKPDNMLLDKSGHLKLADFGTCMKM-NKEGMVrcDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTP 276
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 567218350 267 YLPPDQEETWSSVFELMEAIvdqpppALPSEN-FSPELSSFISTCL--QKDPNSRSSAKELMEHPFL 330
Cdd:cd05622  277 FYADSLVGTYSKIMNHKNSL------TFPDDNdISKEAKNLICAFLtdREVRLGRNGVEEIKRHLFF 337
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
71-330 2.71e-29

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


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 113.83  E-value: 2.71e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  71 DMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNiDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDG 150
Cdd:cd14114    5 DILEELGTGAFGVVHRCTERATGNNFAAKFIMTP-HESDKETVRKEIQIMNQLHHPKLINLHDAFEDDNEMVLILEFLSG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 151 GSLADFLKSVK-TIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHR--GEVKITDFGVSTVMtNTAGLANTF 227
Cdd:cd14114   84 GELFERIAAEHyKMSEAEVINYMRQVCEGLCHMH-ENNIVHLDIKPENIMCTTKrsNEVKLIDFGLATHL-DPKESVKVT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 228 VGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFELMEAIVDQPppalpSENFSPELSSFI 307
Cdd:cd14114  162 TGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKSCDWNFDDSA-----FSGISEEAKDFI 236
                        250       260
                 ....*....|....*....|...
gi 567218350 308 STCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14114  237 RKLLLADPNKRMTIHQALEHPWL 259
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
71-330 3.62e-29

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: 113.51  E-value: 3.62e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  71 DMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEA-----IRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLIL 145
Cdd:cd14196    8 DIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRAsrrgvSREEIEREVSILRQVLHPNIITLHDVYENRTDVVLIL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 146 EYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLhHDKHIIHRDLKPSNLLINHRG----EVKITDFGVSTVMTNTA 221
Cdd:cd14196   88 ELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYL-HTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHEIEDGV 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 222 GLANTFvGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFELMEAIVDqpppalpsENFS- 300
Cdd:cd14196  167 EFKNIF-GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDE--------EFFSh 237
                        250       260       270
                 ....*....|....*....|....*....|..
gi 567218350 301 -PELS-SFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14196  238 tSELAkDFIRKLLVKETRKRLTIQEALRHPWI 269
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
69-328 3.93e-29

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: 113.67  E-value: 3.93e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  69 DLDMVKFLGKGS-SGVVQLVQHKWTGQFFALKVIQLNIDEAI-RKSIAQELKINQSSQ---CPYLVNSYQSFYDNGAISL 143
Cdd:cd14052    1 RFANVELIGSGEfSQVYKVSERVPTGKVYAVKKLKPNYAGAKdRLRRLEEVSILRELTldgHDNIVQLIDSWEYHGHLYI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 144 ILEYMDGGSLADFLKSV---KTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNT 220
Cdd:cd14052   81 QTELCENGSLDVFLSELgllGRLDEFRVWKILVELSLGLRFIH-DHHFVHLDLKPANVLITFEGTLKIGDFGMATVWPLI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 221 AGLANTfvGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGkfpYLPPDQEETW--------------SSVFELMEAI 286
Cdd:cd14052  160 RGIERE--GDREYIAPEILSEHMYDKPADIFSLGLILLEAAAN---VVLPDNGDAWqklrsgdlsdaprlSSTDLHSASS 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 567218350 287 VDQPPPalPSENFSPELSSFISTCLQK----DPNSRSSAKELMEHP 328
Cdd:cd14052  235 PSSNPP--PDPPNMPILSGSLDRVVRWmlspEPDRRPTADDVLATP 278
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
68-331 4.39e-29

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: 114.72  E-value: 4.39e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  68 SDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKViqLNIDEAIRKSIAQELK----INQSSQCPYLVNSYQSFYDNGAISL 143
Cdd:cd05598    1 SMFEKIKTIGVGAFGEVSLVRKKDTNALYAMKT--LRKKDVLKRNQVAHVKaerdILAEADNEWVVKLYYSFQDKENLYF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 144 ILEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAG- 222
Cdd:cd05598   79 VMDYIPGGDLMSLLIKKGIFEEDLARFYIAELVCAIESVH-KMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHDs 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 223 ---LANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEET------WSSVFELmeaivdqPPPA 293
Cdd:cd05598  158 kyyLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAQTPAETqlkvinWRTTLKI-------PHEA 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 567218350 294 lpseNFSPELSSFIST--CLQKDPNSRSSAKELMEHPFLN 331
Cdd:cd05598  231 ----NLSPEAKDLILRlcCDAEDRLGRNGADEIKAHPFFA 266
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
75-330 6.09e-29

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: 112.80  E-value: 6.09e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  75 FLGKGSSGVVQLVQHKWTGQFFALKVIQLnidEAIRKSiaqELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLA 154
Cdd:cd13995   11 FIPRGAFGKVYLAQDTKTKKRMACKLIPV---EQFKPS---DVEIQACFRHENIAELYGALLWEETVHLFMEAGEGGSVL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 155 DFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVkITDFGVSTVMTNTAGLANTFVGTYNYM 234
Cdd:cd13995   85 EKLESCGPMREFEIIWVTKHVLKGLDFLH-SKNIIHHDIKPSNIVFMSTKAV-LVDFGLSVQMTEDVYVPKDLRGTEIYM 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 235 SPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFELMEAivDQPPPALPSENFSPELSSFISTCLQKD 314
Cdd:cd13995  163 SPEVILCRGHNTKADIYSLGATIIHMQTGSPPWVRRYPRSAYPSYLYIIHK--QAPPLEDIAQDCSPAMRELLEAALERN 240
                        250
                 ....*....|....*.
gi 567218350 315 PNSRSSAKELMEHPFL 330
Cdd:cd13995  241 PNHRSSAAELLKHEAL 256
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
69-327 1.01e-28

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


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 112.20  E-value: 1.01e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  69 DLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRksiaqELKINQSSQCPYLVNSYQSF----------YDN 138
Cdd:cd14047    7 DFKEIELIGSGGFGQVFKAKHRIDGKTYAIKRVKLNNEKAER-----EVKALAKLDHPNIVRYNGCWdgfdydpetsSSN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 139 GAIS------LILEYMDGGSLADFLKSVKTIPESYLSA--IFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITD 210
Cdd:cd14047   82 SSRSktkclfIQMEFCEKGTLESWIEKRNGEKLDKVLAleIFEQITKGVEYIH-SKKLIHRDLKPSNIFLVDTGKVKIGD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 211 FGVSTVMTNTAGLANTfVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLE----CATGKfpylppDQEETWSSVfelmeai 286
Cdd:cd14047  161 FGLVTSLKNDGKRTKS-KGTLSYMSPEQISSQDYGKEVDIYALGLILFEllhvCDSAF------EKSKFWTDL------- 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 567218350 287 VDQPPPALPSENFSPElSSFISTCLQKDPNSRSSAKELMEH 327
Cdd:cd14047  227 RNGILPDIFDKRYKIE-KTIIKKMLSKKPEDRPNASEILRT 266
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
76-330 1.01e-28

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: 112.80  E-value: 1.01e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGgSLAD 155
Cdd:cd07871   13 LGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTAIREVSLLKNLKHANIVTLHDIIHTERCLTLVFEYLDS-DLKQ 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 156 FLKSVKTIPESYLSAIFK-QVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVGTYNYM 234
Cdd:cd07871   92 YLDNCGNLMSMHNVKIFMfQLLRGLSYCHKRK-ILHRDLKPQNLLINEKGELKLADFGLARAKSVPTKTYSNEVVTLWYR 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 235 SPERIVGN-KYGNKSDIWSLGLVVLECATGK--FP-------------YLPPDQEETWSSV--FELMEAIVDQPPPALPS 296
Cdd:cd07871  171 PPDVLLGStEYSTPIDMWGVGCILYEMATGRpmFPgstvkeelhlifrLLGTPTEETWPGVtsNEEFRSYLFPQYRAQPL 250
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 567218350 297 ENFSPELSS----FISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd07871  251 INHAPRLDTdgidLLSSLLLYETKSRISAEAALRHSYF 288
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
74-330 1.24e-28

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: 111.95  E-value: 1.24e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVI--QLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGG 151
Cdd:cd14187   13 RFLGKGGFAKCYEITDADTKEVFAGKIVpkSLLLKPHQKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVVLELCRRR 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 152 SLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVGTY 231
Cdd:cd14187   93 SLLELHKRRKALTEPEARYYLRQIILGCQYLHRNR-VIHRDLKLGNLFLNDDMEVKIGDFGLATKVEYDGERKKTLCGTP 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 232 NYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFELMEAIvdqpppalpSENFSPELSSFISTCL 311
Cdd:cd14187  172 NYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSI---------PKHINPVAASLIQKML 242
                        250
                 ....*....|....*....
gi 567218350 312 QKDPNSRSSAKELMEHPFL 330
Cdd:cd14187  243 QTDPTARPTINELLNDEFF 261
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
76-330 1.28e-28

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: 112.79  E-value: 1.28e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGgSLAD 155
Cdd:cd07873   10 LGEGTYATVYKGRSKLTDNLVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIIHTEKSLTLVFEYLDK-DLKQ 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 156 FLKSVKTIPESYLSAIFK-QVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVGTYNYM 234
Cdd:cd07873   89 YLDDCGNSINMHNVKLFLfQLLRGLAYCHRRK-VLHRDLKPQNLLINERGELKLADFGLARAKSIPTKTYSNEVVTLWYR 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 235 SPERIVGN-KYGNKSDIWSLGLVVLECATGK---------------FPYLPPDQEETWSSVFELMEAIVDQPPPALPS-- 296
Cdd:cd07873  168 PPDILLGStDYSTQIDMWGVGCIFYEMSTGRplfpgstveeqlhfiFRILGTPTEETWPGILSNEEFKSYNYPKYRADal 247
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 567218350 297 ENFSPELSS----FISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd07873  248 HNHAPRLDSdgadLLSKLLQFEGRKRISAEEAMKHPYF 285
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
74-339 1.58e-28

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: 113.08  E-value: 1.58e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVIQLNI---DEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDG 150
Cdd:cd05590    1 RVLGKGSFGKVMLARLKESGRLYAVKVLKKDVilqDDDVECTMTEKRILSLARNHPFLTQLYCCFQTPDRLFFVMEFVNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 151 GSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVGT 230
Cdd:cd05590   81 GDLMFHIQKSRRFDEARARFYAAEITSALMFLH-DKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGIFNGKTTSTFCGT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 231 YNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEetwssvfELMEAIVDQPP--PALPSENFSPELSSFis 308
Cdd:cd05590  160 PDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENED-------DLFEAILNDEVvyPTWLSQDAVDILKAF-- 230
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 567218350 309 tcLQKDPNSR------SSAKELMEHPFLNKYNNSEIN 339
Cdd:cd05590  231 --MTKNPTMRlgsltlGGEEAILRHPFFKELDWEKLN 265
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
74-334 1.87e-28

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK6 is widely expressed in many tissues and is expressed as multiple splice variants with different domain architectures. It is post-translationally palmitoylated and localized in the membrane. GRK6 plays important roles in the regulation of dopamine, M3 muscarinic, opioid, and chemokine receptor signaling. It also plays maladaptive roles in addiction and Parkinson's disease. GRK6-deficient mice exhibit altered dopamine receptor regulation, decreased lymphocyte chemotaxis, and increased acute inflammation and neutrophil chemotaxis. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 112.04  E-value: 1.87e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVIQlniDEAIRKSIAQELKINQSS-----QCPYLVNSYQSFYDNGAISLILEYM 148
Cdd:cd05630    6 RVLGKGGFGEVCACQVRATGKMYACKKLE---KKRIKKRKGEAMALNEKQilekvNSRFVVSLAYAYETKDALCLVLTLM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 149 DGGSLADFLKSVKTIPESYLSAIF--KQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANT 226
Cdd:cd05630   83 NGGDLKFHIYHMGQAGFPEARAVFyaAEICCGLEDLHRER-IVYRDLKPENILLDDHGHIRISDLGLAVHVPEGQTIKGR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 227 fVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYlppdQEETWSSVFELMEAIVDQPPPALpSENFSPELSSF 306
Cdd:cd05630  162 -VGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPF----QQRKKKIKREEVERLVKEVPEEY-SEKFSPQARSL 235
                        250       260       270
                 ....*....|....*....|....*....|...
gi 567218350 307 ISTCLQKDPNSR-----SSAKELMEHPFLNKYN 334
Cdd:cd05630  236 CSMLLCKDPAERlgcrgGGAREVKEHPLFKKLN 268
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
71-330 2.32e-28

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: 111.63  E-value: 2.32e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  71 DMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQE-----LKINQSSQCPYLVNSYQSFYDNGAISLIL 145
Cdd:cd14195    8 EMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSSSRRGVSREeiereVNILREIQHPNIITLHDIFENKTDVVLIL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 146 EYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLINHRG----EVKITDFGVSTVMTNTA 221
Cdd:cd14195   88 ELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHS-KRIAHFDLKPENIMLLDKNvpnpRIKLIDFGIAHKIEAGN 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 222 GLANTFvGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVfelmeAIVDQPPPALPSENFSP 301
Cdd:cd14195  167 EFKNIF-GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNI-----SAVNYDFDEEYFSNTSE 240
                        250       260
                 ....*....|....*....|....*....
gi 567218350 302 ELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14195  241 LAKDFIRRLLVKDPKKRMTIAQSLEHSWI 269
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
74-329 2.52e-28

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: 112.51  E-value: 2.52e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVIQ---LNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDG 150
Cdd:cd05588    1 RVIGRGSYAKVLMVELKKTKRIYAMKVIKkelVNDDEDIDWVQTEKHVFETASNHPFLVGLHSCFQTESRLFFVIEFVNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 151 GSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVGT 230
Cdd:cd05588   81 GDLMFHMQRQRRLPEEHARFYSAEISLALNFLH-EKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTFCGT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 231 YNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFE--LMEAIVDQP---PPALpsenfSPELSS 305
Cdd:cd05588  160 PNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPFDIVGSSDNPDQNTEdyLFQVILEKPiriPRSL-----SVKAAS 234
                        250       260       270
                 ....*....|....*....|....*....|
gi 567218350 306 FISTCLQKDPNSR------SSAKELMEHPF 329
Cdd:cd05588  235 VLKGFLNKNPAERlgchpqTGFADIQSHPF 264
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
73-330 3.06e-28

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


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 111.59  E-value: 3.06e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  73 VKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGgS 152
Cdd:cd07870    5 LEKLGEGSYATVYKGISRINGQLVALKVISMKTEEGVPFTAIREASLLKGLKHANIVLLHDIIHTKETLTFVFEYMHT-D 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 153 LADFLKSVKTIPESYLSAIFK-QVLQGLIYLHHdKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVGTY 231
Cdd:cd07870   84 LAQYMIQHPGGLHPYNVRLFMfQLLRGLAYIHG-QHILHRDLKPQNLLISYLGELKLADFGLARAKSIPSQTYSSEVVTL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 232 NYMSPERIVG-NKYGNKSDIWSLGLVVLECATGKfPYLP-----PDQ------------EETWSSVFELMEAIVD-QPPP 292
Cdd:cd07870  163 WYRPPDVLLGaTDYSSALDIWGAGCIFIEMLQGQ-PAFPgvsdvFEQlekiwtvlgvptEDTWPGVSKLPNYKPEwFLPC 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 567218350 293 ALPSENF-------SPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd07870  242 KPQQLRVvwkrlsrPPKAEDLASQMLMMFPKDRISAQDALLHPYF 286
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
143-326 3.19e-28

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 115.28  E-value: 3.19e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 143 LILEYMDGGSLADFLK-----SVKTIPEsylsaIFKQVLQGLIYLHHdKHIIHRDLKPSNLLINHRGEVKITDFGV---- 213
Cdd:NF033483  84 IVMEYVDGRTLKDYIRehgplSPEEAVE-----IMIQILSALEHAHR-NGIVHRDIKPQNILITKDGRVKVTDFGIaral 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 214 -STVMTNTaglaNTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYlppDQEetwSSVfelmeAI----VD 288
Cdd:NF033483 158 sSTTMTQT----NSVLGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPF---DGD---SPV-----SVaykhVQ 222
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 567218350 289 QPPPAlPSE---NFSPELSSFISTCLQKDPNSR-SSAKELME 326
Cdd:NF033483 223 EDPPP-PSElnpGIPQSLDAVVLKATAKDPDDRyQSAAEMRA 263
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
74-329 3.64e-28

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: 110.51  E-value: 3.64e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSL 153
Cdd:cd14184    7 KVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKEHLIENEVSILRRVKHPNIIMLIEEMDTPAELYLVMELVKGGDL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 154 ADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLI----NHRGEVKITDFGVSTVMTntaGLANTFVG 229
Cdd:cd14184   87 FDAITSSTKYTERDASAMVYNLASALKYLH-GLCIVHRDIKPENLLVceypDGTKSLKLGDFGLATVVE---GPLYTVCG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 230 TYNYMSPERIVGNKYGNKSDIWSLGLV--VLECAtgkfpyLPPDQEETwssvfELMEAIVDQ--------PPPALpsENF 299
Cdd:cd14184  163 TPTYVAPEIIAETGYGLKVDIWAAGVItyILLCG------FPPFRSEN-----NLQEDLFDQillgklefPSPYW--DNI 229
                        250       260       270
                 ....*....|....*....|....*....|
gi 567218350 300 SPELSSFISTCLQKDPNSRSSAKELMEHPF 329
Cdd:cd14184  230 TDSAKELISHMLQVNVEARYTAEQILSHPW 259
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
77-330 3.86e-28

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: 110.30  E-value: 3.86e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  77 GKGSSGVVQLVQHKWTGQFFALKVIQLNIDEaiRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLADF 156
Cdd:cd14111   12 ARGRFGVIRRCRENATGKNFPAKIVPYQAEE--KQGVLQEYEILKSLHHERIMALHEAYITPRYLVLIAEFCSGKELLHS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 157 LKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGvSTVMTNTAGL--ANTFVGTYNYM 234
Cdd:cd14111   90 LIDRFRYSEDDVVGYLVQILQGLEYLH-GRRVLHLDIKPDNIMVTNLNAIKIVDFG-SAQSFNPLSLrqLGRRTGTLEYM 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 235 SPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVfelMEAIVDqPPPALPseNFSPELSSFISTCLQKD 314
Cdd:cd14111  168 APEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKI---LVAKFD-AFKLYP--NVSQSASLFLKKVLSSY 241
                        250
                 ....*....|....*.
gi 567218350 315 PNSRSSAKELMEHPFL 330
Cdd:cd14111  242 PWSRPTTKDCFAHAWL 257
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
72-330 3.99e-28

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: 111.69  E-value: 3.99e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  72 MVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNID------EAIRKSIAQELKINQSSQCPYLVNSYQSF-YDNGAISLI 144
Cdd:cd14041   10 LLHLLGRGGFSEVYKAFDLTEQRYVAVKIHQLNKNwrdekkENYHKHACREYRIHKELDHPRIVKLYDYFsLDTDSFCTV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 145 LEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHDKH-IIHRDLKPSN-LLINHR--GEVKITDFGVSTVMTNT 220
Cdd:cd14041   90 LEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKPpIIHYDLKPGNiLLVNGTacGEIKITDFGLSKIMDDD 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 221 A-------GLANTFVGTYNYMSPE-RIVGN---KYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFELMEAIVDQ 289
Cdd:cd14041  170 SynsvdgmELTSQGAGTYWYLPPEcFVVGKeppKISNKVDVWSVGVIFYQCLYGRKPFGHNQSQQDILQENTILKATEVQ 249
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 567218350 290 PPpalPSENFSPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14041  250 FP---PKPVVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYL 287
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
67-330 4.43e-28

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: 112.84  E-value: 4.43e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  67 LSDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLN--IDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLI 144
Cdd:cd05627    1 LDDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKAdmLEKEQVAHIRAERDILVEADGAWVVKMFYSFQDKRNLYLI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 145 LEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLINHRGEVKITDFGVSTVM------- 217
Cdd:cd05627   81 MEFLPGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQ-LGFIHRDIKPDNLLLDAKGHVKLSDFGLCTGLkkahrte 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 218 ----------------------------TNTAGLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLP 269
Cdd:cd05627  160 fyrnlthnppsdfsfqnmnskrkaetwkKNRRQLAYSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCS 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 567218350 270 PDQEETWSSVFELMEAIVDqpPPALPSENFSPELssFISTCLQKDPN-SRSSAKELMEHPFL 330
Cdd:cd05627  240 ETPQETYRKVMNWKETLVF--PPEVPISEKAKDL--ILRFCTDAENRiGSNGVEEIKSHPFF 297
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
67-327 5.21e-28

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


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 110.73  E-value: 5.21e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  67 LSDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVN-----------SYQSF 135
Cdd:cd14048    5 LTDFEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRIRLPNNELAREKVLREVRALAKLDHPGIVRyfnawlerppeGWQEK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 136 YDNGAISLILEYMDGGSLADFLKSVKTI---PESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFG 212
Cdd:cd14048   85 MDEVYLYIQMQLCRKENLKDWMNRRCTMesrELFVCLNIFKQIASAVEYLH-SKGLIHRDLKPSNVFFSLDDVVKVGDFG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 213 VSTVMTNTAGLANTF------------VGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATgkfpylppdqeeTWSSVF 280
Cdd:cd14048  164 LVTAMDQGEPEQTVLtpmpayakhtgqVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELIY------------SFSTQM 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 567218350 281 ELMEAIVDQPPPALPS--ENFSPELSSFISTCLQKDPNSRSSAKELMEH 327
Cdd:cd14048  232 ERIRTLTDVRKLKFPAlfTNKYPEERDMVQQMLSPSPSERPEAHEVIEH 280
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
68-326 7.18e-28

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: 109.85  E-value: 7.18e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  68 SDLDMVKFLGKGSSGVVQLvqHKWTGQF-FALKVIQ---LNIDEAIrksiaQELKINQSSQCPYLVNSYQSFYDNGAISL 143
Cdd:cd05059    4 SELTFLKELGSGQFGVVHL--GKWRGKIdVAIKMIKegsMSEDDFI-----EEAKVMMKLSHPKLVQLYGVCTKQRPIFI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 144 ILEYMDGGSLADFLKSVKTIPES-YLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTN--- 219
Cdd:cd05059   77 VTEYMANGCLLNYLRERRGKFQTeQLLEMCKDVCEAMEYLE-SNGFIHRDLAARNCLVGEQNVVKVSDFGLARYVLDdey 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 220 TAGLANTFvgTYNYMSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPYlppdqeETWSSVfELMEAI-----VDQPPPA 293
Cdd:cd05059  156 TSSVGTKF--PVKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSeGKMPY------ERFSNS-EVVEHIsqgyrLYRPHLA 226
                        250       260       270
                 ....*....|....*....|....*....|...
gi 567218350 294 lpsenfSPELSSFISTCLQKDPNSRSSAKELME 326
Cdd:cd05059  227 ------PTEVYTIMYSCWHEKPEERPTFKILLS 253
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
76-333 8.35e-28

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: 110.00  E-value: 8.35e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNID--------EAIRKSIAQELKI-NQSSQCPYLVNSYQSFYDNGAISLILE 146
Cdd:cd14182   11 LGRGVSSVVRRCIHKPTRQEYAVKIIDITGGgsfspeevQELREATLKEIDIlRKVSGHPNIIQLKDTYETNTFFFLVFD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 147 YMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLaNT 226
Cdd:cd14182   91 LMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALH-KLNIVHRDLKPENILLDDDMNIKLTDFGFSCQLDPGEKL-RE 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 227 FVGTYNYMSPERIVGNK------YGNKSDIWSLGLVVLECATGKFPYlppdqeetWSSVFELMEAIVDQPPPALPS---E 297
Cdd:cd14182  169 VCGTPGYLAPEIIECSMddnhpgYGKEVDMWSTGVIMYTLLAGSPPF--------WHRKQMLMLRMIMSGNYQFGSpewD 240
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 567218350 298 NFSPELSSFISTCLQKDPNSRSSAKELMEHPFLNKY 333
Cdd:cd14182  241 DRSDTVKDLISRFLVVQPQKRYTAEEALAHPFFQQY 276
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
74-334 9.23e-28

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: 110.95  E-value: 9.23e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQH---KWTGQFFALKVIQ---LNIDEAIRKSIaqELKINQSSQCPYLVNSYQSFYDNGAISLILEY 147
Cdd:cd05582    1 KVLGQGSFGKVFLVRKitgPDAGTLYAMKVLKkatLKVRDRVRTKM--ERDILADVNHPFIVKLHYAFQTEGKLYLILDF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 148 MDGGSLADFL-KSVKTIPES---YLSaifkQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGL 223
Cdd:cd05582   79 LRGGDLFTRLsKEVMFTEEDvkfYLA----ELALALDHLH-SLGIIYRDLKPENILLDEDGHIKLTDFGLSKESIDHEKK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 224 ANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSsvfELMEAIVDQPppalpsENFSPEL 303
Cdd:cd05582  154 AYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMT---MILKAKLGMP------QFLSPEA 224
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 567218350 304 SSFISTCLQKDPNSR-----SSAKELMEHPFLNKYN 334
Cdd:cd05582  225 QSLLRALFKRNPANRlgagpDGVEEIKRHPFFATID 260
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
64-353 1.72e-27

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: 111.64  E-value: 1.72e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  64 ELSLSDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKViqLNIDEAIRKS----IAQELKINQSSQCPYLVNSYQSFYDNG 139
Cdd:cd05624   68 QLHRDDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKI--LNKWEMLKRAetacFREERNVLVNGDCQWITTLHYAFQDEN 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 140 AISLILEYMDGGSLADFLKSVK-TIPESyLSAIFKQVLQGLIYLHHDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMT 218
Cdd:cd05624  146 YLYLVMDYYVGGDLLTLLSKFEdKLPED-MARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFGSCLKMN 224
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 219 NTAGLANTF-VGTYNYMSPERIVG-----NKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFELMEAIvdqppp 292
Cdd:cd05624  225 DDGTVQSSVaVGTPDYISPEILQAmedgmGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHEERF------ 298
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 567218350 293 ALPSE--NFSPELSSFIS--TCLQKDPNSRSSAKELMEHPFLNKYNNSEI-NL-ASYFTDAGSPLAT 353
Cdd:cd05624  299 QFPSHvtDVSEEAKDLIQrlICSRERRLGQNGIEDFKKHAFFEGLNWENIrNLeAPYIPDVSSPSDT 365
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
73-330 2.60e-27

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: 108.51  E-value: 2.60e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  73 VKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAiRKSIAQELKI-NQSSQCPyLVNSYQSFYDNGAISLILEYMDGG 151
Cdd:cd14192    9 HEVLGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKE-REEVKNEINImNQLNHVN-LIQLYDAFESKTNLTLIMEYVDGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 152 SLADflksvKTIPESY----LSAIF--KQVLQGLIYLHHdKHIIHRDLKPSNLL-INHRG-EVKITDFGVSTVMTNTAGL 223
Cdd:cd14192   87 ELFD-----RITDESYqlteLDAILftRQICEGVHYLHQ-HYILHLDLKPENILcVNSTGnQIKIIDFGLARRYKPREKL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 224 ANTFvGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVfelMEAIVDQPPPALpsENFSPEL 303
Cdd:cd14192  161 KVNF-GTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNNI---VNCKWDFDAEAF--ENLSEEA 234
                        250       260
                 ....*....|....*....|....*..
gi 567218350 304 SSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14192  235 KDFISRLLVKEKSCRMSATQCLKHEWL 261
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
76-330 2.77e-27

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: 108.33  E-value: 2.77e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVI--QLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSF-YDNGAISLILEYMDGGS 152
Cdd:cd14165    9 LGEGSYAKVKSAYSERLKCNVAIKIIdkKKAPDDFVEKFLPRELEILARLNHKSIIKTYEIFeTSDGKVYIVMELGVQGD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 153 LADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVST-VMTNTAG---LANTFV 228
Cdd:cd14165   89 LLEFIKLRGALPEDVARKMFHQLSSAIKYCH-ELDIVHRDLKCENLLLDKDFNIKLTDFGFSKrCLRDENGrivLSKTFC 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 229 GTYNYMSPERIVGNKYGNK-SDIWSLGLVVLECATGKFPYlppDQEETWSSVFELMEAIVDQPppalPSENFSPELSSFI 307
Cdd:cd14165  168 GSAAYAAPEVLQGIPYDPRiYDIWSLGVILYIMVCGSMPY---DDSNVKKMLKIQKEHRVRFP----RSKNLTSECKDLI 240
                        250       260
                 ....*....|....*....|...
gi 567218350 308 STCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14165  241 YRLLQPDVSQRLCIDEVLSHPWL 263
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
76-276 3.19e-27

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: 108.69  E-value: 3.19e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKV--IQLNIDEAIRKSIAQELKINQSSQCPYLVNS------YQSFYDNGAISLILEY 147
Cdd:cd13989    1 LGSGGFGYVTLWKHQDTGEYVAIKKcrQELSPSDKNRERWCLEVQIMKKLNHPNVVSArdvppeLEKLSPNDLPLLAMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 148 MDGGSLADFLKSVKT---IPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINH-RGEV--KITDFGVSTVMTNTA 221
Cdd:cd13989   81 CSGGDLRKVLNQPENccgLKESEVRTLLSDISSAISYLH-ENRIIHRDLKPENIVLQQgGGRViyKLIDLGYAKELDQGS 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 567218350 222 gLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETW 276
Cdd:cd13989  160 -LCTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPFLPNWQPVQW 213
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
76-328 3.52e-27

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 111.88  E-value: 3.52e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQL---NIDEAIRKSIAQELKINqssqCPY--LVNSYQSFYDNGA--------IS 142
Cdd:PTZ00283  40 LGSGATGTVLCAKRVSDGEPFAVKVVDMegmSEADKNRAQAEVCCLLN----CDFfsIVKCHEDFAKKDPrnpenvlmIA 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 143 LILEYMDGGSLADFLKS----VKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMT 218
Cdd:PTZ00283 116 LVLDYANAGDLRQEIKSraktNRTFREHEAGLLFIQVLLAVHHVH-SKHMIHRDIKSANILLCSNGLVKLGDFGFSKMYA 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 219 NTAG--LANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETwssvfeLMEAIVDQPPPaLPS 296
Cdd:PTZ00283 195 ATVSddVGRTFCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGENMEEV------MHKTLAGRYDP-LPP 267
                        250       260       270
                 ....*....|....*....|....*....|..
gi 567218350 297 eNFSPELSSFISTCLQKDPNSRSSAKELMEHP 328
Cdd:PTZ00283 268 -SISPEMQEIVTALLSSDPKRRPSSSKLLNMP 298
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
76-334 4.31e-27

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: 108.81  E-value: 4.31e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQ---LNIDEAIRKSIAQELKINQSSqCPYLVNSYQSFYDNGAISLILEYMDGGS 152
Cdd:cd05585    2 IGKGSFGKVMQVRKKDTSRIYALKTIRkahIVSRSEVTHTLAERTVLAQVD-CPFIVPLKFSFQSPEKLYLVLAFINGGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 153 LADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVGTYN 232
Cdd:cd05585   81 LFHHLQREGRFDLSRARFYTAELLCALECLH-KFNVIYRDLKPENILLDYTGHIALCDFGLCKLNMKDDDKTNTFCGTPE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 233 YMSPERIVGNKYGNKSDIWSLGLVVLECATGkfpyLPPDQEEtwsSVFELMEAIVdQPPPALPsENFSPELSSFISTCLQ 312
Cdd:cd05585  160 YLAPELLLGHGYTKAVDWWTLGVLLYEMLTG----LPPFYDE---NTNEMYRKIL-QEPLRFP-DGFDRDAKDLLIGLLN 230
                        250       260
                 ....*....|....*....|....*
gi 567218350 313 KDPNSR---SSAKELMEHPFLNKYN 334
Cdd:cd05585  231 RDPTKRlgyNGAQEIKNHPFFDQID 255
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
143-328 5.52e-27

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


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 107.32  E-value: 5.52e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 143 LILEY----MDggsLADFLKSVKTIPESYLSAIFKQVLQGlIYLHHDKHIIHRDLKPSNLLIN-HRGEVKITDFGVSTVM 217
Cdd:cd14005   83 LIMERpepcQD---LFDFITERGALSENLARIIFRQVVEA-VRHCHQRGVLHRDIKDENLLINlRTGEVKLIDFGCGALL 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 218 TNTAglANTFVGTYNYMSPERIVGNKY-GNKSDIWSLGLVVLECATGKFPYlppDQEEtwssvfELMEAIVDQPPpalps 296
Cdd:cd14005  159 KDSV--YTDFDGTRVYSPPEWIRHGRYhGRPATVWSLGILLYDMLCGDIPF---ENDE------QILRGNVLFRP----- 222
                        170       180       190
                 ....*....|....*....|....*....|..
gi 567218350 297 eNFSPELSSFISTCLQKDPNSRSSAKELMEHP 328
Cdd:cd14005  223 -RLSKECCDLISRCLQFDPSKRPSLEQILSHP 253
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
69-343 7.47e-27

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: 108.60  E-value: 7.47e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  69 DLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQlniDEAIRKSIAQELKINQ--------SSQCPYLVNSYQSFYDNGA 140
Cdd:cd14223    1 DFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLD---KKRIKMKQGETLALNErimlslvsTGDCPFIVCMSYAFHTPDK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 141 ISLILEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNT 220
Cdd:cd14223   78 LSFILDLMNGGDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMH-SRFVVYRDLKPANILLDEFGHVRISDLGLACDFSKK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 221 AGLANtfVGTYNYMSPERIV-GNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFELMEAIVDQPppalpsENF 299
Cdd:cd14223  157 KPHAS--VGTHGYMAPEVLQkGVAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTMAVELP------DSF 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 567218350 300 SPELSSFISTCLQKDPNSR-----SSAKELMEHPFLNKYNNSEINLASY 343
Cdd:cd14223  229 SPELRSLLEGLLQRDVNRRlgcmgRGAQEVKEEPFFRGLDWQMVFLQKY 277
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
79-327 7.85e-27

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


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 107.43  E-value: 7.85e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  79 GSSGVVQLVQHKWTGQFFALKVIQLNIDEAIR---KSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSL-- 153
Cdd:cd14146    3 GVGGFGKVYRATWKGQEVAVKAARQDPDEDIKataESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFARGGTLnr 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 154 -------ADFLKSVKTIPESYLSAIFKQVLQGLIYLHHDK--HIIHRDLKPSNLLINHRGE--------VKITDFGVSTV 216
Cdd:cd14146   83 alaaanaAPGPRRARRIPPHILVNWAVQIARGMLYLHEEAvvPILHRDLKSSNILLLEKIEhddicnktLKITDFGLARE 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 217 MTNTAGLANTfvGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVfelmeaIVDQPPPALPS 296
Cdd:cd14146  163 WHRTTKMSAA--GTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYRGIDGLAVAYGV------AVNKLTLPIPS 234
                        250       260       270
                 ....*....|....*....|....*....|.
gi 567218350 297 ENFSPeLSSFISTCLQKDPNSRSSAKELMEH 327
Cdd:cd14146  235 TCPEP-FAKLMKECWEQDPHIRPSFALILEQ 264
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
76-330 9.28e-27

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: 106.87  E-value: 9.28e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQL-VQHKWTGQFfALKVI--QLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSF-YDNGAISLILEYMDGg 151
Cdd:cd14164    8 IGEGSFSKVKLaTSQKYCCKV-AIKIVdrRRASPDFVQKFLPRELSILRRVNHPNIVQMFECIeVANGRLYIVMEAAAT- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 152 SLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGE-VKITDFGVSTVMTNTAGLANTFVGT 230
Cdd:cd14164   86 DLLQKIQEVHHIPKDLARDMFAQMVGAVNYLH-DMNIVHRDLKCENILLSADDRkIKIADFGFARFVEDYPELSTTFCGS 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 231 YNYMSPERIVGNKY-GNKSDIWSLGLVVLECATGKFPYlppdqEETWSSVFELMEAIVDQPPPALPSEnfspELSSFIST 309
Cdd:cd14164  165 RAYTPPEVILGTPYdPKKYDVWSLGVVLYVMVTGTMPF-----DETNVRRLRLQQRGVLYPSGVALEE----PCRALIRT 235
                        250       260
                 ....*....|....*....|.
gi 567218350 310 CLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14164  236 LLQFNPSTRPSIQQVAGNSWL 256
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
74-333 1.04e-26

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 108.31  E-value: 1.04e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVIQLN------------IDE-AIRKSIAQELKINQSSQCPYLVNSYQSFYDNGA 140
Cdd:PTZ00024  15 AHLGEGTYGKVEKAYDTLTGKIVAIKKVKIIeisndvtkdrqlVGMcGIHFTTLRELKIMNEIKHENIMGLVDVYVEGDF 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 141 ISLILEYMDGgSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVST----- 215
Cdd:PTZ00024  95 INLVMDIMAS-DLKKVVDRKIRLTESQVKCILLQILNGLNVLH-KWYFMHRDLSPANIFINSKGICKIADFGLARrygyp 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 216 -VMTNTAGLANTF--------VGTYNYMSPERIVG-NKYGNKSDIWSLGLVVLECATGKfPYLPPDQE-ETWSSVFELME 284
Cdd:PTZ00024 173 pYSDTLSKDETMQrreemtskVVTLWYRAPELLMGaEKYHFAVDMWSVGCIFAELLTGK-PLFPGENEiDQLGRIFELLG 251
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 567218350 285 AIVDQPPP---ALPS-ENFSP----ELSSFISTC-----------LQKDPNSRSSAKELMEHPFLNKY 333
Cdd:PTZ00024 252 TPNEDNWPqakKLPLyTEFTPrkpkDLKTIFPNAsddaidllqslLKLNPLERISAKEALKHEYFKSD 319
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
72-340 1.14e-26

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: 107.45  E-value: 1.14e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  72 MVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNID------EAIRKSIAQELKINQSSQCPYLVNSYQSF-YDNGAISLI 144
Cdd:cd14040   10 LLHLLGRGGFSEVYKAFDLYEQRYAAVKIHQLNKSwrdekkENYHKHACREYRIHKELDHPRIVKLYDYFsLDTDTFCTV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 145 LEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHDKH-IIHRDLKPSNLLI---NHRGEVKITDFGVSTVMTNT 220
Cdd:cd14040   90 LEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKPpIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDD 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 221 A------GLANTFVGTYNYMSPE-RIVGN---KYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFELMEAIVDQP 290
Cdd:cd14040  170 SygvdgmDLTSQGAGTYWYLPPEcFVVGKeppKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQENTILKATEVQF 249
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 567218350 291 P--PALpsenfSPELSSFISTCLQKDPNSRSSAKELMEHPFL---NKYNNSEINL 340
Cdd:cd14040  250 PvkPVV-----SNEAKAFIRRCLAYRKEDRFDVHQLASDPYLlphMRRSNSSGNL 299
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
76-267 1.97e-26

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: 105.81  E-value: 1.97e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKwTGQFFALKVIQLN--IDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSL 153
Cdd:cd14161   11 LGKGTYGRVKKARDS-SGRLVAIKSIRKDriKDEQDLLHIRREIEIMSSLNHPHIISVYEVFENSSKIVIVMEYASRGDL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 154 ADFLKSVKTIPESYLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKITDFGVSTVMtNTAGLANTFVGTYNY 233
Cdd:cd14161   90 YDYISERQRLSELEARHFFRQIVSAVHYCHANG-IVHRDLKLENILLDANGNIKIADFGLSNLY-NQDKFLQTYCGSPLY 167
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 567218350 234 MSPERIVGNKY-GNKSDIWSLGLVVLECATGKFPY 267
Cdd:cd14161  168 ASPEIVNGRPYiGPEVDSWSLGVLLYILVHGTMPF 202
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
67-337 2.44e-26

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: 107.26  E-value: 2.44e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  67 LSDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVI----QlNIDEAIR--KSIA--QELKinqssQCPY---LVNSYQSf 135
Cdd:cd07852    6 LRRYEILKKLGKGAYGIVWKAIDKKTGEVVALKKIfdafR-NATDAQRtfREIMflQELN-----DHPNiikLLNVIRA- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 136 yDNGA-ISLILEYMDggslADfLKSV--KTIPES----YlsaIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKI 208
Cdd:cd07852   79 -ENDKdIYLVFEYME----TD-LHAVirANILEDihkqY---IMYQLLKALKYLH-SGGVIHRDLKPSNILLNSDCRVKL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 209 TDFG----VSTVMTNTAGLANT-FVGTYNYMSPERIVGNKYGNKS-DIWSLGLVVLECATGK--FP-------------Y 267
Cdd:cd07852  149 ADFGlarsLSQLEEDDENPVLTdYVATRWYRAPEILLGSTRYTKGvDMWSVGCILGEMLLGKplFPgtstlnqlekiieV 228
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 567218350 268 L-PPDQE--ETWSSVF--ELMEAIVDQPPPALPsENF---SPELSSFISTCLQKDPNSRSSAKELMEHPFLNKYNNSE 337
Cdd:cd07852  229 IgRPSAEdiESIQSPFaaTMLESLPPSRPKSLD-ELFpkaSPDALDLLKKLLVFNPNKRLTAEEALRHPYVAQFHNPA 305
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
71-330 2.52e-26

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: 106.45  E-value: 2.52e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  71 DMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDeaiRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDG 150
Cdd:cd14085    6 EIESELGRGATSVVYRCRQKGTQKPYAVKKLKKTVD---KKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLELVTG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 151 GSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGE---VKITDFGVSTVMTNTAgLANTF 227
Cdd:cd14085   83 GELFDRIVEKGYYSERDAADAVKQILEAVAYLH-ENGIVHRDLKPENLLYATPAPdapLKIADFGLSKIVDQQV-TMKTV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 228 VGTYNYMSPERIVGNKYGNKSDIWSLGLV--VLECAtgkfpYLPPDQEETWSSVFE-LMEAIVDQPPPALpsENFSPELS 304
Cdd:cd14085  161 CGTPGYCAPEILRGCAYGPEVDMWSVGVItyILLCG-----FEPFYDERGDQYMFKrILNCDYDFVSPWW--DDVSLNAK 233
                        250       260
                 ....*....|....*....|....*.
gi 567218350 305 SFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14085  234 DLVKKLIVLDPKKRLTTQQALQHPWV 259
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
76-330 7.19e-26

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: 105.05  E-value: 7.19e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKViqLNIDEAIRKS---------------------------IAQELKINQSSQCPYL 128
Cdd:cd14199   10 IGKGSYGVVKLAYNEDDNTYYAMKV--LSKKKLMRQAgfprrppprgaraapegctqprgpierVYQEIAILKKLDHPNV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 129 VNSYQSFYDNGA--ISLILEYMDGGSLADfLKSVKTIPESYLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEV 206
Cdd:cd14199   88 VKLVEVLDDPSEdhLYMVFELVKQGPVME-VPTLKPLSEDQARFYFQDLIKGIEYLHYQK-IIHRDVKPSNLLVGEDGHI 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 207 KITDFGVSTVMTNTAGLANTFVGTYNYMSPERIVGNK---YGNKSDIWSLGlVVLEC-ATGKFPYLppDQEetwssVFEL 282
Cdd:cd14199  166 KIADFGVSNEFEGSDALLTNTVGTPAFMAPETLSETRkifSGKALDVWAMG-VTLYCfVFGQCPFM--DER-----ILSL 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 567218350 283 MEAIVDQPPPALPSENFSPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14199  238 HSKIKTQPLEFPDQPDISDDLKDLLFRMLDKNPESRISVPEIKLHPWV 285
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
76-330 7.56e-26

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: 105.34  E-value: 7.56e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQeLKINQSSqcPYLVNSYQSFYDNGAISLILEYMDGGSLAD 155
Cdd:cd14180   14 LGEGSFSVCRKCRHRQSGQEYAVKIISRRMEANTQREVAA-LRLCQSH--PNIVALHEVLHDQYHTYLVMELLRGGELLD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 156 FLKSVKTIPESYLSAIFKQVLQGLIYLhHDKHIIHRDLKPSNLLINHRGE---VKITDFGVSTVMTNTAGLANTFVGTYN 232
Cdd:cd14180   91 RIKKKARFSESEASQLMRSLVSAVSFM-HEAGVVHRDLKPENILYADESDgavLKVIDFGFARLRPQGSRPLQTPCFTLQ 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 233 YMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFELMEAIV--DQPPPALPSENFSPELSSFISTC 310
Cdd:cd14180  170 YAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSKRGKMFHNHAADIMHKIKegDFSLEGEAWKGVSEEAKDLVRGL 249
                        250       260
                 ....*....|....*....|
gi 567218350 311 LQKDPNSRSSAKELMEHPFL 330
Cdd:cd14180  250 LTVDPAKRLKLSELRESDWL 269
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
76-330 8.41e-26

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: 104.13  E-value: 8.41e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVI---QLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGS 152
Cdd:cd14070   10 LGEGSFAKVREGLHAVTGEKVAIKVIdkkKAKKDSYVTKNLRREGRIQQMIRHPNITQLLDILETENSYYLVMELCPGGN 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 153 LADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVStvmtNTA---GLANTFV- 228
Cdd:cd14070   90 LMHRIYDKKRLEEREARRYIRQLVSAVEHLH-RAGVVHRDLKIENLLLDENDNIKLIDFGLS----NCAgilGYSDPFSt 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 229 --GTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPY-LPPdqeetwSSVFELMEAIVDQPPPALPSEnFSPELSS 305
Cdd:cd14070  165 qcGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPFtVEP------FSLRALHQKMVDKEMNPLPTD-LSPGAIS 237
                        250       260
                 ....*....|....*....|....*
gi 567218350 306 FISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14070  238 FLRSLLEPDPLKRPNIKQALANRWL 262
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
91-267 8.74e-26

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: 104.01  E-value: 8.74e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  91 WTGQFFALKVIQLNIDEAI---RKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLADFLkSVKTIPESY 167
Cdd:cd14061   15 WRGEEVAVKAARQDPDEDIsvtLENVRQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEYARGGALNRVL-AGRKIPPHV 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 168 LSAIFKQVLQGLIYLHHDKH--IIHRDLKPSNLLINHRGE--------VKITDFGVSTVMTNTAGLANTfvGTYNYMSPE 237
Cdd:cd14061   94 LVDWAIQIARGMNYLHNEAPvpIIHRDLKSSNILILEAIEnedlenktLKITDFGLAREWHKTTRMSAA--GTYAWMAPE 171
                        170       180       190
                 ....*....|....*....|....*....|
gi 567218350 238 RIVGNKYGNKSDIWSLGLVVLECATGKFPY 267
Cdd:cd14061  172 VIKSSTFSKASDVWSYGVLLWELLTGEVPY 201
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
73-330 9.00e-26

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 105.35  E-value: 9.00e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  73 VKFLGKGSSGVVQLVQHKWTGQFFALKVI-------QLNIDE-AIRKSIAQELKINQSSQ-CPYLVNSYQSFYDNGA-IS 142
Cdd:cd14136   15 VRKLGWGHFSTVWLCWDLQNKRFVALKVVksaqhytEAALDEiKLLKCVREADPKDPGREhVVQLLDDFKHTGPNGThVC 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 143 LILEYMdGGSLADFLKS--VKTIPESYLSAIFKQVLQGLIYLHHDKHIIHRDLKPSNLLINH-RGEVKITDFGVSTVM-- 217
Cdd:cd14136   95 MVFEVL-GPNLLKLIKRynYRGIPLPLVKKIARQVLQGLDYLHTKCGIIHTDIKPENVLLCIsKIEVKIADLGNACWTdk 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 218 --TNTaglantfVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYlPPDQEETWSS-------VFELMEAIvd 288
Cdd:cd14136  174 hfTED-------IQTRQYRSPEVILGAGYGTPADIWSTACMAFELATGDYLF-DPHSGEDYSRdedhlalIIELLGRI-- 243
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 567218350 289 qPPPALPSENFSPE------------------------------------LSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14136  244 -PRSIILSGKYSREffnrkgelrhisklkpwpledvlvekykwskeeakeFASFLLPMLEYDPEKRATAAQCLQHPWL 320
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
65-343 1.27e-25

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK3, also called beta-adrenergic receptor kinase 2 (beta-ARK2), is widely expressed in many tissues. It is involved in modulating the cholinergic response of airway smooth muscles, and also plays a role in dopamine receptor regulation. GRK3-deficient mice show a lack of olfactory receptor desensitization and altered regulation of the M2 muscarinic airway. GRK3 promoter polymorphisms may also be associated with bipolar disorder. GRK3 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 105.53  E-value: 1.27e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  65 LSLSDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQlniDEAIRKSIAQELKINQ--------SSQCPYLVNSYQSFY 136
Cdd:cd05633    2 LTMNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLD---KKRIKMKQGETLALNErimlslvsTGDCPFIVCMTYAFH 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 137 DNGAISLILEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTV 216
Cdd:cd05633   79 TPDKLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMH-NRFVVYRDLKPANILLDEHGHVRISDLGLACD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 217 MTNTAGLANtfVGTYNYMSPERIV-GNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSsvFELMEAIVDQPPPalp 295
Cdd:cd05633  158 FSKKKPHAS--VGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHE--IDRMTLTVNVELP--- 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 567218350 296 sENFSPELSSFISTCLQKDPNSR-----SSAKELMEHPFLNKYNNSEINLASY 343
Cdd:cd05633  231 -DSFSPELKSLLEGLLQRDVSKRlgchgRGAQEVKEHSFFKGIDWQQVYLQKY 282
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
76-330 1.27e-25

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: 104.74  E-value: 1.27e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLAD 155
Cdd:cd14168   18 LGTGAFSEVVLAEERATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGELFD 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 156 FLKSVKTIPESYLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLI---NHRGEVKITDFGVSTvMTNTAGLANTFVGTYN 232
Cdd:cd14168   98 RIVEKGFYTEKDASTLIRQVLDAVYYLHR-MGIVHRDLKPENLLYfsqDEESKIMISDFGLSK-MEGKGDVMSTACGTPG 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 233 YMSPERIVGNKYGNKSDIWSLGLV--VLECAtgkfpyLPPDQEETWSSVFE-LMEAIVDQPPPALpsENFSPELSSFIST 309
Cdd:cd14168  176 YVAPEVLAQKPYSKAVDCWSIGVIayILLCG------YPPFYDENDSKLFEqILKADYEFDSPYW--DDISDSAKDFIRN 247
                        250       260
                 ....*....|....*....|.
gi 567218350 310 CLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14168  248 LMEKDPNKRYTCEQALRHPWI 268
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
76-330 1.30e-25

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: 103.55  E-value: 1.30e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSG-VVQLVQHK----WTGQFFalKVIQLNIDEAIRksiaQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDG 150
Cdd:cd14191   10 LGSGKFGqVFRLVEKKtkkvWAGKFF--KAYSAKEKENIR----QEISIMNCLHHPKLVQCVDAFEEKANIVMVLEMVSG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 151 GSLAD-FLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLL-INHRG-EVKITDFGVSTVMTNTAGLANTF 227
Cdd:cd14191   84 GELFErIIDEDFELTERECIKYMRQISEGVEYIH-KQGIVHLDLKPENIMcVNKTGtKIKLIDFGLARRLENAGSLKVLF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 228 vGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVfelMEAIVDQPPPALpsENFSPELSSFI 307
Cdd:cd14191  163 -GTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANV---TSATWDFDDEAF--DEISDDAKDFI 236
                        250       260
                 ....*....|....*....|...
gi 567218350 308 STCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14191  237 SNLLKKDMKARLTCTQCLQHPWL 259
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
76-330 1.70e-25

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: 103.45  E-value: 1.70e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNiDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLAD 155
Cdd:cd14193   12 LGGGRFGQVHKCEEKSSGLKLAAKIIKAR-SQKEKEEVKNEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYVDGGELFD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 156 flksvKTIPESY----LSAI--FKQVLQGLIYLHHdKHIIHRDLKPSNLLINHR--GEVKITDFGVSTVMTNTAGLANTF 227
Cdd:cd14193   91 -----RIIDENYnlteLDTIlfIKQICEGIQYMHQ-MYILHLDLKPENILCVSReaNQVKIIDFGLARRYKPREKLRVNF 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 228 vGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFELMEAIVDQPppalpSENFSPELSSFI 307
Cdd:cd14193  165 -GTPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILACQWDFEDEE-----FADISEEAKDFI 238
                        250       260
                 ....*....|....*....|...
gi 567218350 308 STCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14193  239 SKLLIKEKSWRMSASEALKHPWL 261
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
105-330 1.78e-25

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: 103.65  E-value: 1.78e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 105 IDEAIRKSIAQELKINQSSQCPYLVNSYQSFYD----NGAISLILEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLI 180
Cdd:cd14031   48 LTKAEQQRFKEEAEMLKGLQHPNIVRFYDSWESvlkgKKCIVLVTELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLQ 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 181 YLH-HDKHIIHRDLKPSNLLINH-RGEVKITDFGVSTVMTNTagLANTFVGTYNYMSPErIVGNKYGNKSDIWSLGLVVL 258
Cdd:cd14031  128 FLHtRTPPIIHRDLKCDNIFITGpTGSVKIGDLGLATLMRTS--FAKSVIGTPEFMAPE-MYEEHYDESVDVYAFGMCML 204
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 567218350 259 ECATGKFPYlppdqeETWSSVFELMEAIVDQPPPALPSENFSPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14031  205 EMATSEYPY------SECQNAAQIYRKVTSGIKPASFNKVTDPEVKEIIEGCIRQNKSERLSIKDLLNHAFF 270
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
64-327 1.83e-25

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: 103.58  E-value: 1.83e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  64 ELSLSDLDMVKFLGKGSSGvvQLVQHKWTGQFFALKVIQLNIDEAIRKSIA---QELKINQSSQCPYLVNSYQSFYDNGA 140
Cdd:cd14145    2 EIDFSELVLEEIIGIGGFG--KVYRAIWIGDEVAVKAARHDPDEDISQTIEnvrQEAKLFAMLKHPNIIALRGVCLKEPN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 141 ISLILEYMDGGSLADFLkSVKTIPESYLSAIFKQVLQGLIYLHHDK--HIIHRDLKPSNLLINHRGE--------VKITD 210
Cdd:cd14145   80 LCLVMEFARGGPLNRVL-SGKRIPPDILVNWAVQIARGMNYLHCEAivPVIHRDLKSSNILILEKVEngdlsnkiLKITD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 211 FGVSTVMTNTAGLANTfvGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVfeLMEAIvdqp 290
Cdd:cd14145  159 FGLAREWHRTTKMSAA--GTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPFRGIDGLAVAYGV--AMNKL---- 230
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 567218350 291 ppALPSENFSPE-LSSFISTCLQKDPNSRSSAKELMEH 327
Cdd:cd14145  231 --SLPIPSTCPEpFARLMEDCWNPDPHSRPPFTNILDQ 266
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
64-330 1.98e-25

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: 104.11  E-value: 1.98e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  64 ELSLSDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQL-NIDEAIRKSIAQELKINQSSQCPYLVN----------SY 132
Cdd:cd07864    3 KRCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLdNEKEGFPITAIREIKILRQLNHRSVVNlkeivtdkqdAL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 133 QSFYDNGAISLILEYMDGgSLADFLKS-VKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDF 211
Cdd:cd07864   83 DFKKDKGAFYLVFEYMDH-DLMGLLESgLVHFSEDHIKSFMKQLLEGLNYCH-KKNFLHRDIKCSNILLNNKGQIKLADF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 212 GVSTVMTNTAGLANT-FVGTYNYMSPERIVGN-KYGNKSDIWSLGLVVLECATGKfPYLPPDQEetwSSVFELMEAIVDQ 289
Cdd:cd07864  161 GLARLYNSEESRPYTnKVITLWYRPPELLLGEeRYGPAIDVWSCGCILGELFTKK-PIFQANQE---LAQLELISRLCGS 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 567218350 290 PPPA-------LPSEN-FSP---------ELSSFIST--------CLQKDPNSRSSAKELMEHPFL 330
Cdd:cd07864  237 PCPAvwpdvikLPYFNtMKPkkqyrrrlrEEFSFIPTpaldlldhMLTLDPSKRCTAEQALNSPWL 302
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
76-363 2.00e-25

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: 104.30  E-value: 2.00e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGgSLAD 155
Cdd:cd07872   14 LGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIVHTDKSLTLVFEYLDK-DLKQ 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 156 FLKSVKTIPESYLSAIF-KQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVGTYNYM 234
Cdd:cd07872   93 YMDDCGNIMSMHNVKIFlYQILRGLAYCHRRK-VLHRDLKPQNLLINERGELKLADFGLARAKSVPTKTYSNEVVTLWYR 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 235 SPERIVG-NKYGNKSDIWSLGLVVLECATGK---------------FPYLPPDQEETW---SSVFELMEAIVDQPPPAlP 295
Cdd:cd07872  172 PPDVLLGsSEYSTQIDMWGVGCIFFEMASGRplfpgstvedelhliFRLLGTPTEETWpgiSSNDEFKNYNFPKYKPQ-P 250
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 567218350 296 SENFSPELSS----FISTCLQKDPNSRSSAKELMEHpflnkynnseinlaSYFTDAGSPLATLGNLSGTFSV 363
Cdd:cd07872  251 LINHAPRLDTegieLLTKFLQYESKKRISAEEAMKH--------------AYFRSLGTRIHSLPESISIFSL 308
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
76-339 2.21e-25

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: 103.95  E-value: 2.21e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIqlnidEAIRKSIAQELKI-NQSSQCPYLVnSYQSFYDNG-AISLILEYMDGGSL 153
Cdd:cd14175    9 IGVGSYSVCKRCVHKATNMEYAVKVI-----DKSKRDPSEEIEIlLRYGQHPNII-TLKDVYDDGkHVYLVTELMRGGEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 154 ADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLL-INHRGE---VKITDFGVSTVMTNTAGLANTFVG 229
Cdd:cd14175   83 LDKILRQKFFSEREASSVLHTICKTVEYLH-SQGVVHRDLKPSNILyVDESGNpesLRICDFGFAKQLRAENGLLMTPCY 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 230 TYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYL--PPDQEEtwssvfELMEAIvDQPPPALPSENF---SPELS 304
Cdd:cd14175  162 TANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFAngPSDTPE------EILTRI-GSGKFTLSGGNWntvSDAAK 234
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 567218350 305 SFISTCLQKDPNSRSSAKELMEHPFLNKYN---NSEIN 339
Cdd:cd14175  235 DLVSKMLHVDPHQRLTAKQVLQHPWITQKDklpQSQLN 272
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
74-334 2.71e-25

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK4 has a limited tissue distribution. It is mainly found in the testis, but is also present in the cerebellum and kidney. It is expressed as multiple splice variants with different domain architectures and is post-translationally palmitoylated and localized in the membrane. GRK4 polymorphisms are associated with hypertension and salt sensitivity, as they cause hyperphosphorylation, desensitization, and internalization of the dopamine 1 (D1) receptor while increasing the expression of the angiotensin II type 1 receptor. GRK4 plays a crucial role in the D1 receptor regulation of sodium excretion and blood pressure. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 103.53  E-value: 2.71e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVIQlniDEAIRKSIAQELKINQSS-----QCPYLVNSYQSFYDNGAISLILEYM 148
Cdd:cd05631    6 RVLGKGGFGEVCACQVRATGKMYACKKLE---KKRIKKRKGEAMALNEKRilekvNSRFVVSLAYAYETKDALCLVLTIM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 149 DGGSLADFLKSVKTIPESYLSAIF--KQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANT 226
Cdd:cd05631   83 NGGDLKFHIYNMGNPGFDEQRAIFyaAELCCGLEDLQRER-IVYRDLKPENILLDDRGHIRISDLGLAVQIPEGETVRGR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 227 fVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFELMEAivDQPPpalPSENFSPELSSF 306
Cdd:cd05631  162 -VGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKERVKREEVDRRVKE--DQEE---YSEKFSEDAKSI 235
                        250       260       270
                 ....*....|....*....|....*....|...
gi 567218350 307 ISTCLQKDPNSR-----SSAKELMEHPFLNKYN 334
Cdd:cd05631  236 CRMLLTKNPKERlgcrgNGAAGVKQHPIFKNIN 268
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
110-330 2.88e-25

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: 102.85  E-value: 2.88e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 110 RKSIAQELKINQSSQCPYLVNSYqSFYDNGA-----ISLILEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLH- 183
Cdd:cd14032   44 RQRFKEEAEMLKGLQHPNIVRFY-DFWESCAkgkrcIVLVTELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHt 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 184 HDKHIIHRDLKPSNLLINH-RGEVKITDFGVSTVmtNTAGLANTFVGTYNYMSPErIVGNKYGNKSDIWSLGLVVLECAT 262
Cdd:cd14032  123 RTPPIIHRDLKCDNIFITGpTGSVKIGDLGLATL--KRASFAKSVIGTPEFMAPE-MYEEHYDESVDVYAFGMCMLEMAT 199
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 567218350 263 GKFPYlppdqeETWSSVFELMEAIVDQPPPALPSENFSPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14032  200 SEYPY------SECQNAAQIYRKVTCGIKPASFEKVTDPEIKEIIGECICKNKEERYEIKDLLSHAFF 261
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
71-329 2.98e-25

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: 102.76  E-value: 2.98e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  71 DMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQL--NIDEAIRKSIaqelkINQSS-QCPYLVNSYQSFYDNGAISLILEY 147
Cdd:cd14665    3 ELVKDIGSGNFGVARLMRDKQTKELVAVKYIERgeKIDENVQREI-----INHRSlRHPNIVRFKEVILTPTHLAIVMEY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 148 MDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLhHDKHIIHRDLKPSNLLINHRG--EVKITDFGVSTVMTNTAGLAN 225
Cdd:cd14665   78 AAGGELFERICNAGRFSEDEARFFFQQLISGVSYC-HSMQICHRDLKLENTLLDGSPapRLKICDFGYSKSSVLHSQPKS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 226 TfVGTYNYMSPERIVGNKYGNK-SDIWSLGLVVLECATGKFPYLPPDQEETWSSVFELMEAIVDQPPPALpseNFSPELS 304
Cdd:cd14665  157 T-VGTPAYIAPEVLLKKEYDGKiADVWSCGVTLYVMLVGAYPFEDPEEPRNFRKTIQRILSVQYSIPDYV---HISPECR 232
                        250       260
                 ....*....|....*....|....*
gi 567218350 305 SFISTCLQKDPNSRSSAKELMEHPF 329
Cdd:cd14665  233 HLISRIFVADPATRITIPEIRNHEW 257
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
76-328 3.06e-25

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: 102.75  E-value: 3.06e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNideaiRKSiAQELKIN-QSSQCPYLVN---SYQSFYDNGAISLI-LEYMDG 150
Cdd:cd14089    9 LGLGINGKVLECFHKKTGEKFALKVLRDN-----PKA-RREVELHwRASGCPHIVRiidVYENTYQGRKCLLVvMECMEG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 151 GSLADFLKSVKTIP--ESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGE---VKITDFGVSTVMTNTAGLaN 225
Cdd:cd14089   83 GELFSRIQERADSAftEREAAEIMRQIGSAVAHLH-SMNIAHRDLKPENLLYSSKGPnaiLKLTDFGFAKETTTKKSL-Q 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 226 TFVGTYNYMSPERIVGNKYgNKS-DIWSLGLV--VLEC---------------------ATGKFPYlpPDQEetWSSVfe 281
Cdd:cd14089  161 TPCYTPYYVAPEVLGPEKY-DKScDMWSLGVImyILLCgyppfysnhglaispgmkkriRNGQYEF--PNPE--WSNV-- 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 567218350 282 lmeaivdqpppalpsenfSPELSSFISTCLQKDPNSRSSAKELMEHP 328
Cdd:cd14089  234 ------------------SEEAKDLIRGLLKTDPSERLTIEEVMNHP 262
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
110-330 3.13e-25

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: 102.77  E-value: 3.13e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 110 RKSIAQELKINQSSQCPYLVNSYQSFYD----NGAISLILEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLH-H 184
Cdd:cd14033   44 RQRFSEEVEMLKGLQHPNIVRFYDSWKStvrgHKCIILVTELMTSGTLKTYLKRFREMKLKLLQRWSRQILKGLHFLHsR 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 185 DKHIIHRDLKPSNLLINH-RGEVKITDFGVSTVmtNTAGLANTFVGTYNYMSPErIVGNKYGNKSDIWSLGLVVLECATG 263
Cdd:cd14033  124 CPPILHRDLKCDNIFITGpTGSVKIGDLGLATL--KRASFAKSVIGTPEFMAPE-MYEEKYDEAVDVYAFGMCILEMATS 200
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 567218350 264 KFPYlppdqeETWSSVFELMEAIVDQPPPALPSENFSPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14033  201 EYPY------SECQNAAQIYRKVTSGIKPDSFYKVKVPELKEIIEGCIRTDKDERFTIQDLLEHRFF 261
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
57-321 3.38e-25

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 107.13  E-value: 3.38e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350   57 PIKPADDELSLSDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQL-NIDEAIRKSIAQELKINQSSQCPYLVNSYQSF 135
Cdd:PTZ00266    2 PGKYDDGESRLNEYEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISYrGLKEREKSQLVIEVNVMRELKHKNIVRYIDRF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  136 YD--NGAISLILEYMDGGSLADFL----KSVKTIPESYLSAIFKQVLQGLIYLHHDK------HIIHRDLKPSNLL---- 199
Cdd:PTZ00266   82 LNkaNQKLYILMEFCDAGDLSRNIqkcyKMFGKIEEHAIVDITRQLLHALAYCHNLKdgpngeRVLHRDLKPQNIFlstg 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  200 INHRGEV-------------KITDFGVSTVMtNTAGLANTFVGTYNYMSPERIV--GNKYGNKSDIWSLGLVVLECATGK 264
Cdd:PTZ00266  162 IRHIGKItaqannlngrpiaKIGDFGLSKNI-GIESMAHSCVGTPYYWSPELLLheTKSYDDKSDMWALGCIIYELCSGK 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 567218350  265 FPYlppDQEETWSSVF-ELMEAivdqppPALPSENFSPELSSFISTCLQKDPNSRSSA 321
Cdd:PTZ00266  241 TPF---HKANNFSQLIsELKRG------PDLPIKGKSKELNILIKNLLNLSAKERPSA 289
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
74-334 3.74e-25

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: 103.73  E-value: 3.74e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVIQLNI---DEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDG 150
Cdd:cd05591    1 KVLGKGSFGKVMLAERKGTDEVYAIKVLKKDVilqDDDVDCTMTEKRILALAAKHPFLTALHSCFQTKDRLFFVMEYVNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 151 GSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhdKH-IIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVG 229
Cdd:cd05591   81 GDLMFQIQRARKFDEPRARFYAAEVTLALMFLH--RHgVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGKTTTTFCG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 230 TYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYlPPDQEEtwssvfELMEAIV--DQPPPALpsenFSPELSSFI 307
Cdd:cd05591  159 TPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPF-EADNED------DLFESILhdDVLYPVW----LSKEAVSIL 227
                        250       260       270
                 ....*....|....*....|....*....|....
gi 567218350 308 STCLQKDPNSR-------SSAKELMEHPFLNKYN 334
Cdd:cd05591  228 KAFMTKNPAKRlgcvasqGGEDAIRQHPFFREID 261
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
76-330 4.05e-25

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


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 102.03  E-value: 4.05e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLN-IDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLA 154
Cdd:cd14075   10 LGSGNFSQVKLGIHQLTKEKVAIKILDKTkLDQKTQRLLSREISSMEKLHHPNIIRLYEVVETLSKLHLVMEYASGGELY 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 155 DFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLaNTFVGTYNYM 234
Cdd:cd14075   90 TKISTEGKLSESEAKPLFAQIVSAVKHMH-ENNIIHRDLKAENVFYASNNCVKVGDFGFSTHAKRGETL-NTFCGSPPYA 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 235 SPERIVGNKY-GNKSDIWSLGLVVLECATGKFPYlppdQEETwssVFELMEAIVD---QPPPALpsenfSPELSSFISTC 310
Cdd:cd14075  168 APELFKDEHYiGIYVDIWALGVLLYFMVTGVMPF----RAET---VAKLKKCILEgtyTIPSYV-----SEPCQELIRGI 235
                        250       260
                 ....*....|....*....|
gi 567218350 311 LQKDPNSRSSAKELMEHPFL 330
Cdd:cd14075  236 LQPVPSDRYSIDEIKNSEWL 255
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
69-295 4.93e-25

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: 104.35  E-value: 4.93e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  69 DLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLN--IDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILE 146
Cdd:cd05628    2 DFESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKAdmLEKEQVGHIRAERDILVEADSLWVVKMFYSFQDKLNLYLIME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 147 YMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMT-------- 218
Cdd:cd05628   82 FLPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQ-LGFIHRDIKPDNLLLDSKGHVKLSDFGLCTGLKkahrtefy 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 219 ---------------------------NTAGLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPD 271
Cdd:cd05628  161 rnlnhslpsdftfqnmnskrkaetwkrNRRQLAFSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSET 240
                        250       260
                 ....*....|....*....|....
gi 567218350 272 QEETWSSVFELMEAIVDqpPPALP 295
Cdd:cd05628  241 PQETYKKVMNWKETLIF--PPEVP 262
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
74-334 5.25e-25

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: 103.13  E-value: 5.25e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVIQlniDEAIRKSIAQELKINQSS-----QCPYLVNSYQSFYDNGAISLILEYM 148
Cdd:cd05632    8 RVLGKGGFGEVCACQVRATGKMYACKRLE---KKRIKKRKGESMALNEKQilekvNSQFVVNLAYAYETKDALCLVLTIM 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 149 DGGSLADFLKSVKTIPESYLSAIF--KQVLQGLIYLHHDkHIIHRDLKPSNLLINHRGEVKITDFGVStVMTNTAGLANT 226
Cdd:cd05632   85 NGGDLKFHIYNMGNPGFEEERALFyaAEILCGLEDLHRE-NTVYRDLKPENILLDDYGHIRISDLGLA-VKIPEGESIRG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 227 FVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQ----EETWSSVFELMEAIvdqpppalpSENFSPE 302
Cdd:cd05632  163 RVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEkvkrEEVDRRVLETEEVY---------SAKFSEE 233
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 567218350 303 LSSFISTCLQKDPNSR-----SSAKELMEHPFLNKYN 334
Cdd:cd05632  234 AKSICKMLLTKDPKQRlgcqeEGAGEVKRHPFFRNMN 270
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
79-329 5.46e-25

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: 102.69  E-value: 5.46e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  79 GSSGVVQLVQHKWTGQFFALKviQLNIDE--------AIRksiaqELKINQSSQCPYLVNSYQ----SFYDNgaISLILE 146
Cdd:cd07843   16 GTYGVVYRARDKKTGEIVALK--KLKMEKekegfpitSLR-----EINILLKLQHPNIVTVKEvvvgSNLDK--IYMVME 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 147 YMDGGsladfLKSV-KTIPESYLSA----IFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFgvstvmtnta 221
Cdd:cd07843   87 YVEHD-----LKSLmETMKQPFLQSevkcLMLQLLSGVAHLH-DNWILHRDLKTSNLLLNNRGILKICDF---------- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 222 GLANTF----------VGTYNYMSPERIVGNK-YGNKSDIWSLGLVVLECATGKfPYLPP----DQ------------EE 274
Cdd:cd07843  151 GLAREYgsplkpytqlVVTLWYRAPELLLGAKeYSTAIDMWSVGCIFAELLTKK-PLFPGkseiDQlnkifkllgtptEK 229
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 567218350 275 TWSSVFELMEA---IVDQPPPALPSENFsPELS------SFISTCLQKDPNSRSSAKELMEHPF 329
Cdd:cd07843  230 IWPGFSELPGAkkkTFTKYPYNQLRKKF-PALSlsdngfDLLNRLLTYDPAKRISAEDALKHPY 292
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
74-331 6.13e-25

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: 102.00  E-value: 6.13e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSL 153
Cdd:cd14183   12 RTIGDGNFAVVKECVERSTGREYALKIINKSKCRGKEHMIQNEVSILRRVKHPNIVLLIEEMDMPTELYLVMELVKGGDL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 154 ADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGE----VKITDFGVSTVMTntaGLANTFVG 229
Cdd:cd14183   92 FDAITSTNKYTERDASGMLYNLASAIKYLH-SLNIVHRDIKPENLLVYEHQDgsksLKLGDFGLATVVD---GPLYTVCG 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 230 TYNYMSPERIVGNKYGNKSDIWSLGLV--VLECATGKFPYLPPDQEETWSsvfELMEAIVDQPPPALpsENFSPELSSFI 307
Cdd:cd14183  168 TPTYVAPEIIAETGYGLKVDIWAAGVItyILLCGFPPFRGSGDDQEVLFD---QILMGQVDFPSPYW--DNVSDSAKELI 242
                        250       260
                 ....*....|....*....|....
gi 567218350 308 STCLQKDPNSRSSAKELMEHPFLN 331
Cdd:cd14183  243 TMMLQVDVDQRYSALQVLEHPWVN 266
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
76-329 6.74e-25

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Kalirin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kalirin, also called Duo or Duet, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. As a GEF, it activates Rac1, RhoA, and RhoG. It is highly expressed in neurons and is required for spine formation. The kalirin gene produces at least 10 isoforms from alternative promoter use and splicing. Of the major isoforms (Kalirin-7, -9, and -12), only kalirin-12 contains the C-terminal kinase domain. Kalirin-12 is highly expressed during embryonic development and it plays an important role in axon outgrowth. The Kalirin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 101.58  E-value: 6.74e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEaiRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLAD 155
Cdd:cd14115    1 IGRGRFSIVKKCLHKATRKDVAVKFVSKKMKK--KEQAAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRLLD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 156 FLKSVKTIPESYLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLINHR---GEVKITDFGvSTVMTNTAGLANTFVGTYN 232
Cdd:cd14115   79 YLMNHDELMEEKVAFYIRDIMEALQYLHNCR-VAHLDIKPENLLIDLRipvPRVKLIDLE-DAVQISGHRHVHHLLGNPE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 233 YMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFELmeaivdqpPPALPSENF---SPELSSFIST 309
Cdd:cd14115  157 FAAPEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRV--------DFSFPDEYFgdvSQAARDFINV 228
                        250       260
                 ....*....|....*....|
gi 567218350 310 CLQKDPNSRSSAKELMEHPF 329
Cdd:cd14115  229 ILQEDPRRRPTAATCLQHPW 248
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
63-330 6.95e-25

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: 101.92  E-value: 6.95e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  63 DELSLSDLDMvkfLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAiRKSIAQELKINQSSQCPYLVNSYQSFYDNGAIS 142
Cdd:cd14190    2 STFSIHSKEV---LGGGKFGKVHTCTEKRTGLKLAAKVINKQNSKD-KEMVLLEIQVMNQLNHRNLIQLYEAIETPNEIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 143 LILEYMDGGSLADflksvKTIPESY-LSAI-----FKQVLQGLIYLHHdKHIIHRDLKPSN-LLINHRG-EVKITDFGVS 214
Cdd:cd14190   78 LFMEYVEGGELFE-----RIVDEDYhLTEVdamvfVRQICEGIQFMHQ-MRVLHLDLKPENiLCVNRTGhQVKIIDFGLA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 215 TVMTNTAGLANTFvGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVF--------ELMEAI 286
Cdd:cd14190  152 RRYNPREKLKVNF-GTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLNNVLmgnwyfdeETFEHV 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 567218350 287 vdqpppalpsenfSPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14190  231 -------------SDEAKDFVSNLIIKERSARMSATQCLKHPWL 261
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
143-327 7.07e-25

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: 101.03  E-value: 7.07e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 143 LILEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAg 222
Cdd:cd14059   58 ILMEYCPYGQLYEVLRAGREITPSLLVDWSKQIASGMNYLHLHK-IIHRDLKSPNVLVTYNDVLKISDFGTSKELSEKS- 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 223 LANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDqeetwSSvfelmeAI---VDQPPPALPSENF 299
Cdd:cd14059  136 TKMSFAGTVAWMAPEVIRNEPCSEKVDIWSFGVVLWELLTGEIPYKDVD-----SS------AIiwgVGSNSLQLPVPST 204
                        170       180
                 ....*....|....*....|....*....
gi 567218350 300 SPE-LSSFISTCLQKDPNSRSSAKELMEH 327
Cdd:cd14059  205 CPDgFKLLMKQCWNSKPRNRPSFRQILMH 233
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
70-324 7.15e-25

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: 102.07  E-value: 7.15e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  70 LDMVKFLGKGSSGVVQLVQHKW----TGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAIS--L 143
Cdd:cd05038    6 LKFIKQLGEGHFGSVELCRYDPlgdnTGEQVAVKSLQPSGEEQHMSDFKREIEILRTLDHEYIVKYKGVCESPGRRSlrL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 144 ILEYMDGGSLADFLKSVK-TIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMT---- 218
Cdd:cd05038   86 IMEYLPSGSLRDYLQRHRdQIDLKRLLLFASQICKGMEYLG-SQRYIHRDLAARNILVESEDLVKISDFGLAKVLPedke 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 219 ----NTAGLANTFvgtynYMSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPYLPPDQ-------EETWSSVFELMEAI 286
Cdd:cd05038  165 yyyvKEPGESPIF-----WYAPECLRESRFSSASDVWSFGVTLYELFTyGDPSQSPPALflrmigiAQGQMIVTRLLELL 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 567218350 287 VDQ----PPPALPSENFspelsSFISTCLQKDPNSRSSAKEL 324
Cdd:cd05038  240 KSGerlpRPPSCPDEVY-----DLMKECWEYEPQDRPSFSDL 276
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
75-329 8.82e-25

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: 102.11  E-value: 8.82e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  75 FLGKGSSGVVQLVQHKWTGQFFALKVIQlNIDEAIRKSIAQELKI-NQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSL 153
Cdd:cd14090    9 LLGEGAYASVQTCINLYTGKEYAVKIIE-KHPGHSRSRVFREVETlHQCQGHPNILQLIEYFEDDERFYLVFEKMRGGPL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 154 ADFLKSVKTIPESYLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLINHRGE---VKITDF----GVSTVMTNTAGLAN- 225
Cdd:cd14090   88 LSHIEKRVHFTEQEASLVVRDIASALDFLHD-KGIAHRDLKPENILCESMDKvspVKICDFdlgsGIKLSSTSMTPVTTp 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 226 ---TFVGTYNYMSPERI---VGN--KYGNKSDIWSLGLVVLECATGKFPYLPP-------DQEETWSSVFELMEAIVDQP 290
Cdd:cd14090  167 ellTPVGSAEYMAPEVVdafVGEalSYDKRCDLWSLGVILYIMLCGYPPFYGRcgedcgwDRGEACQDCQELLFHSIQEG 246
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 567218350 291 PPALPSENF---SPELSSFISTCLQKDPNSRSSAKELMEHPF 329
Cdd:cd14090  247 EYEFPEKEWshiSAEAKDLISHLLVRDASQRYTAEQVLQHPW 288
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
68-334 1.11e-24

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: 102.39  E-value: 1.11e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  68 SDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNiDEAIRKSIAQ---ELKINQSSQCPYLVNSYQSFYDNGAISLI 144
Cdd:cd05601    1 KDFEVKNVIGRGHFGEVQVVKEKATGDIYAMKVLKKS-ETLAQEEVSFfeeERDIMAKANSPWITKLQYAFQDSENLYLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 145 LEYMDGGSLADFL-KSVKTIPES----YLSAIfkqVLQglIYLHHDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMT- 218
Cdd:cd05601   80 MEYHPGGDLLSLLsRYDDIFEESmarfYLAEL---VLA--IHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSAAKLSs 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 219 NTAGLANTFVGTYNYMSPE------RIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFELMEAIvdqppp 292
Cdd:cd05601  155 DKTVTSKMPVGTPDYIAPEvltsmnGGSKGTYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIMNFKKFL------ 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 567218350 293 ALPSE-NFSPELSSFISTCLQkDPNSRSSAKELMEHPFLNKYN 334
Cdd:cd05601  229 KFPEDpKVSESAVDLIKGLLT-DAKERLGYEGLCCHPFFSGID 270
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
76-330 1.16e-24

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: 101.74  E-value: 1.16e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGS-SGVVQLVQHKWTGQFFALKVIQ------LNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYM 148
Cdd:cd14096    9 IGEGAfSNVYKAVPLRNTGKPVAIKVVRkadlssDNLKGSSRANILKEVQIMKRLSHPNIVKLLDFQESDEYYYIVLELA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 149 DGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLIN--------HR----------------- 203
Cdd:cd14096   89 DGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLH-EIGVVHRDIKPENLLFEpipfipsiVKlrkadddetkvdegefi 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 204 --------GEVKITDFGVSTVMTNTAglANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGkFPYLPPDQEET 275
Cdd:cd14096  168 pgvggggiGIVKLADFGLSKQVWDSN--TKTPCGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCG-FPPFYDESIET 244
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 567218350 276 wssvfeLMEAIVDQPPPALPS--ENFSPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14096  245 ------LTEKISRGDYTFLSPwwDEISKSAKDLISHLLTVDPAKRYDIDEFLAHPWI 295
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
76-278 1.30e-24

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: 101.58  E-value: 1.30e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNS------YQSFYDNGAISLILEYMD 149
Cdd:cd14038    2 LGTGGFGNVLRWINQETGEQVAIKQCRQELSPKNRERWCLEIQIMKRLNHPNVVAArdvpegLQKLAPNDLPLLAMEYCQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 150 GGSLADFLKSVKT---IPESYLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLInHRGEV----KITDFGVSTVMtNTAG 222
Cdd:cd14038   82 GGDLRKYLNQFENccgLREGAILTLLSDISSALRYLHENR-IIHRDLKPENIVL-QQGEQrlihKIIDLGYAKEL-DQGS 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 567218350 223 LANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSS 278
Cdd:cd14038  159 LCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPFLPNWQPVQWHG 214
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
73-336 1.43e-24

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: 103.17  E-value: 1.43e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  73 VKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNiDEAIRKSIAQ---ELKINQSSQCPYLVNSYQSFYDNGAISLILEYMD 149
Cdd:cd05626    6 IKTLGIGAFGEVCLACKVDTHALYAMKTLRKK-DVLNRNQVAHvkaERDILAEADNEWVVKLYYSFQDKDNLYFVMDYIP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 150 GGSLADFLKSVKTIPEsYLSAIFKQVLQGLIYLHHDKHIIHRDLKPSNLLINHRGEVKITDFGVST-------------- 215
Cdd:cd05626   85 GGDMMSLLIRMEVFPE-VLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLCTgfrwthnskyyqkg 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 216 -------------------------VMT--------NTAGLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECAT 262
Cdd:cd05626  164 shirqdsmepsdlwddvsncrcgdrLKTleqratkqHQRCLAHSLVGTPNYIAPEVLLRKGYTQLCDWWSVGVILFEMLV 243
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 567218350 263 GKFPYLPPDQEETWSSVFELMEAIvdQPPPALpseNFSPELSSFIST--CLQKDPNSRSSAKELMEHPFLNKYNNS 336
Cdd:cd05626  244 GQPPFLAPTPTETQLKVINWENTL--HIPPQV---KLSPEAVDLITKlcCSAEERLGRNGADDIKAHPFFSEVDFS 314
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
79-326 1.49e-24

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: 100.83  E-value: 1.49e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  79 GSSGVVQLVQHKWTGQFFALKVIQLNIDEAIR---KSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLAD 155
Cdd:cd14148    3 GVGGFGKVYKGLWRGEEVAVKAARQDPDEDIAvtaENVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEYARGGALNR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 156 FLKSvKTIPESYLSAIFKQVLQGLIYLHHDK--HIIHRDLKPSNLLINHRGE--------VKITDFGVSTVMTNTAGLAN 225
Cdd:cd14148   83 ALAG-KKVPPHVLVNWAVQIARGMNYLHNEAivPIIHRDLKSSNILILEPIEnddlsgktLKITDFGLAREWHKTTKMSA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 226 TfvGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVfeLMEAIvdqpppALPSENFSPE-LS 304
Cdd:cd14148  162 A--GTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYREIDALAVAYGV--AMNKL------TLPIPSTCPEpFA 231
                        250       260
                 ....*....|....*....|..
gi 567218350 305 SFISTCLQKDPNSRSSAKELME 326
Cdd:cd14148  232 RLLEECWDPDPHGRPDFGSILK 253
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
76-278 1.74e-24

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: 101.15  E-value: 1.74e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQ-----SFYDNGAISLILEYMDG 150
Cdd:cd14039    1 LGTGGFGNVCLYQNQETGEKIAIKSCRLELSVKNKDRWCHEIQIMKKLNHPNVVKACDvpeemNFLVNDVPLLAMEYCSG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 151 GSLADFLKSVKT---IPESYLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEV---KITDFGVSTVMtNTAGLA 224
Cdd:cd14039   81 GDLRKLLNKPENccgLKESQVLSLLSDIGSGIQYLHENK-IIHRDLKPENIVLQEINGKivhKIIDLGYAKDL-DQGSLC 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 567218350 225 NTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSS 278
Cdd:cd14039  159 TSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPFLHNLQPFTWHE 212
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
76-330 1.75e-24

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


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 101.24  E-value: 1.75e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIqlnidEAIRKSIAQELKIN-QSSQCPYLVnSYQSFYDNGA-ISLILEYMDGGSL 153
Cdd:cd14178   11 IGIGSYSVCKRCVHKATSTEYAVKII-----DKSKRDPSEEIEILlRYGQHPNII-TLKDVYDDGKfVYLVMELMRGGEL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 154 ADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLL-INHRGE---VKITDFGVSTVMTNTAGLANTFVG 229
Cdd:cd14178   85 LDRILRQKCFSEREASAVLCTITKTVEYLH-SQGVVHRDLKPSNILyMDESGNpesIRICDFGFAKQLRAENGLLMTPCY 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 230 TYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYL--PPDQEEtwssvfELMeAIVDQPPPALPSENF---SPELS 304
Cdd:cd14178  164 TANFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPFAngPDDTPE------EIL-ARIGSGKYALSGGNWdsiSDAAK 236
                        250       260
                 ....*....|....*....|....*.
gi 567218350 305 SFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14178  237 DIVSKMLHVDPHQRLTAPQVLRHPWI 262
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
76-330 2.23e-24

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: 100.32  E-value: 2.23e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIqlNIDEA---IRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGS 152
Cdd:cd14097    9 LGQGSFGVVIEATHKETQTKWAIKKI--NREKAgssAVKLLEREVDILKHVNHAHIIHLEEVFETPKRMYLVMELCEDGE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 153 LADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLI-------NHRGEVKITDFGVSTV-MTNTAGLA 224
Cdd:cd14097   87 LKELLLRKGFFSENETRHIIQSLASAVAYLH-KNDIVHRDLKLENILVkssiidnNDKLNIKVTDFGLSVQkYGLGEDML 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 225 NTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEetwssvfELMEAIV--DQPPPALPSENFSPE 302
Cdd:cd14097  166 QETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEE-------KLFEEIRkgDLTFTQSVWQSVSDA 238
                        250       260
                 ....*....|....*....|....*...
gi 567218350 303 LSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14097  239 AKNVLQQLLKVDPAHRMTASELLDNPWI 266
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
65-353 2.39e-24

Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-alpha is expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 102.79  E-value: 2.39e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  65 LSLSDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKViqLNIDEAIRKS----IAQELKINQSSQCPYLVNSYQSFYDNGA 140
Cdd:cd05623   69 LHKEDFEILKVIGRGAFGEVAVVKLKNADKVFAMKI--LNKWEMLKRAetacFREERDVLVNGDSQWITTLHYAFQDDNN 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 141 ISLILEYMDGGSLADFLKSVKT-IPESYLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLINHRGEVKITDFGVS-TVMT 218
Cdd:cd05623  147 LYLVMDYYVGGDLLTLLSKFEDrLPEDMARFYLAEMVLAIDSVHQ-LHYVHRDIKPDNILMDMNGHIRLADFGSClKLME 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 219 NTAGLANTFVGTYNYMSPERIVG-----NKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFELMEAIvdQPPPA 293
Cdd:cd05623  226 DGTVQSSVAVGTPDYISPEILQAmedgkGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKERF--QFPTQ 303
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 567218350 294 LP--SENFSPELSSFIstCLQKDPNSRSSAKELMEHPFLN--KYNNSEINLASYFTDAGSPLAT 353
Cdd:cd05623  304 VTdvSENAKDLIRRLI--CSREHRLGQNGIEDFKNHPFFVgiDWDNIRNCEAPYIPEVSSPTDT 365
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
74-332 2.53e-24

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


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 101.26  E-value: 2.53e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVIQlNIDEAIRksiaqELKIN-QSSQCPYLV---NSYQSFYDN-GAISLILEYM 148
Cdd:cd14170    8 QVLGLGINGKVLQIFNKRTQEKFALKMLQ-DCPKARR-----EVELHwRASQCPHIVrivDVYENLYAGrKCLLIVMECL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 149 DGGSLADFL--KSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHR---GEVKITDFGVSTVMTNTAGL 223
Cdd:cd14170   82 DGGELFSRIqdRGDQAFTEREASEIMKSIGEAIQYLH-SINIAHRDVKPENLLYTSKrpnAILKLTDFGFAKETTSHNSL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 224 ANTFVGTYnYMSPERIVGNKYGNKSDIWSLGLV--VLECAtgkfpyLPPDQEETWSSVFELMEAIVDQPPPALPSENFSP 301
Cdd:cd14170  161 TTPCYTPY-YVAPEVLGPEKYDKSCDMWSLGVImyILLCG------YPPFYSNHGLAISPGMKTRIRMGQYEFPNPEWSE 233
                        250       260       270
                 ....*....|....*....|....*....|....
gi 567218350 302 ---ELSSFISTCLQKDPNSRSSAKELMEHPFLNK 332
Cdd:cd14170  234 vseEVKMLIRNLLKTEPTQRMTITEFMNHPWIMQ 267
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
76-259 3.25e-24

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: 100.02  E-value: 3.25e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIqLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLAD 155
Cdd:cd14222    1 LGKGFFGQAIKVTHKATGKVMVMKEL-IRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTLKD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 156 FLKSVKTIPESYLSAIFKQVLQGLIYLhHDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLAN---------- 225
Cdd:cd14222   80 FLRADDPFPWQQKVSFAKGIASGMAYL-HSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEEKKKPPpdkpttkkrt 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 567218350 226 ----------TFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLE 259
Cdd:cd14222  159 lrkndrkkryTVVGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCE 202
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
76-330 3.81e-24

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


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 100.41  E-value: 3.81e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVI-------QLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSF-----YDNGAISL 143
Cdd:cd14200    8 IGKGSYGVVKLAYNESDDKYYAMKVLskkkllkQYGFPRRPPPRGSKAAQGEQAKPLAPLERVYQEIailkkLDHVNIVK 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 144 ILEYMDGGS------LADFLKS--VKTIP------ESYLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKIT 209
Cdd:cd14200   88 LIEVLDDPAednlymVFDLLRKgpVMEVPsdkpfsEDQARLYFRDIVLGIEYLHYQK-IVHRDIKPSNLLLGDDGHVKIA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 210 DFGVSTVMTNTAGLANTFVGTYNYMSPERIV--GNKYGNKS-DIWSLGLVVLECATGKFPYLPpdqeetwSSVFELMEAI 286
Cdd:cd14200  167 DFGVSNQFEGNDALLSSTAGTPAFMAPETLSdsGQSFSGKAlDVWAMGVTLYCFVYGKCPFID-------EFILALHNKI 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 567218350 287 VDQPPPALPSENFSPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14200  240 KNKPVEFPEEPEISEELKDLILKMLDKNPETRITVPEIKVHPWV 283
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
68-331 5.09e-24

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: 100.88  E-value: 5.09e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  68 SDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKViqLNIDEAIRKS----IAQELKINQSSQCPYLVNSYQSFYDNGAISL 143
Cdd:cd05597    1 DDFEILKVIGRGAFGEVAVVKLKSTEKVYAMKI--LNKWEMLKRAetacFREERDVLVNGDRRWITKLHYAFQDENYLYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 144 ILEYMDGGSLADFL-KSVKTIPES----YLSAIfkqVLQglIYLHHDKHIIHRDLKPSNLLINHRGEVKITDFGvSTVMT 218
Cdd:cd05597   79 VMDYYCGGDLLTLLsKFEDRLPEEmarfYLAEM---VLA--IDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFG-SCLKL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 219 NTAGL--ANTFVGTYNYMSPERIVGN-----KYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFELMEAIvdqpp 291
Cdd:cd05597  153 REDGTvqSSVAVGTPDYISPEILQAMedgkgRYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKEHF----- 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 567218350 292 pALPS--ENFSPELSSFIS--TCLQKDPNSRSSAKELMEHPFLN 331
Cdd:cd05597  228 -SFPDdeDDVSEEAKDLIRrlICSRERRLGQNGIDDFKKHPFFE 270
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
76-326 5.67e-24

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: 99.51  E-value: 5.67e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLnidEAIRksiAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLAD 155
Cdd:cd13991   14 IGRGSFGEVHRMEDKQTGFQCAVKKVRL---EVFR---AEELMACAGLTSPRVVPLYGAVREGPWVNIFMDLKEGGSLGQ 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 156 FLKSVKTIPESYLSAIFKQVLQGLIYLhHDKHIIHRDLKPSNLLINHRG-EVKITDFGVSTVMTNtAGLA------NTFV 228
Cdd:cd13991   88 LIKEQGCLPEDRALHYLGQALEGLEYL-HSRKILHGDVKADNVLLSSDGsDAFLCDFGHAECLDP-DGLGkslftgDYIP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 229 GTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPylppdqeetWSSVFE--LMEAIVDQPPP--ALPSeNFSPELS 304
Cdd:cd13991  166 GTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHP---------WTQYYSgpLCLKIANEPPPlrEIPP-SCAPLTA 235
                        250       260
                 ....*....|....*....|..
gi 567218350 305 SFISTCLQKDPNSRSSAKELME 326
Cdd:cd13991  236 QAIQAGLRKEPVHRASAAELRR 257
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
72-327 5.77e-24

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: 99.68  E-value: 5.77e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  72 MVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIaQELKINQSSQCPYLVNS--YQSFYDNGAIS---LILE 146
Cdd:cd13986    4 IQRLLGEGGFSFVYLVEDLSTGRLYALKKILCHSKEDVKEAM-REIENYRLFNHPNILRLldSQIVKEAGGKKevyLLLP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 147 YMDGGSLADFLK--SVK--TIPESYLSAIFKQVLQGLIYLH--HDKHIIHRDLKPSNLLINHRGEVKITDFG---VSTVM 217
Cdd:cd13986   83 YYKRGSLQDEIErrLVKgtFFPEDRILHIFLGICRGLKAMHepELVPYAHRDIKPGNVLLSEDDEPILMDLGsmnPARIE 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 218 TNTAGLANTFV------GTYNYMSPE-------RIVgnkyGNKSDIWSLGLVVLECATGKFPYlppdqEETWSSVFELME 284
Cdd:cd13986  163 IEGRREALALQdwaaehCTMPYRAPElfdvkshCTI----DEKTDIWSLGCTLYALMYGESPF-----ERIFQKGDSLAL 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 567218350 285 AIVDQ--PPPalPSENFSPELSSFISTCLQKDPNSRSSAKELMEH 327
Cdd:cd13986  234 AVLSGnySFP--DNSRYSEELHQLVKSMLVVNPAERPSIDDLLSR 276
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
65-326 6.02e-24

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: 99.18  E-value: 6.02e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  65 LSLSDLDMVKFLGKGSSGVVqlVQHKWTGQFFALKVIQLNIDEairKSIAQELKINQSSQCPYLVNSYQSFYDNGaISLI 144
Cdd:cd05083    3 LNLQKLTLGEIIGEGEFGAV--LQGEYMGQKVAVKNIKCDVTA---QAFLEETAVMTKLQHKNLVRLLGVILHNG-LYIV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 145 LEYMDGGSLADFLKSV--KTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVmtNTAG 222
Cdd:cd05083   77 MELMSKGNLVNFLRSRgrALVPVIQLLQFSLDVAEGMEYLE-SKKLVHRDLAARNILVSEDGVAKISDFGLAKV--GSMG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 223 LANTFVgTYNYMSPERIVGNKYGNKSDIWSLGLVVLEC-ATGKFPYlpPDQeetwsSVFELMEAiVDQPPPALPSENFSP 301
Cdd:cd05083  154 VDNSRL-PVKWTAPEALKNKKFSSKSDVWSYGVLLWEVfSYGRAPY--PKM-----SVKEVKEA-VEKGYRMEPPEGCPP 224
                        250       260
                 ....*....|....*....|....*
gi 567218350 302 ELSSFISTCLQKDPNSRSSAKELME 326
Cdd:cd05083  225 DVYSIMTSCWEAEPGKRPSFKKLRE 249
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
73-331 7.23e-24

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 99.51  E-value: 7.23e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  73 VKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNI-DEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMD-- 149
Cdd:PLN00009   7 VEKIGEGTYGVVYKARDRVTNETIALKKIRLEQeDEGVPSTAIREISLLKEMQHGNIVRLQDVVHSEKRLYLVFEYLDld 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 150 ----GGSLADFLKSVKTIpESYLSaifkQVLQGLIYLHHDKhIIHRDLKPSNLLINHR-GEVKITDFGVSTVMTNTAGLA 224
Cdd:PLN00009  87 lkkhMDSSPDFAKNPRLI-KTYLY----QILRGIAYCHSHR-VLHRDLKPQNLLIDRRtNALKLADFGLARAFGIPVRTF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 225 NTFVGTYNYMSPERIVGNK-YGNKSDIWSLGLVVLECATGKfPYLPPDQ----------------EETW---SSVFELME 284
Cdd:PLN00009 161 THEVVTLWYRAPEILLGSRhYSTPVDIWSVGCIFAEMVNQK-PLFPGDSeidelfkifrilgtpnEETWpgvTSLPDYKS 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 567218350 285 AIVDQPPPALPS--ENFSPELSSFISTCLQKDPNSRSSAKELMEHPFLN 331
Cdd:PLN00009 240 AFPKWPPKDLATvvPTLEPAGVDLLSKMLRLDPSKRITARAALEHEYFK 288
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
76-329 8.06e-24

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: 99.11  E-value: 8.06e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLAD 155
Cdd:cd14027    1 LDSGGFGKVSLCFHRTQGLVVLKTVYTGPNCIEHNEALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNLMH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 156 FLKSVkTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTV-----MTN--------TAG 222
Cdd:cd14027   81 VLKKV-SVPLSVKGRIILEIIEGMAYLH-GKGVIHKDLKPENILVDNDFHIKIADLGLASFkmwskLTKeehneqreVDG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 223 LANTFVGTYNYMSPERI--VGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEEtwssvfELMEAIV--DQPPPALPSEN 298
Cdd:cd14027  159 TAKKNAGTLYYMAPEHLndVNAKPTEKSDVYSFAIVLWAIFANKEPYENAINED------QIIMCIKsgNRPDVDDITEY 232
                        250       260       270
                 ....*....|....*....|....*....|...
gi 567218350 299 FSPELSSFISTCLQKDPNSRSSAKELMEH--PF 329
Cdd:cd14027  233 CPREIIDLMKLCWEANPEARPTFPGIEEKfrPF 265
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
76-343 8.44e-24

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: 99.05  E-value: 8.44e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKV-----IQLNIDE--AIRKSIAQELkINQSSQCPYLVNSYQSFYDNGAISLILEYM 148
Cdd:cd05606    2 IGRGGFGEVYGCRKADTGKMYAMKCldkkrIKMKQGEtlALNERIMLSL-VSTGGDCPFIVCMTYAFQTPDKLCFILDLM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 149 DGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANtfV 228
Cdd:cd05606   81 NGGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMH-NRFIVYRDLKPANILLDEHGHVRISDLGLACDFSKKKPHAS--V 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 229 GTYNYMSPERIV-GNKYGNKSDIWSLGLVVLECATGKFPYL---PPDQEEtwssvFELMEAIVDqppPALPsENFSPELS 304
Cdd:cd05606  158 GTHGYMAPEVLQkGVAYDSSADWFSLGCMLYKLLKGHSPFRqhkTKDKHE-----IDRMTLTMN---VELP-DSFSPELK 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 567218350 305 SFISTCLQKDPNSR-----SSAKELMEHPFLNKYNNSEINLASY 343
Cdd:cd05606  229 SLLEGLLQRDVSKRlgclgRGATEVKEHPFFKGVDWQQVYLQKY 272
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
76-330 9.44e-24

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: 100.09  E-value: 9.44e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNideaiRKSIAQELKIN-QSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLA 154
Cdd:cd14176   27 IGVGSYSVCKRCIHKATNMEFAVKIIDKS-----KRDPTEEIEILlRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 155 DFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLL-INHRG---EVKITDFGVSTVMTNTAGLANTFVGT 230
Cdd:cd14176  102 DKILRQKFFSEREASAVLFTITKTVEYLH-AQGVVHRDLKPSNILyVDESGnpeSIRICDFGFAKQLRAENGLLMTPCYT 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 231 YNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYL--PPDQEE-----TWSSVFELMEAIVDqpppalpseNFSPEL 303
Cdd:cd14176  181 ANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFAngPDDTPEeilarIGSGKFSLSGGYWN---------SVSDTA 251
                        250       260
                 ....*....|....*....|....*..
gi 567218350 304 SSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14176  252 KDLVSKMLHVDPHQRLTAALVLRHPWI 278
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
76-324 1.02e-23

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: 98.87  E-value: 1.02e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIqLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLAD 155
Cdd:cd14221    1 LGKGCFGQAIKVTHRETGEVMVMKEL-IRFDEETQRTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTLRG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 156 FLKSVKT-IPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVM----TNTAGLAN----- 225
Cdd:cd14221   80 IIKSMDShYPWSQRVSFAKDIASGMAYLH-SMNIIHRDLNSHNCLVRENKSVVVADFGLARLMvdekTQPEGLRSlkkpd 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 226 -----TFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLEC---ATGKFPYLPPDQEetwssvFEL-MEAIVDQ-PPPALP 295
Cdd:cd14221  159 rkkryTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEIigrVNADPDYLPRTMD------FGLnVRGFLDRyCPPNCP 232
                        250       260
                 ....*....|....*....|....*....
gi 567218350 296 senfsPELSSFISTCLQKDPNSRSSAKEL 324
Cdd:cd14221  233 -----PSFFPIAVLCCDLDPEKRPSFSKL 256
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
76-330 1.06e-23

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: 98.81  E-value: 1.06e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLAD 155
Cdd:cd14169   11 LGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKEAMVENEIAVLRRINHENIVSLEDIYESPTHLYLAMELVTGGELFD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 156 FLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLIN---HRGEVKITDFGVSTVmtNTAGLANTFVGTYN 232
Cdd:cd14169   91 RIIERGSYTEKDASQLIGQVLQAVKYLH-QLGIVHRDLKPENLLYAtpfEDSKIMISDFGLSKI--EAQGMLSTACGTPG 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 233 YMSPERIVGNKYGNKSDIWSLGLV--VLECAtgkfpyLPPDQEETWSSVFELM---EAIVDQPppalPSENFSPELSSFI 307
Cdd:cd14169  168 YVAPELLEQKPYGKAVDVWAIGVIsyILLCG------YPPFYDENDSELFNQIlkaEYEFDSP----YWDDISESAKDFI 237
                        250       260
                 ....*....|....*....|...
gi 567218350 308 STCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14169  238 RHLLERDPEKRFTCEQALQHPWI 260
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
76-259 1.28e-23

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: 98.35  E-value: 1.28e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIqLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLAD 155
Cdd:cd14154    1 LGKGFFGQAIKVTHRETGEVMVMKEL-IRFDEEAQRNFLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGGTLKD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 156 FLKSV-KTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTV----------MTNTAGLA 224
Cdd:cd14154   80 VLKDMaRPLPWAQRVRFAKDIASGMAYLH-SMNIIHRDLNSHNCLVREDKTVVVADFGLARLiveerlpsgnMSPSETLR 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 567218350 225 N----------TFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLE 259
Cdd:cd14154  159 HlkspdrkkryTVVGNPYWMAPEMLNGRSYDEKVDIFSFGIVLCE 203
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
74-334 1.53e-23

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: 98.80  E-value: 1.53e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKviQLNIDEAIRKSIAQ----ELKINQSSQCPYLVNSYQSFYDNGAISLILEYMD 149
Cdd:cd05608    7 RVLGKGGFGEVSACQMRATGKLYACK--KLNKKRLKKRKGYEgamvEKRILAKVHSRFIVSLAYAFQTKTDLCLVMTIMN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 150 GGSLADFLKSVKT----IPESylSAIF--KQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGL 223
Cdd:cd05608   85 GGDLRYHIYNVDEenpgFQEP--RACFytAQIISGLEHLHQRR-IIYRDLKPENVLLDDDGNVRISDLGLAVELKDGQTK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 224 ANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSsvfELMEAIVDQppPALPSENFSPEL 303
Cdd:cd05608  162 TKGYAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFRARGEKVENK---ELKQRILND--SVTYSEKFSPAS 236
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 567218350 304 SSFISTCLQKDPNSR-----SSAKELMEHPFLNKYN 334
Cdd:cd05608  237 KSICEALLAKDPEKRlgfrdGNCDGLRTHPFFRDIN 272
pknD PRK13184
serine/threonine-protein kinase PknD;
71-326 1.57e-23

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 102.16  E-value: 1.57e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  71 DMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQ--LNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYM 148
Cdd:PRK13184   5 DIIRLIGKGGMGEVYLAYDPVCSRRVALKKIRedLSENPLLKKRFLREAKIAADLIHPGIVPVYSICSDGDPVYYTMPYI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 149 DGGSLADFLKSV------------KTIPESYLSaIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFG---- 212
Cdd:PRK13184  85 EGYTLKSLLKSVwqkeslskelaeKTSVGAFLS-IFHKICATIEYVH-SKGVLHRDLKPDNILLGLFGEVVILDWGaaif 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 213 --------------VSTVMTNTAGLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEEtwss 278
Cdd:PRK13184 163 kkleeedlldidvdERNICYSSMTIPGKIVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRKKGRK---- 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 567218350 279 vFELMEAIVDqPPPALPSENFSPELSSFISTCLQKDPNSR-SSAKELME 326
Cdd:PRK13184 239 -ISYRDVILS-PIEVAPYREIPPFLSQIAMKALAVDPAERySSVQELKQ 285
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
69-325 1.73e-23

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: 97.64  E-value: 1.73e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  69 DLDMVKFLGKGSSGVVQLvqHKWTGQF-FALKVIQ---LNIDEAIrksiaQELKINQSSQCPYLVNSYQSFYDNGAISLI 144
Cdd:cd05113    5 DLTFLKELGTGQFGVVKY--GKWRGQYdVAIKMIKegsMSEDEFI-----EEAKVMMNLSHEKLVQLYGVCTKQRPIFII 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 145 LEYMDGGSLADFLKSVKTIPE-SYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTN---T 220
Cdd:cd05113   78 TEYMANGCLLNYLREMRKRFQtQQLLEMCKDVCEAMEYLE-SKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVLDdeyT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 221 AGLANTFvgTYNYMSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPYLPPDQEETWSSVFELMEAIvdqpPPALPSEnf 299
Cdd:cd05113  157 SSVGSKF--PVRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSlGKMPYERFTNSETVEHVSQGLRLY----RPHLASE-- 228
                        250       260
                 ....*....|....*....|....*.
gi 567218350 300 spELSSFISTCLQKDPNSRSSAKELM 325
Cdd:cd05113  229 --KVYTIMYSCWHEKADERPTFKILL 252
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
66-329 1.74e-23

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: 98.98  E-value: 1.74e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  66 SLSDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQL-NIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGA--IS 142
Cdd:cd07845    5 SVTEFEKLNRIGEGTYGIVYRARDTTSGEIVALKKVRMdNERDGIPISSLREITLLLNLRHPNIVELKEVVVGKHLdsIF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 143 LILEYMDGgSLADFLKSVKT-IPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTA 221
Cdd:cd07845   85 LVMEYCEQ-DLASLLDNMPTpFSESQVKCLMLQLLRGLQYLH-ENFIIHRDLKVSNLLLTDKGCLKIADFGLARTYGLPA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 222 GLANTFVGTYNYMSPERIVGNKYGNKS-DIWSLGLVVLECATGKfPYLPPDQEetwssvFELMEAIVDQppPALPSENFS 300
Cdd:cd07845  163 KPMTPKVVTLWYRAPELLLGCTTYTTAiDMWAVGCILAELLAHK-PLLPGKSE------IEQLDLIIQL--LGTPNESIW 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 567218350 301 PELS----------------------SFISTC--------LQKDPNSRSSAKELMEHPF 329
Cdd:cd07845  234 PGFSdlplvgkftlpkqpynnlkhkfPWLSEAglrllnflLMYDPKKRATAEEALESSY 292
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
70-273 1.83e-23

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: 98.53  E-value: 1.83e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  70 LDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQ-LNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYM 148
Cdd:cd07848    3 FEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFKdSEENEEVKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFEYV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 149 DGGSLaDFLKSVKT--IPESYLSAIFkQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANT 226
Cdd:cd07848   83 EKNML-ELLEEMPNgvPPEKVRSYIY-QLIKAIHWCHKND-IVHRDIKPENLLISHNDVLKLCDFGFARNLSEGSNANYT 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 567218350 227 -FVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKfPYLPPDQE 273
Cdd:cd07848  160 eYVATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQ-PLFPGESE 206
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
66-327 2.43e-23

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: 97.79  E-value: 2.43e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  66 SLSDLDMVKFLGKGSSGvvQLVQHKWTGQFFALKVIQLNIDEAIR---KSIAQELKINQSSQCPYLVNSYQSFYDNGAIS 142
Cdd:cd14147    1 SFQELRLEEVIGIGGFG--KVYRGSWRGELVAVKAARQDPDEDISvtaESVRQEARLFAMLAHPNIIALKAVCLEEPNLC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 143 LILEYMDGGSLADFLKSvKTIPESYLSAIFKQVLQGLIYLHHDK--HIIHRDLKPSNLLINHRGE--------VKITDFG 212
Cdd:cd14147   79 LVMEYAAGGPLSRALAG-RRVPPHVLVNWAVQIARGMHYLHCEAlvPVIHRDLKSNNILLLQPIEnddmehktLKITDFG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 213 VSTVMTNTAGLANTfvGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDqeeTWSSVFELMEAIVDQPPP 292
Cdd:cd14147  158 LAREWHKTTQMSAA--GTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRGID---CLAVAYGVAVNKLTLPIP 232
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 567218350 293 ALPSENFspelSSFISTCLQKDPNSRSSAKELMEH 327
Cdd:cd14147  233 STCPEPF----AQLMADCWAQDPHRRPDFASILQQ 263
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
73-337 2.47e-23

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: 98.90  E-value: 2.47e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  73 VKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIR-KSIAQELKINQSSQCPYL------------VNSYQSFYdng 139
Cdd:cd07851   20 LSPVGSGAYGQVCSAFDTKTGRKVAIKKLSRPFQSAIHaKRTYRELRLLKHMKHENViglldvftpassLEDFQDVY--- 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 140 aisLILEYMdGGSLADFLKSVKtIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGV----ST 215
Cdd:cd07851   97 ---LVTHLM-GADLNNIVKCQK-LSDDHIQFLVYQILRGLKYIH-SAGIIHRDLKPSNLAVNEDCELKILDFGLarhtDD 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 216 VMTntaglanTFVGTYNYMSPErIVGNK--YGNKSDIWSLGLVVLECATGK--FPYLPP-DQ-----EETWSSVFELMEA 285
Cdd:cd07851  171 EMT-------GYVATRWYRAPE-IMLNWmhYNQTVDIWSVGCIMAELLTGKtlFPGSDHiDQlkrimNLVGTPDEELLKK 242
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 567218350 286 IVD-------QPPPALPSENF-------SPELSSFISTCLQKDPNSRSSAKELMEHPFLNKYNNSE 337
Cdd:cd07851  243 ISSesarnyiQSLPQMPKKDFkevfsgaNPLAIDLLEKMLVLDPDKRITAAEALAHPYLAEYHDPE 308
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
73-330 3.50e-23

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: 97.73  E-value: 3.50e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  73 VKFLGKGSSGVVQLVQHKWTGQFFALKVIQL-NIDEAIRKSIAQE---LKINQSSQCPYLVNsyqsFYDNGA-------- 140
Cdd:cd07863    5 VAEIGVGAYGTVYKARDPHSGHFVALKSVRVqTNEDGLPLSTVREvalLKRLEAFDHPNIVR----LMDVCAtsrtdret 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 141 -ISLILEYMDGgSLADFLKSVKT--IPESYLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKITDFGVSTVM 217
Cdd:cd07863   81 kVTLVFEHVDQ-DLRTYLDKVPPpgLPAETIKDLMRQFLRGLDFLHANC-IVHRDLKPENILVTSGGQVKLADFGLARIY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 218 TNTAGLANTFVgTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFELMEAIVDQPPP---AL 294
Cdd:cd07863  159 SCQMALTPVVV-TLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPEDDWPrdvTL 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 567218350 295 PSENFSPELSSFISTC---------------LQKDPNSRSSAKELMEHPFL 330
Cdd:cd07863  238 PRGAFSPRGPRPVQSVvpeieesgaqlllemLTFNPHKRISAFRALQHPFF 288
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
68-333 3.75e-23

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: 98.53  E-value: 3.75e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  68 SDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVI-----QLNIDEAIRksiaqELKINQSSQCPYLVN--------SYQS 134
Cdd:cd07849    5 PRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKIspfehQTYCLRTLR-----EIKILLRFKHENIIGildiqrppTFES 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 135 FYDngaISLILEYMDggslADFLKSVKTIPESY--LSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFG 212
Cdd:cd07849   80 FKD---VYIVQELME----TDLYKLIKTQHLSNdhIQYFLYQILRGLKYIH-SANVLHRDLKPSNLLLNTNCDLKICDFG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 213 VSTVMTNTA---GLANTFVGTYNYMSPERIVGNKYGNKS-DIWSLGLVVLECATGK--FP---YL-----------PPDQ 272
Cdd:cd07849  152 LARIADPEHdhtGFLTEYVATRWYRAPEIMLNSKGYTKAiDIWSVGCILAEMLSNRplFPgkdYLhqlnlilgilgTPSQ 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 567218350 273 EETWSSVFELMEAIVDQPP--PALPSENFSPELSS----FISTCLQKDPNSRSSAKELMEHPFLNKY 333
Cdd:cd07849  232 EDLNCIISLKARNYIKSLPfkPKVPWNKLFPNADPkaldLLDKMLTFNPHKRITVEEALAHPYLEQY 298
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
76-327 4.88e-23

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: 96.41  E-value: 4.88e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNIDeaiRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLAD 155
Cdd:cd14065    1 LGKGFFGEVYKVTHRETGKVMVMKELKRFDE---QRSFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGTLEE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 156 FLKSVK-TIPESYLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLI---NHRGEVKITDFGVSTVMTNTA------GLAN 225
Cdd:cd14065   78 LLKSMDeQLPWSQRVSLAKDIASGMAYLHS-KNIIHRDLNSKNCLVreaNRGRNAVVADFGLAREMPDEKtkkpdrKKRL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 226 TFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECaTGKFP----YLPPDQEetwssvFEL-MEAIVDQPPPALPSENFS 300
Cdd:cd14065  157 TVVGSPYWMAPEMLRGESYDEKVDVFSFGIVLCEI-IGRVPadpdYLPRTMD------FGLdVRAFRTLYVPDCPPSFLP 229
                        250       260
                 ....*....|....*....|....*..
gi 567218350 301 PELSsfistCLQKDPNSRSSAKELMEH 327
Cdd:cd14065  230 LAIR-----CCQLDPEKRPSFVELEHH 251
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
110-332 6.36e-23

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: 97.04  E-value: 6.36e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 110 RKSIAQELKINQSSQCPYLVNSYQSFYD----NGAISLILEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLH-H 184
Cdd:cd14030   68 RQRFKEEAGMLKGLQHPNIVRFYDSWEStvkgKKCIVLVTELMTSGTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHtR 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 185 DKHIIHRDLKPSNLLINH-RGEVKITDFGVSTVmtNTAGLANTFVGTYNYMSPErIVGNKYGNKSDIWSLGLVVLECATG 263
Cdd:cd14030  148 TPPIIHRDLKCDNIFITGpTGSVKIGDLGLATL--KRASFAKSVIGTPEFMAPE-MYEEKYDESVDVYAFGMCMLEMATS 224
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 567218350 264 KFPYlppdqeETWSSVFELMEAIVDQPPPALPSENFSPELSSFISTCLQKDPNSRSSAKELMEHPFLNK 332
Cdd:cd14030  225 EYPY------SECQNAAQIYRRVTSGVKPASFDKVAIPEVKEIIEGCIRQNKDERYAIKDLLNHAFFQE 287
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
71-329 6.38e-23

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: 96.38  E-value: 6.38e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  71 DMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQ--LNIDEAIRKSIaqelkINQSS-QCPYLVNSYQSFYDNGAISLILEY 147
Cdd:cd14662    3 ELVKDIGSGNFGVARLMRNKETKELVAVKYIErgLKIDENVQREI-----INHRSlRHPNIIRFKEVVLTPTHLAIVMEY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 148 MDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLI--NHRGEVKITDFGVSTVMTNTAGLAN 225
Cdd:cd14662   78 AAGGELFERICNAGRFSEDEARYFFQQLISGVSYCHS-MQICHRDLKLENTLLdgSPAPRLKICDFGYSKSSVLHSQPKS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 226 TfVGTYNYMSPERIVGNKYGNK-SDIWSLGLVVLECATGKFPYLPPDQEETWSSVFELMEAIVDQPPPALpseNFSPELS 304
Cdd:cd14662  157 T-VGTPAYIAPEVLSRKEYDGKvADVWSCGVTLYVMLVGAYPFEDPDDPKNFRKTIQRIMSVQYKIPDYV---RVSQDCR 232
                        250       260
                 ....*....|....*....|....*
gi 567218350 305 SFISTCLQKDPNSRSSAKELMEHPF 329
Cdd:cd14662  233 HLLSRIFVANPAKRITIPEIKNHPW 257
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
76-329 1.07e-22

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: 96.67  E-value: 1.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALK-VIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQ------SFYDN--GAISLILE 146
Cdd:cd07865   20 IGQGTFGEVFKARHRKTGQIVALKkVLMENEKEGFPITALREIKILQLLKHENVVNLIEicrtkaTPYNRykGSIYLVFE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 147 YMDGgSLADFL--KSVK-TIPEsyLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKITDFGVS-TVMTNTAG 222
Cdd:cd07865  100 FCEH-DLAGLLsnKNVKfTLSE--IKKVMKMLLNGLYYIHRNK-ILHRDMKAANILITKDGVLKLADFGLArAFSLAKNS 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 223 LANTF---VGTYNYMSPERIVGNK-YGNKSDIWSLGLVVLECATgKFPYLPPDQE----------------ETWSSV--- 279
Cdd:cd07865  176 QPNRYtnrVVTLWYRPPELLLGERdYGPPIDMWGAGCIMAEMWT-RSPIMQGNTEqhqltlisqlcgsitpEVWPGVdkl 254
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 567218350 280 -----FELMEAIVDQPPPALPSENFSPELSSFISTCLQKDPNSRSSAKELMEHPF 329
Cdd:cd07865  255 elfkkMELPQGQKRKVKERLKPYVKDPYALDLIDKLLVLDPAKRIDADTALNHDF 309
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
76-330 1.49e-22

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: 95.63  E-value: 1.49e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHK-----WTGQFFALKVI----QLNIDEAIRksIAQELKINQSSQCPYLVNSYQSFYDNGAISLILE 146
Cdd:cd14076    9 LGEGEFGKVKLGWPLpkanhRSGVQVAIKLIrrdtQQENCQTSK--IMREINILKGLTHPNIVRLLDVLKTKKYIGIVLE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 147 YMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLINHRGEVKITDFG-VSTVMTNTAGLAN 225
Cdd:cd14076   87 FVSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHK-KGVVHRDLKLENLLLDKNRNLVITDFGfANTFDHFNGDLMS 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 226 TFVGTYNYMSPERIVGNK--YGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFELMEAIVdQPPPALPsENFSPEL 303
Cdd:cd14076  166 TSCGSPCYAAPELVVSDSmyAGRKADIWSCGVILYAMLAGYLPFDDDPHNPNGDNVPRLYRYIC-NTPLIFP-EYVTPKA 243
                        250       260
                 ....*....|....*....|....*..
gi 567218350 304 SSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14076  244 RDLLRRILVPNPRKRIRLSAIMRHAWL 270
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
76-331 2.76e-22

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: 95.29  E-value: 2.76e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNID-EAIRKSIAQELKINQS-SQCPYLVN--SYQSFYDNGA--ISLILEYMD 149
Cdd:cd07837    9 IGEGTYGKVYKARDKNTGKLVALKKTRLEMEeEGVPSTALREVSLLQMlSQSIYIVRllDVEHVEENGKplLYLVFEYLD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 150 GgSLADFLKSVK-----TIPESYLSAIFKQVLQGLIYLHhdKH-IIHRDLKPSNLLIN-HRGEVKITDFGVSTVMTNTAG 222
Cdd:cd07837   89 T-DLKKFIDSYGrgphnPLPAKTIQSFMYQLCKGVAHCH--SHgVMHRDLKPQNLLVDkQKGLLKIADLGLGRAFTIPIK 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 223 LANTFVGTYNYMSPERIVG-NKYGNKSDIWSLGLVVLECATgKFPYLPPD----------------QEETWSSVFELME- 284
Cdd:cd07837  166 SYTHEIVTLWYRAPEVLLGsTHYSTPVDMWSVGCIFAEMSR-KQPLFPGDselqqllhifrllgtpNEEVWPGVSKLRDw 244
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 567218350 285 AIVDQPPP-----ALPSenFSPELSSFISTCLQKDPNSRSSAKELMEHPFLN 331
Cdd:cd07837  245 HEYPQWKPqdlsrAVPD--LEPEGVDLLTKMLAYDPAKRISAKAALQHPYFD 294
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
74-329 3.28e-22

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


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 94.40  E-value: 3.28e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVI-QLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGS 152
Cdd:cd14082    9 EVLGSGQFGIVYGGKHRKTGRDVAIKVIdKLRFPTKQESQLRNEVAILQQLSHPGVVNLECMFETPERVFVVMEKLHGDM 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 153 LADFLKSVKT-IPESYLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLINHRG---EVKITDFGVSTVMTNTAgLANTFV 228
Cdd:cd14082   89 LEMILSSEKGrLPERITKFLVTQILVALRYLHS-KNIVHCDLKPENVLLASAEpfpQVKLCDFGFARIIGEKS-FRRSVV 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 229 GTYNYMSPErIVGNKYGNKS-DIWSLGLVVLECATGKFPYlppdQEEtwssvfelmEAIVDQPP------PALPSENFSP 301
Cdd:cd14082  167 GTPAYLAPE-VLRNKGYNRSlDMWSVGVIIYVSLSGTFPF----NED---------EDINDQIQnaafmyPPNPWKEISP 232
                        250       260
                 ....*....|....*....|....*...
gi 567218350 302 ELSSFISTCLQKDPNSRSSAKELMEHPF 329
Cdd:cd14082  233 DAIDLINNLLQVKMRKRYSVDKSLSHPW 260
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
109-326 4.05e-22

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: 94.77  E-value: 4.05e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 109 IRKSIAQELKINQSSQCPYLVnSYQSFYDNGAISLILEYMDGG-SLADFLKSVKTIPESYLSA--IFK---QVLQGLIYL 182
Cdd:cd14001   48 YQERLKEEAKILKSLNHPNIV-GFRAFTKSEDGSLCLAMEYGGkSLNDLIEERYEAGLGPFPAatILKvalSIARALEYL 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 183 HHDKHIIHRDLKPSNLLINHRGE-VKITDFGVSTVMT-NTAGLAN---TFVGTYNYMSPERIVGNK-YGNKSDIWSLGLV 256
Cdd:cd14001  127 HNEKKILHGDIKSGNVLIKGDFEsVKLCDFGVSLPLTeNLEVDSDpkaQYVGTEPWKAKEALEEGGvITDKADIFAYGLV 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 257 VLECATGKFPYLPP------DQEETWSSVFELMEAIVDQPP--PALPSENFSPELSSFI---STCLQKDPNSRSSAKELM 325
Cdd:cd14001  207 LWEMMTLSVPHLNLldieddDEDESFDEDEEDEEAYYGTLGtrPALNLGELDDSYQKVIelfYACTQEDPKDRPSAAHIV 286

                 .
gi 567218350 326 E 326
Cdd:cd14001  287 E 287
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
62-331 5.23e-22

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 95.43  E-value: 5.23e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  62 DDELSLSDLDMVKFLGKGSSGVVQLVQHKwTGQFFALKVIQLNIDEAIRKS----IAQELKINQSSQCPYLVNSYQSFYD 137
Cdd:PTZ00426  24 KNKMKYEDFNFIRTLGTGSFGRVILATYK-NEDFPPVAIKRFEKSKIIKQKqvdhVFSERKILNYINHPFCVNLYGSFKD 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 138 NGAISLILEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVM 217
Cdd:PTZ00426 103 ESYLYLVLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQ-SLNIVYRDLKPENLLLDKDGFIKMTDFGFAKVV 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 218 TNTaglANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFELMEAIvdqppPALPSE 297
Cdd:PTZ00426 182 DTR---TYTLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFYANEPLLIYQKILEGIIYF-----PKFLDN 253
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 567218350 298 NFSPELSSFISTCLQKD-PNSRSSAKELMEHPFLN 331
Cdd:PTZ00426 254 NCKHLMKKLLSHDLTKRyGNLKKGAQNVKEHPWFG 288
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
73-336 6.04e-22

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS1 functions as a tumor suppressor and is implicated in cell cycle regulation. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. Promoter methylation, loss of heterozygosity, and missense mutations targeting the LATS1 gene have also been found in human sarcomas and ovarian cancers. In addition, decreased expression of LATS1 is associated with an aggressive phenotype and poor prognosis. LATS1 induces G2 arrest and promotes cytokinesis. It may be a component of the mitotic exit network in higher eukaryotes. The LATS1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 95.88  E-value: 6.04e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  73 VKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNiDEAIRKSIAQ---ELKINQSSQCPYLVNSYQSFYDNGAISLILEYMD 149
Cdd:cd05625    6 IKTLGIGAFGEVCLARKVDTKALYATKTLRKK-DVLLRNQVAHvkaERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 150 GGSLADFLKSVKTIPESyLSAIFKQVLQGLIYLHHDKHIIHRDLKPSNLLINHRGEVKITDFGVST-------------- 215
Cdd:cd05625   85 GGDMMSLLIRMGVFPED-LARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfrwthdskyyqsg 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 216 --------VMTNTAG-------------------------LANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECAT 262
Cdd:cd05625  164 dhlrqdsmDFSNEWGdpencrcgdrlkplerraarqhqrcLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLV 243
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 567218350 263 GKFPYLPPDQEETWSSVFElMEAIVDQPPPAlpseNFSPELSSFISTcLQKDPNSR---SSAKELMEHPFLNKYNNS 336
Cdd:cd05625  244 GQPPFLAQTPLETQMKVIN-WQTSLHIPPQA----KLSPEASDLIIK-LCRGPEDRlgkNGADEIKAHPFFKTIDFS 314
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
71-330 7.31e-22

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


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 94.31  E-value: 7.31e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  71 DMVKFLGKGSSGVVQLVQHKWTGQFFALKVIqlniDEAIRKSiAQELKI-NQSSQCPYLVnSYQSFYDNGA-ISLILEYM 148
Cdd:cd14177    7 ELKEDIGVGSYSVCKRCIHRATNMEFAVKII----DKSKRDP-SEEIEIlMRYGQHPNII-TLKDVYDDGRyVYLVTELM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 149 DGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLI----NHRGEVKITDFGVSTVMTNTAGLA 224
Cdd:cd14177   81 KGGELLDRILRQKFFSEREASAVLYTITKTVDYLHC-QGVVHRDLKPSNILYmddsANADSIRICDFGFAKQLRGENGLL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 225 NTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYL--PPDQEE-----TWSSVFELMEAIVDqpppalpse 297
Cdd:cd14177  160 LTPCYTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFAngPNDTPEeillrIGSGKFSLSGGNWD--------- 230
                        250       260       270
                 ....*....|....*....|....*....|...
gi 567218350 298 NFSPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14177  231 TVSDAAKDLLSHMLHVDPHQRYTAEQVLKHSWI 263
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
67-326 8.64e-22

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: 93.73  E-value: 8.64e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  67 LSDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIqlNIDEAIRKS---IAQELKINQSSQCPYLVNSYQSFYDNGAISL 143
Cdd:cd14049    5 LNEFEEIARLGKGGYGKVYKVRNKLDGQYYAIKKI--LIKKVTKRDcmkVLREVKVLAGLQHPNIVGYHTAWMEHVQLML 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 144 -ILEYMDGGSLADFLKSVKTIPESYLSA--------------IFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRG-EVK 207
Cdd:cd14049   83 yIQMQLCELSLWDWIVERNKRPCEEEFKsapytpvdvdvttkILQQLLEGVTYIH-SMGIVHRDLKPRNIFLHGSDiHVR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 208 ITDFGV-----------STVMTNTAGLANTF-VGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECatgkFPYLPPDQEET 275
Cdd:cd14049  162 IGDFGLacpdilqdgndSTTMSRLNGLTHTSgVGTCLYAAPEQLEGSHYDFKSDMYSIGVILLEL----FQPFGTEMERA 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 567218350 276 wssvfELMEAIVDQPPPalpsENFS---PELSSFISTCLQKDPNSRSSAKELME 326
Cdd:cd14049  238 -----EVLTQLRNGQIP----KSLCkrwPVQAKYIKLLTSTEPSERPSASQLLE 282
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
76-329 9.33e-22

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: 93.94  E-value: 9.33e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSG-VVQLVQHKWTGQFFALKVIQLNI-DEAIRKSIAQE---LKINQSSQCPYLVNSYQ----SFYD-NGAISLIL 145
Cdd:cd07862    9 IGEGAYGkVFKARDLKNGGRFVALKRVRVQTgEEGMPLSTIREvavLRHLETFEHPNVVRLFDvctvSRTDrETKLTLVF 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 146 EYMDGgSLADFLKSVKT--IPESYLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGL 223
Cdd:cd07862   89 EHVDQ-DLTTYLDKVPEpgVPTETIKDMMFQLLRGLDFLHSHR-VVHRDLKPQNILVTSSGQIKLADFGLARIYSFQMAL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 224 ANTFVgTYNYMSPERIVGNKYGNKSDIWSLGLVVLEC--------------ATGK-FPYLPPDQEETWSSVFELMEAIVd 288
Cdd:cd07862  167 TSVVV-TLWYRAPEVLLQSSYATPVDLWSVGCIFAEMfrrkplfrgssdvdQLGKiLDVIGLPGEEDWPRDVALPRQAF- 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 567218350 289 QPPPALPSENFSPEL----SSFISTCLQKDPNSRSSAKELMEHPF 329
Cdd:cd07862  245 HSKSAQPIEKFVTDIdelgKDLLLKCLTFNPAKRISAYSALSHPY 289
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
74-330 1.11e-21

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


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 92.96  E-value: 1.11e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVIqlnideAIRKSIAQELKINQSSQCPYLVNSYQSFYDNG-AISLILEYMDGG- 151
Cdd:cd14109   10 EDEKRAAQGAPFHVTERSTGRNFLAQLR------YGDPFLMREVDIHNSLDHPNIVQMHDAYDDEKlAVTVIDNLASTIe 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 152 -SLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHrGEVKITDFGVSTVMtNTAGLANTFVGT 230
Cdd:cd14109   84 lVRDNLLPGKDYYTERQVAVFVRQLLLALKHMH-DLGIAHLDLRPEDILLQD-DKLKLADFGQSRRL-LRGKLTTLIYGS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 231 YNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFELMEAIVDQpppalPSENFSPELSSFISTC 310
Cdd:cd14109  161 PEFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDRETLTNVRSGKWSFDSS-----PLGNISDDARDFIKKL 235
                        250       260
                 ....*....|....*....|
gi 567218350 311 LQKDPNSRSSAKELMEHPFL 330
Cdd:cd14109  236 LVYIPESRLTVDEALNHPWF 255
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
72-333 1.53e-21

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: 94.01  E-value: 1.53e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  72 MVKFLGKGSSGVVQLVQHKWT--GQFFALKVIQlNI--DEAIRKSIAQELK-INQSSQCPYLVNSYQS---FYDN-GAIS 142
Cdd:cd07857    4 LIKELGQGAYGIVCSARNAETseEETVAIKKIT-NVfsKKILAKRALRELKlLRHFRGHKNITCLYDMdivFPGNfNELY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 143 LILEYMDGgSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGV----STVMT 218
Cdd:cd07857   83 LYEELMEA-DLHQIIRSGQPLTDAHFQSFIYQILCGLKYIH-SANVLHRDLKPGNLLVNADCELKICDFGLargfSENPG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 219 NTAGLANTFVGTYNYMSPERIVGNKYGNKS-DIWSLGLVVLECATGK---------------FPYLPPDQEETWS----- 277
Cdd:cd07857  161 ENAGFMTEYVATRWYRAPEIMLSFQSYTKAiDVWSVGCILAELLGRKpvfkgkdyvdqlnqiLQVLGTPDEETLSrigsp 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 567218350 278 SVFELMEAIVDQPPPALPS--ENFSPELSSFISTCLQKDPNSRSSAKELMEHPFLNKY 333
Cdd:cd07857  241 KAQNYIRSLPNIPKKPFESifPNANPLALDLLEKLLAFDPTKRISVEEALEHPYLAIW 298
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
141-329 1.77e-21

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: 92.04  E-value: 1.77e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 141 ISLILEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLI---NHRGEVKITDFGVSTVM 217
Cdd:cd14012   79 VYLLTEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEALEYLH-RNGVVHKSLHAGNVLLdrdAGTGIVKLTDYSLGKTL 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 218 TN--TAGLANTFVGTYnYMSPERI-VGNKYGNKSDIWSLGLVVLECATGKfpylppdqeETWSSVfelmeaivDQPPPAL 294
Cdd:cd14012  158 LDmcSRGSLDEFKQTY-WLPPELAqGSKSPTRKTDVWDLGLLFLQMLFGL---------DVLEKY--------TSPNPVL 219
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 567218350 295 PSENFSPELSSFISTCLQKDPNSRSSAKELMEHPF 329
Cdd:cd14012  220 VSLDLSASLQDFLSKCLSLDPKKRPTALELLPHEF 254
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
73-335 2.12e-21

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: 93.69  E-value: 2.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  73 VKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNiDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNG------------- 139
Cdd:cd07854   10 LRPLGCGSNGLVFSAVDSDCDKRVAVKKIVLT-DPQSVKHALREIKIIRRLDHDNIVKVYEVLGPSGsdltedvgsltel 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 140 -AISLILEYMDGgSLADFLKSvKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEV-KITDFGVSTVM 217
Cdd:cd07854   89 nSVYIVQEYMET-DLANVLEQ-GPLSEEHARLFMYQLLRGLKYIH-SANVLHRDLKPANVFINTEDLVlKIGDFGLARIV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 218 ----TNTAGLANTFVGTYnYMSPERIVG-NKYGNKSDIWSLGLVVLECATGKfPYLPPDQEetwssvFELMEAIVDQPP- 291
Cdd:cd07854  166 dphySHKGYLSEGLVTKW-YRSPRLLLSpNNYTKAIDMWAAGCIFAEMLTGK-PLFAGAHE------LEQMQLILESVPv 237
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 567218350 292 -----------------------PALPSENFSPELSS----FISTCLQKDPNSRSSAKELMEHPFLNKYNN 335
Cdd:cd07854  238 vreedrnellnvipsfvrndggePRRPLRDLLPGVNPealdFLEQILTFNPMDRLTAEEALMHPYMSCYSC 308
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
70-324 2.24e-21

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak2 is widely expressed in many tissues and is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 92.77  E-value: 2.24e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  70 LDMVKFLGKGSSGVVQLVQHKW----TGQFFALKVIQLNIDEAIRkSIAQELKINQSSQCPYLVNSYQSFYDNGA--ISL 143
Cdd:cd14205    6 LKFLQQLGKGNFGSVEMCRYDPlqdnTGEVVAVKKLQHSTEEHLR-DFEREIEILKSLQHDNIVKYKGVCYSAGRrnLRL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 144 ILEYMDGGSLADFL-KSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVM----- 217
Cdd:cd14205   85 IMEYLPYGSLRDYLqKHKERIDHIKLLQYTSQICKGMEYLG-TKRYIHRDLATRNILVENENRVKIGDFGLTKVLpqdke 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 218 ---TNTAGLANTFvgtynYMSPERIVGNKYGNKSDIWSLGLVVLECAT---------GKFPYLPPDQEETWSSVFELMEA 285
Cdd:cd14205  164 yykVKEPGESPIF-----WYAPESLTESKFSVASDVWSFGVVLYELFTyieksksppAEFMRMIGNDKQGQMIVFHLIEL 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 567218350 286 IVDQppPALPSENFSP-ELSSFISTCLQKDPNSRSSAKEL 324
Cdd:cd14205  239 LKNN--GRLPRPDGCPdEIYMIMTECWNNNVNQRPSFRDL 276
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
75-329 2.25e-21

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: 93.12  E-value: 2.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  75 FLGKGSSGVVQLVQHK--WTGQFFALKVIQLNIDEA--IRKSIAQELKINQSSQCPYLVNSYQSFYD--NGAISLILEYM 148
Cdd:cd07842    7 CIGRGTYGRVYKAKRKngKDGKEYAIKKFKGDKEQYtgISQSACREIALLRELKHENVVSLVEVFLEhaDKSVYLLFDYA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 149 DggslADFL--------KSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLI----NHRGEVKITDFGVSTV 216
Cdd:cd07842   87 E----HDLWqiikfhrqAKRVSIPPSMVKSLLWQILNGIHYLH-SNWVLHRDLKPANILVmgegPERGVVKIGDLGLARL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 217 MTN-TAGLA--NTFVGTYNYMSPERIVGNKYGNKS-DIWSLGLVVLECATGKfPYLPPDQEETWSSV----------FEL 282
Cdd:cd07842  162 FNApLKPLAdlDPVVVTIWYRAPELLLGARHYTKAiDIWAIGCIFAELLTLE-PIFKGREAKIKKSNpfqrdqleriFEV 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 567218350 283 M--------EAIVDQP--------------PPALPS------ENFSPELSSFISTCLQKDPNSRSSAKELMEHPF 329
Cdd:cd07842  241 LgtptekdwPDIKKMPeydtlksdtkastyPNSLLAkwmhkhKKPDSQGFDLLRKLLEYDPTKRITAEEALEHPY 315
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
74-330 2.26e-21

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


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 92.36  E-value: 2.26e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVIQlnidEAIRKSIAQELKInQSSQCPYLV---NSYQSFYDNGAISLI-LEYMD 149
Cdd:cd14172   10 QVLGLGVNGKVLECFHRRTGQKCALKLLY----DSPKARREVEHHW-RASGGPHIVhilDVYENMHHGKRCLLIiMECME 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 150 GGSLADFLKSV--KTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHR---GEVKITDFGVSTVMTNTAGLA 224
Cdd:cd14172   85 GGELFSRIQERgdQAFTEREASEIMRDIGTAIQYLH-SMNIAHRDVKPENLLYTSKekdAVLKLTDFGFAKETTVQNALQ 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 225 NTFVGTYnYMSPERIVGNKYGNKSDIWSLGLV--VLECAtgkfpyLPPDQEETWSSVFELMEAIVDQPPPALPSENF--- 299
Cdd:cd14172  164 TPCYTPY-YVAPEVLGPEKYDKSCDMWSLGVImyILLCG------FPPFYSNTGQAISPGMKRRIRMGQYGFPNPEWaev 236
                        250       260       270
                 ....*....|....*....|....*....|.
gi 567218350 300 SPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14172  237 SEEAKQLIRHLLKTDPTERMTITQFMNHPWI 267
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
73-332 2.26e-21

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


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 93.59  E-value: 2.26e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  73 VKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAI-RKSIAQELKINQSSQCPYLV--------NSYQSFYDngaISL 143
Cdd:cd07858   10 IKPIGRGAYGIVCSAKNSETNEKVAIKKIANAFDNRIdAKRTLREIKLLRHLDHENVIaikdimppPHREAFND---VYI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 144 ILEYMDGgSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGL 223
Cdd:cd07858   87 VYELMDT-DLHQIIRSSQTLSDDHCQYFLYQLLRGLKYIH-SANVLHRDLKPSNLLLNANCDLKICDFGLARTTSEKGDF 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 224 ANTFVGTYNYMSPERIVG-NKYGNKSDIWSLGLVVLECATGK--FP---YL-----------PPDQEETWSSVFELMEAI 286
Cdd:cd07858  165 MTEYVVTRWYRAPELLLNcSEYTTAIDVWSVGCIFAELLGRKplFPgkdYVhqlklitellgSPSEEDLGFIRNEKARRY 244
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 567218350 287 VDQPPPAlPSENFS---PELSSFISTCLQK----DPNSRSSAKELMEHPFLNK 332
Cdd:cd07858  245 IRSLPYT-PRQSFArlfPHANPLAIDLLEKmlvfDPSKRITVEEALAHPYLAS 296
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
143-266 3.11e-21

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: 91.79  E-value: 3.11e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 143 LILEYMDGGSLADFL--KSVKTIPESYLS--AIFKQVLQGLIYLHHD--KHIIHRDLKPSNLLINHRGEVKITDFGVSTV 216
Cdd:cd14664   67 LVYEYMPNGSLGELLhsRPESQPPLDWETrqRIALGSARGLAYLHHDcsPLIIHRDVKSNNILLDEEFEAHVADFGLAKL 146
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 567218350 217 MTNTAGLANTFV-GTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFP 266
Cdd:cd14664  147 MDDKDSHVMSSVaGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRP 197
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
128-333 3.53e-21

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 94.31  E-value: 3.53e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 128 LVNSYQSFYDNGAISLILEYMDGGslaDFLKSVKTIPESYLSaiFKQVLQGLIYLH--------HDKHIIHRDLKPSNLL 199
Cdd:PTZ00267 127 IVKHFDDFKSDDKLLLIMEYGSGG---DLNKQIKQRLKEHLP--FQEYEVGLLFYQivlaldevHSRKMMHRDLKSANIF 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 200 INHRGEVKITDFGVSTVMTNTAGL--ANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWS 277
Cdd:PTZ00267 202 LMPTGIIKLGDFGFSKQYSDSVSLdvASSFCGTPYYLAPELWERKRYSKKADMWSLGVILYELLTLHRPFKGPSQREIMQ 281
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 567218350 278 SVfelMEAIVDQPPPALpsenfSPELSSFISTCLQKDPNSRSSAKELMEHPFLnKY 333
Cdd:PTZ00267 282 QV---LYGKYDPFPCPV-----SSGMKALLDPLLSKNPALRPTTQQLLHTEFL-KY 328
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
75-326 4.11e-21

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: 91.29  E-value: 4.11e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  75 FLGKGSSGVVqlVQHKWTGQFFALKVIQlnideAIRKSIAQELKINQSSQCPYL-------VNSYQSFYDNGAISLIL-E 146
Cdd:cd13979   10 PLGSGGFGSV--YKATYKGETVAVKIVR-----RRRKNRASRQSFWAELNAARLrhenivrVLAAETGTDFASLGLIImE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 147 YMDGGSLADFL-KSVKTIPESYLSAIFKQVLQGLIYLHHDkHIIHRDLKPSNLLINHRGEVKITDFGVSTVM--TNTAGL 223
Cdd:cd13979   83 YCGNGTLQQLIyEGSEPLPLAHRILISLDIARALRFCHSH-GIVHLDVKPANILISEQGVCKLCDFGCSVKLgeGNEVGT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 224 -ANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLppdqeetwssvfELMEAIV------DQPPPALPS 296
Cdd:cd13979  162 pRSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYA------------GLRQHVLyavvakDLRPDLSGL 229
                        250       260       270
                 ....*....|....*....|....*....|..
gi 567218350 297 ENFSP--ELSSFISTCLQKDPNSRSSAKELME 326
Cdd:cd13979  230 EDSEFgqRLRSLISRCWSAQPAERPNADESLL 261
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
64-326 4.62e-21

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: 91.64  E-value: 4.62e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  64 ELSLSDLDMVKFLGKGSSGVVQ--LVQHKWTGQFF---ALKViqLNIDEAIRKSIA--QELKINQSSQCPYLVNSYqsfy 136
Cdd:cd05032    2 ELPREKITLIRELGQGSFGMVYegLAKGVVKGEPEtrvAIKT--VNENASMRERIEflNEASVMKEFNCHHVVRLL---- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 137 dnGAIS------LILEYMDGGSLADFLKS------------VKTIPESYLSAIfkQVLQGLIYLHhDKHIIHRDLKPSNL 198
Cdd:cd05032   76 --GVVStgqptlVVMELMAKGDLKSYLRSrrpeaennpglgPPTLQKFIQMAA--EIADGMAYLA-AKKFVHRDLAARNC 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 199 LINHRGEVKITDFGVSTVMTNT-----AGLANTFVgtyNYMSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPYLPPDQ 272
Cdd:cd05032  151 MVAEDLTVKIGDFGMTRDIYETdyyrkGGKGLLPV---RWMAPESLKDGVFTTKSDVWSFGVVLWEMATlAEQPYQGLSN 227
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 567218350 273 EEtwssVFELMEA--IVDQPppalpsENFSPELSSFISTCLQKDPNSRSSAKELME 326
Cdd:cd05032  228 EE----VLKFVIDggHLDLP------ENCPDKLLELMRMCWQYNPKMRPTFLEIVS 273
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
70-324 4.67e-21

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: 91.49  E-value: 4.67e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  70 LDMVKFLGKGSSGVVQLVQHK----WTGQFFALKVIQLNIDEAIRkSIAQELKINQSSQCPYLVNSYQSFYDNG--AISL 143
Cdd:cd05081    6 LKYISQLGKGNFGSVELCRYDplgdNTGALVAVKQLQHSGPDQQR-DFQREIQILKALHSDFIVKYRGVSYGPGrrSLRL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 144 ILEYMDGGSLADFL-KSVKTIPESYLSAIFKQVLQGLIYLHHDKHIiHRDLKPSNLLINHRGEVKITDFGVSTVM----- 217
Cdd:cd05081   85 VMEYLPSGCLRDFLqRHRARLDASRLLLYSSQICKGMEYLGSRRCV-HRDLAARNILVESEAHVKIADFGLAKLLpldkd 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 218 ---TNTAGLANTFvgtynYMSPERIVGNKYGNKSDIWSLGLVVLE----CATGKFP---YL----PPDQEETWSSVFELM 283
Cdd:cd05081  164 yyvVREPGQSPIF-----WYAPESLSDNIFSRQSDVWSFGVVLYElftyCDKSCSPsaeFLrmmgCERDVPALCRLLELL 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 567218350 284 EAIVDQP-PPALPSENFSPELSsfistCLQKDPNSRSSAKEL 324
Cdd:cd05081  239 EEGQRLPaPPACPAEVHELMKL-----CWAPSPQDRPSFSAL 275
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
74-330 4.91e-21

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


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 91.21  E-value: 4.91e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVI--QLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYD-NGAISLILEYMDG 150
Cdd:cd14163    6 KTIGEGTYSKVKEAFSKKHQRKVAIKIIdkSGGPEEFIQRFLPRELQIVERLDHKNIIHVYEMLESaDGKIYLVMELAED 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 151 GSLADFLKSVKTIPESYLSAIFKQVLQGLIYLhHDKHIIHRDLKPSNLLINHRgEVKITDFGVSTVM-TNTAGLANTFVG 229
Cdd:cd14163   86 GDVFDCVLHGGPLPEHRAKALFRQLVEAIRYC-HGCGVAHRDLKCENALLQGF-TLKLTDFGFAKQLpKGGRELSQTFCG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 230 TYNYMSPERIVGNKY-GNKSDIWSLGLV--VLECATgkfpyLPPDQEETWSSVFELMEAIvdqpppALPSE-NFSPELSS 305
Cdd:cd14163  164 STAYAAPEVLQGVPHdSRKGDIWSMGVVlyVMLCAQ-----LPFDDTDIPKMLCQQQKGV------SLPGHlGVSRTCQD 232
                        250       260
                 ....*....|....*....|....*
gi 567218350 306 FISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14163  233 LLKRLLEPDMVLRPSIEEVSWHPWL 257
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
64-320 1.01e-20

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: 90.49  E-value: 1.01e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  64 ELSLSDLDMVKFLGKGSSGVVqlvqhkWTGQF---FALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGA 140
Cdd:cd05072    3 EIPRESIKLVKKLGAGQFGEV------WMGYYnnsTKVAVKTLKPGTMSVQAFLEEANLMKTLQHDKLVRLYAVVTKEEP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 141 ISLILEYMDGGSLADFLKSVK----TIPESY-LSAifkQVLQGLIYLHHdKHIIHRDLKPSNLLINHRGEVKITDFGVST 215
Cdd:cd05072   77 IYIITEYMAKGSLLDFLKSDEggkvLLPKLIdFSA---QIAEGMAYIER-KNYIHRDLRAANVLVSESLMCKIADFGLAR 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 216 VMTN---TAGLANTFvgTYNYMSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPYlpPDQEETwssvfELMEAIvdQPP 291
Cdd:cd05072  153 VIEDneyTAREGAKF--PIKWTAPEAINFGSFTIKSDVWSFGILLYEIVTyGKIPY--PGMSNS-----DVMSAL--QRG 221
                        250       260       270
                 ....*....|....*....|....*....|
gi 567218350 292 PALPS-ENFSPELSSFISTCLQKDPNSRSS 320
Cdd:cd05072  222 YRMPRmENCPDELYDIMKTCWKEKAEERPT 251
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
64-318 1.22e-20

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: 89.95  E-value: 1.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  64 ELSLSDLDMVKFLGKGSSGVVqlvqhkWTGQFFA-LKVIQLNIDEAIRKSIA--QELKINQSSQCPYLVNSYqSFYDNGA 140
Cdd:cd05067    3 EVPRETLKLVERLGAGQFGEV------WMGYYNGhTKVAIKSLKQGSMSPDAflAEANLMKQLQHQRLVRLY-AVVTQEP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 141 ISLILEYMDGGSLADFLKSV--KTIPESYLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMT 218
Cdd:cd05067   76 IYIITEYMENGSLVDFLKTPsgIKLTINKLLDMAAQIAEGMAFIEE-RNYIHRDLRAANILVSDTLSCKIADFGLARLIE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 219 N---TAGLANTFvgTYNYMSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPYlpPDQeeTWSSVFELMEAIVDQPPPal 294
Cdd:cd05067  155 DneyTAREGAKF--PIKWTAPEAINYGTFTIKSDVWSFGILLTEIVThGRIPY--PGM--TNPEVIQNLERGYRMPRP-- 226
                        250       260
                 ....*....|....*....|....
gi 567218350 295 psENFSPELSSFISTCLQKDPNSR 318
Cdd:cd05067  227 --DNCPEELYQLMRLCWKERPEDR 248
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
76-335 1.31e-20

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: 91.09  E-value: 1.31e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNIDE-AIRKSIAQELKINQSSQCPYLVNSYQSFYDNGA-ISLILEYMdGGSL 153
Cdd:cd07856   18 VGMGAFGLVCSARDQLTGQNVAVKKIMKPFSTpVLAKRTYRELKLLKHLRHENIISLSDIFISPLEdIYFVTELL-GTDL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 154 ADFLKSvKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTV----MTNtaglantFVG 229
Cdd:cd07856   97 HRLLTS-RPLEKQFIQYFLYQILRGLKYVH-SAGVIHRDLKPSNILVNENCDLKICDFGLARIqdpqMTG-------YVS 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 230 TYNYMSPE-RIVGNKYGNKSDIWSLGLVVLECATGKfPYLP-PDQEETWSSVFELMEAIVDQPPPALPSEN--------- 298
Cdd:cd07856  168 TRYYRAPEiMLTWQKYDVEVDIWSAGCIFAEMLEGK-PLFPgKDHVNQFSIITELLGTPPDDVINTICSENtlrfvqslp 246
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 567218350 299 ------FS-------PELSSFISTCLQKDPNSRSSAKELMEHPFLNKYNN 335
Cdd:cd07856  247 krervpFSekfknadPDAIDLLEKMLVFDPKKRISAAEALAHPYLAPYHD 296
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
64-326 2.00e-20

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


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 89.33  E-value: 2.00e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  64 ELSLSDLDMVKFLGKGSSGVVqlVQHKWTGQFFALKVIQlNIDEAIRKSIAqELKINQSSQCPYLVNSYQSFYDNGAISL 143
Cdd:cd05039    2 AINKKDLKLGELIGKGEFGDV--MLGDYRGQKVAVKCLK-DDSTAAQAFLA-EASVMTTLRHPNLVQLLGVVLEGNGLYI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 144 ILEYMDGGSLADFLKS----VKTIPESYLSAIfkQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVStvmtn 219
Cdd:cd05039   78 VTEYMAKGSLVDYLRSrgraVITRKDQLGFAL--DVCEGMEYLE-SKKFVHRDLAARNVLVSEDNVAKVSDFGLA----- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 220 TAGLANTFVGTY--NYMSPERIVGNKYGNKSDIWSLGLVVLEC-ATGKFPYLPPDQEETWSSVFE--LMEAivdqpPPAL 294
Cdd:cd05039  150 KEASSNQDGGKLpiKWTAPEALREKKFSTKSDVWSFGILLWEIySFGRVPYPRIPLKDVVPHVEKgyRMEA-----PEGC 224
                        250       260       270
                 ....*....|....*....|....*....|..
gi 567218350 295 PsenfsPELSSFISTCLQKDPNSRSSAKELME 326
Cdd:cd05039  225 P-----PEVYKVMKNCWELDPAKRPTFKQLRE 251
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
74-328 2.02e-20

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: 89.96  E-value: 2.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKviQLNIDEAIRKSIAQ----ELKINQSSQCPYLVNSYQSFYDNGAISLILEYMD 149
Cdd:cd05607    8 RVLGKGGFGEVCAVQVKNTGQMYACK--KLDKKRLKKKSGEKmallEKEILEKVNSPFIVSLAYAFETKTHLCLVMSLMN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 150 GGSLADFLKSVKTIPESYLSAIF--KQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTf 227
Cdd:cd05607   86 GGDLKYHIYNVGERGIEMERVIFysAQITCGILHLHSLK-IVYRDMKPENVLLDDNGNCRLSDLGLAVEVKEGKPITQR- 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 228 VGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPP----DQEETWSSVFElmEAIVDQPPpalpseNFSPEL 303
Cdd:cd05607  164 AGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRDHkekvSKEELKRRTLE--DEVKFEHQ------NFTEEA 235
                        250       260
                 ....*....|....*....|....*
gi 567218350 304 SSFISTCLQKDPNSRSSAKELMEHP 328
Cdd:cd05607  236 KDICRLFLAKKPENRLGSRTNDDDP 260
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
76-329 2.13e-20

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: 89.64  E-value: 2.13e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNIdeairKSIAQelkINQSS--QC-------PYLVNSYQSFYDN--GAISLI 144
Cdd:cd07831    7 IGEGTFSEVLKAQSRKTGKYYAIKCMKKHF-----KSLEQ---VNNLReiQAlrrlsphPNILRLIEVLFDRktGRLALV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 145 LEYMDGgSLADFLKSVKT-IPESYLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLInHRGEVKITDFGvSTVMTNTAGL 223
Cdd:cd07831   79 FELMDM-NLYELIKGRKRpLPEKRVKNYMYQLLKSLDHMHR-NGIFHRDIKPENILI-KDDILKLADFG-SCRGIYSKPP 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 224 ANTFVGTYNYMSPERIV-GNKYGNKSDIWSLGLVVLECATgKFPYLPPDQEetwssvfelmeaiVDQ----------PPP 292
Cdd:cd07831  155 YTEYISTRWYRAPECLLtDGYYGPKMDIWAVGCVFFEILS-LFPLFPGTNE-------------LDQiakihdvlgtPDA 220
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 567218350 293 AL-----PSE----NFSPELSSFISTCLQK---------------DPNSRSSAKELMEHPF 329
Cdd:cd07831  221 EVlkkfrKSRhmnyNFPSKKGTGLRKLLPNasaegldllkkllayDPDERITAKQALRHPY 281
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
131-337 2.20e-20

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: 90.87  E-value: 2.20e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 131 SYQSFYDngaISLILEYMdGGSLADFLKSVKtIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITD 210
Cdd:cd07877   90 SLEEFND---VYLVTHLM-GADLNNIVKCQK-LTDDHVQFLIYQILRGLKYIH-SADIIHRDLKPSNLAVNEDCELKILD 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 211 FGVStvmTNTAGLANTFVGTYNYMSPERIVGNKYGNKS-DIWSLGLVVLECATGKFPYLPPDQEETWSSVF--------E 281
Cdd:cd07877  164 FGLA---RHTDDEMTGYVATRWYRAPEIMLNWMHYNQTvDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILrlvgtpgaE 240
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 282 LMEAIVD-------QPPPALPSENFS-------PELSSFISTCLQKDPNSRSSAKELMEHPFLNKYNNSE 337
Cdd:cd07877  241 LLKKISSesarnyiQSLTQMPKMNFAnvfiganPLAVDLLEKMLVLDSDKRITAAQALAHAYFAQYHDPD 310
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
68-326 2.42e-20

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: 89.40  E-value: 2.42e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  68 SDLDMVKFLGKGSSGVVqlvqHK--WTGQF------FALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYqSFYDNG 139
Cdd:cd05057    7 TELEKGKVLGSGAFGTV----YKgvWIPEGekvkipVAIKVLREETGPKANEEILDEAYVMASVDHPHLVRLL-GICLSS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 140 AISLILEYMDGGSLADFLKSVK-TIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVstvmt 218
Cdd:cd05057   82 QVQLITQLMPLGCLLDYVRNHRdNIGSQLLLNWCVQIAKGMSYLE-EKRLVHRDLAARNVLVKTPNHVKITDFGL----- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 219 ntAGLANTFVGTYNY---------MSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPYLPPDQEEtwssVFELMEAIVD 288
Cdd:cd05057  156 --AKLLDVDEKEYHAeggkvpikwMALESIQYRIYTHKSDVWSYGVTVWELMTfGAKPYEGIPAVE----IPDLLEKGER 229
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 567218350 289 QPPPALPSENfspeLSSFISTCLQKDPNSRSSAKELME 326
Cdd:cd05057  230 LPQPPICTID----VYMVLVKCWMIDAESRPTFKELAN 263
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
76-326 4.49e-20

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: 88.34  E-value: 4.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNIDeaiRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLAD 155
Cdd:cd14156    1 IGSGFFSKVYKVTHGATGKVMVVKIYKNDVD---QHKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCLEE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 156 FLKSvKTIPESYLS--AIFKQVLQGLIYLHHdKHIIHRDLKPSNLLI--NHRG-EVKITDFGVSTVM----TNTAGLANT 226
Cdd:cd14156   78 LLAR-EELPLSWREkvELACDISRGMVYLHS-KNIYHRDLNSKNCLIrvTPRGrEAVVTDFGLAREVgempANDPERKLS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 227 FVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECaTGKFPYLPPDQEETWS---SVFELMEAIVDQPPPALpsenfspEL 303
Cdd:cd14156  156 LVGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEI-LARIPADPEVLPRTGDfglDVQAFKEMVPGCPEPFL-------DL 227
                        250       260
                 ....*....|....*....|...
gi 567218350 304 SsfiSTCLQKDPNSRSSAKELME 326
Cdd:cd14156  228 A---ASCCRMDAFKRPSFAELLD 247
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
174-331 4.56e-20

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: 88.92  E-value: 4.56e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 174 QVLQGLIYLHHDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVG-----------TYNYMSPERIVGN 242
Cdd:cd14011  122 QISEALSFLHNDVKLVHGNICPESVVINSNGEWKLAGFDFCISSEQATDQFPYFREydpnlpplaqpNLNYLAPEYILSK 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 243 KYGNKSDIWSLGLVVLEC-ATGKFPYlppDQEETWSSvFELMEAIVDQPPPALpSENFSPELSSFISTCLQKDPNSRSSA 321
Cdd:cd14011  202 TCDPASDMFSLGVLIYAIyNKGKPLF---DCVNNLLS-YKKNSNQLRQLSLSL-LEKVPEELRDHVKTLLNVTPEVRPDA 276
                        170
                 ....*....|
gi 567218350 322 KELMEHPFLN 331
Cdd:cd14011  277 EQLSKIPFFD 286
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
76-330 7.05e-20

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. DYRK4 is a testis-specific kinase with restricted expression to postmeiotic spermatids. It may function during spermiogenesis, however, it is not required for male fertility. DYRK4 has also been detected in a human teratocarcinoma cell line induced to produce postmitotic neurons. It may have a role in neuronal differentiation. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. The DYRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 89.38  E-value: 7.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSG-VVQLVQHKwTGQFFALKVI------------QLNIDEAIRKSiAQELKINqssqcpyLVNSYQSFYDNGAIS 142
Cdd:cd14225   51 IGKGSFGqVVKALDHK-TNEHVAIKIIrnkkrfhhqalvEVKILDALRRK-DRDNSHN-------VIHMKEYFYFRNHLC 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 143 LILEYMdGGSLADFLK-------SVKTIPESYLSAIfkQVLQGLiylhHDKHIIHRDLKPSNLLINHRGE--VKITDFGV 213
Cdd:cd14225  122 ITFELL-GMNLYELIKknnfqgfSLSLIRRFAISLL--QCLRLL----YRERIIHCDLKPENILLRQRGQssIKVIDFGS 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 214 STvmtntagLANTFVGTY----NYMSPERIVGNKYGNKSDIWSLGLVVLECATGkFPYLPPDQE-ETWSSVFElmeaIVD 288
Cdd:cd14225  195 SC-------YEHQRVYTYiqsrFYRSPEVILGLPYSMAIDMWSLGCILAELYTG-YPLFPGENEvEQLACIME----VLG 262
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 567218350 289 QPPPAL-----------------------------PS--------ENFSPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14225  263 LPPPELienaqrrrlffdskgnprcitnskgkkrrPNskdlasalKTSDPLFLDFIRRCLEWDPSKRMTPDEALQHEWI 341
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
76-330 7.13e-20

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 5 (MAPKAP5 or MK5) is also called PRAK (p38-regulated/activated protein kinase). It contains a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 88.29  E-value: 7.13e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIqlnIDeaiRKSIAQELKINQssQC---PYLVNSYQSF----------YDNGAIS 142
Cdd:cd14171   14 LGTGISGPVRVCVKKSTGERFALKIL---LD---RPKARTEVRLHM--MCsghPNIVQIYDVYansvqfpgesSPRARLL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 143 LILEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLINHRGE---VKITDFGVSTVmtn 219
Cdd:cd14171   86 IVMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHS-LNIAHRDLKPENLLLKDNSEdapIKLCDFGFAKV--- 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 220 TAGLANTFVGTYNYMSPERIVGNKYGNKS-----------------DIWSLGLVVLECATGKFPYLP--PDQEETWSSVF 280
Cdd:cd14171  162 DQGDLMTPQFTPYYVAPQVLEAQRRHRKErsgiptsptpytydkscDMWSLGVIIYIMLCGYPPFYSehPSRTITKDMKR 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 567218350 281 ELMEAIVDqpppaLPSENF---SPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14171  242 KIMTGSYE-----FPEEEWsqiSEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
68-325 8.09e-20

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: 87.70  E-value: 8.09e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  68 SDLDMVKFLGKGSSGVVqlvqhkWTGQFFALKVIQLnidEAIRKSIAQELKINQSSQC------PYLVNSYQSFYDNGAI 141
Cdd:cd05112    4 SELTFVQEIGSGQFGLV------HLGYWLNKDKVAI---KTIREGAMSEEDFIEEAEVmmklshPKLVQLYGVCLEQAPI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 142 SLILEYMDGGSLADFLKSVK-TIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNT 220
Cdd:cd05112   75 CLVFEFMEHGCLSDYLRTQRgLFSAETLLGMCLDVCEGMAYLE-EASVIHRDLAARNCLVGENQVVKVSDFGMTRFVLDD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 221 AGLANTfvGT---YNYMSPERIVGNKYGNKSDIWSLGLVVLEC-ATGKFPYlppdQEETWSSVFELMEAIVDQPPPALPS 296
Cdd:cd05112  154 QYTSST--GTkfpVKWSSPEVFSFSRYSSKSDVWSFGVLMWEVfSEGKIPY----ENRSNSEVVEDINAGFRLYKPRLAS 227
                        250       260
                 ....*....|....*....|....*....
gi 567218350 297 ENfspeLSSFISTCLQKDPNSRSSAKELM 325
Cdd:cd05112  228 TH----VYEIMNHCWKERPEDRPSFSLLL 252
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
71-330 9.26e-20

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


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 87.26  E-value: 9.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  71 DMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEaiRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDG 150
Cdd:cd14108    5 DIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPVRAKK--KTSARRELALLAELDHKSIVRFHDAFEKRRVVIIVTELCHE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 151 GSLADFLKSvKTIPESYLSAIFKQVLQGLIYLHHDkHIIHRDLKPSNLLINHRGE--VKITDFGVSTVMTNTAGLANTFv 228
Cdd:cd14108   83 ELLERITKR-PTVCESEVRSYMRQLLEGIEYLHQN-DVLHLDLKPENLLMADQKTdqVRICDFGNAQELTPNEPQYCKY- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 229 GTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFELMEAIVDQPPPALpsenfSPELSSFIS 308
Cdd:cd14108  160 GTPEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNIRNYNVAFEESMFKDL-----CREAKGFII 234
                        250       260
                 ....*....|....*....|..
gi 567218350 309 TCLQKDpNSRSSAKELMEHPFL 330
Cdd:cd14108  235 KVLVSD-RLRPDAEETLEHPWF 255
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
153-330 1.02e-19

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


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 87.33  E-value: 1.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 153 LADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLIN-HRGEVKITDFGVSTVMTNTagLANTFVGTY 231
Cdd:cd14100   93 LFDFITERGALPEELARSFFRQVLEAVRHCH-NCGVLHRDIKDENILIDlNTGELKLIDFGSGALLKDT--VYTDFDGTR 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 232 NYMSPERIVGNKY-GNKSDIWSLGLVVLECATGKFPYlppDQEEtwssvfELMEAIVdqpppaLPSENFSPELSSFISTC 310
Cdd:cd14100  170 VYSPPEWIRFHRYhGRSAAVWSLGILLYDMVCGDIPF---EHDE------EIIRGQV------FFRQRVSSECQHLIKWC 234
                        170       180
                 ....*....|....*....|
gi 567218350 311 LQKDPNSRSSAKELMEHPFL 330
Cdd:cd14100  235 LALRPSDRPSFEDIQNHPWM 254
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
174-330 1.11e-19

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


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 89.03  E-value: 1.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 174 QVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTV--------MTNTaglantfVGTYNYMSPERIVGNK-Y 244
Cdd:cd07853  111 QILRGLKYLH-SAGILHRDIKPGNLLVNSNCVLKICDFGLARVeepdeskhMTQE-------VVTQYYRAPEILMGSRhY 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 245 GNKSDIWSLGLVVLECATGK---------------FPYL-PPDQEETWSSVFELMEAIVDQP--PPALP-----SENFSP 301
Cdd:cd07853  183 TSAVDIWSVGCIFAELLGRRilfqaqspiqqldliTDLLgTPSLEAMRSACEGARAHILRGPhkPPSLPvlytlSSQATH 262
                        170       180
                 ....*....|....*....|....*....
gi 567218350 302 ELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd07853  263 EAVHLLCRMLVFDPDKRISAADALAHPYL 291
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
171-267 1.28e-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: 87.06  E-value: 1.28e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 171 IFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGL--ANTFVGTYNYMSPERI---VGNKYG 245
Cdd:cd14062   94 IARQTAQGMDYLH-AKNIIHRDLKSNNIFLHEDLTVKIGDFGLATVKTRWSGSqqFEQPTGSILWMAPEVIrmqDENPYS 172
                         90       100
                 ....*....|....*....|..
gi 567218350 246 NKSDIWSLGLVVLECATGKFPY 267
Cdd:cd14062  173 FQSDVYAFGIVLYELLTGQLPY 194
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
74-330 1.38e-19

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


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 87.78  E-value: 1.38e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAiRKSIAQELK-INQSSQCPYLVNSYQSFYDNGAISLILEYMDGGS 152
Cdd:cd14174    8 ELLGEGAYAKVQGCVSLQNGKEYAVKIIEKNAGHS-RSRVFREVEtLYQCQGNKNILELIEFFEDDTRFYLVFEKLRGGS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 153 LADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGE---VKITDFGV-STVMTNTAGLA---- 224
Cdd:cd14174   87 ILAHIQKRKHFNEREASRVVRDIASALDFLH-TKGIAHRDLKPENILCESPDKvspVKICDFDLgSGVKLNSACTPittp 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 225 --NTFVGTYNYMSPERI-----VGNKYGNKSDIWSLGLVVLECATGKFPYLPP-------DQEETWSSVFELMEAIVDQP 290
Cdd:cd14174  166 elTTPCGSAEYMAPEVVevftdEATFYDKRCDLWSLGVILYIMLSGYPPFVGHcgtdcgwDRGEVCRVCQNKLFESIQEG 245
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 567218350 291 PPALPSENF---SPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14174  246 KYEFPDKDWshiSSEAKDLISKLLVRDAKERLSAAQVLQHPWV 288
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
76-333 1.50e-19

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: 88.19  E-value: 1.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIR-KSIAQELKINQSSQCPYLVNSYQSFYDNGAIS------LILEYM 148
Cdd:cd07855   13 IGSGAYGVVCSAIDTKSGQKVAIKKIPNAFDVVTTaKRTLRELKILRHFKHDNIIAIRDILRPKVPYAdfkdvyVVLDLM 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 149 DGgSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTF- 227
Cdd:cd07855   93 ES-DLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSAN-VIHRDLKPSNLLVNENCELKIGDFGMARGLCTSPEEHKYFm 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 228 ---VGTYNYMSPE-RIVGNKYGNKSDIWSLGLVVLEcATGKFPYLP-----------------PDQEETWSSVFELMEAI 286
Cdd:cd07855  171 teyVATRWYRAPElMLSLPEYTQAIDMWSVGCIFAE-MLGRRQLFPgknyvhqlqliltvlgtPSQAVINAIGADRVRRY 249
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 567218350 287 VDQPP--PALPSENF----SPELSSFISTCLQKDPNSRSSAKELMEHPFLNKY 333
Cdd:cd07855  250 IQNLPnkQPVPWETLypkaDQQALDLLSQMLRFDPSERITVAEALQHPFLAKY 302
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
92-326 2.30e-19

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


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 89.90  E-value: 2.30e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350    92 TGQFFALKVIQLNI--DEAIRKSIAQELKINQSSQCPYLVnsyqSFYDNGA-----ISLILEYMDGGSLADFLKSVKTIP 164
Cdd:TIGR03903    2 TGHEVAIKLLRTDApeEEHQRARFRRETALCARLYHPNIV----ALLDSGEappglLFAVFEYVPGRTLREVLAADGALP 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350   165 ESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRG---EVKITDFGVSTVMTN-------TAGLANTFVGTYNYM 234
Cdd:TIGR03903   78 AGETGRLMLQVLDALACAH-NQGIVHRDLKPQNIMVSQTGvrpHAKVLDFGIGTLLPGvrdadvaTLTRTTEVLGTPTYC 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350   235 SPERIVGNKYGNKSDIWSLGLVVLECATGKfpylppdQEETWSSVFELMEAIVDQPPPALPSENFSPELSSFISTCLQKD 314
Cdd:TIGR03903  157 APEQLRGEPVTPNSDLYAWGLIFLECLTGQ-------RVVQGASVAEILYQQLSPVDVSLPPWIAGHPLGQVLRKALNKD 229
                          250
                   ....*....|...
gi 567218350   315 PNSRS-SAKELME 326
Cdd:TIGR03903  230 PRQRAaSAPALAE 242
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
76-324 2.53e-19

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: 86.56  E-value: 2.53e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQ-HKWTGQ----FFALKVIQlNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDG 150
Cdd:cd05092   13 LGEGAFGKVFLAEcHNLLPEqdkmLVAVKALK-EATESARQDFQREAELLTVLQHQHIVRFYGVCTEGEPLIMVFEYMRH 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 151 GSLADFLKS----VKTIPE-----------SYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVST 215
Cdd:cd05092   92 GDLNRFLRShgpdAKILDGgegqapgqltlGQMLQIASQIASGMVYLA-SLHFVHRDLATRNCLVGQGLVVKIGDFGMSR 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 216 VM--TNTAGLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPYLPPDQEETWSSVFELMEAivdQPPP 292
Cdd:cd05092  171 DIysTDYYRVGGRTMLPIRWMPPESILYRKFTTESDIWSFGVVLWEIFTyGKQPWYQLSNTEAIECITQGREL---ERPR 247
                        250       260       270
                 ....*....|....*....|....*....|..
gi 567218350 293 ALPsenfsPELSSFISTCLQKDPNSRSSAKEL 324
Cdd:cd05092  248 TCP-----PEVYAIMQGCWQREPQQRHSIKDI 274
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
75-330 2.95e-19

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: 86.06  E-value: 2.95e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  75 FLGKGSSGVVqLVQHKWT-GQFFALKVIQlnideaiRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMD---- 149
Cdd:cd14101    7 LLGKGGFGTV-YAGHRISdGLQVAIKQIS-------RNRVQQWSKLPGVNPVPNEVALLQSVGGGPGHRGVIRLLDwfei 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 150 -------------GGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHR-GEVKITDFGVST 215
Cdd:cd14101   79 pegfllvlerpqhCQDLFDYITERGALDESLARRFFKQVVEAVQHCH-SKGVVHRDIKDENILVDLRtGDIKLIDFGSGA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 216 VMTNTagLANTFVGTYNYMSPERIVGNKY-GNKSDIWSLGLVVLECATGKFPYlppDQEEtwssvfELMEAIVDQPPPAl 294
Cdd:cd14101  158 TLKDS--MYTDFDGTRVYSPPEWILYHQYhALPATVWSLGILLYDMVCGDIPF---ERDT------DILKAKPSFNKRV- 225
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 567218350 295 psenfSPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14101  226 -----SNDCRSLIRSCLAYNPSDRPSLEQILLHPWM 256
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
64-329 3.58e-19

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: 85.94  E-value: 3.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  64 ELSLSDLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQ---LNIDEAIRK-SIAQELKINQSSQCPYLVNSYQSFYdng 139
Cdd:cd05052    2 EIERTDITMKHKLGGGQYGEVYEGVWKKYNLTVAVKTLKedtMEVEEFLKEaAVMKEIKHPNLVQLLGVCTREPPFY--- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 140 aisLILEYMDGGSLADFLKSV--KTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVM 217
Cdd:cd05052   79 ---IITEFMPYGNLLDYLRECnrEELNAVVLLYMATQIASAMEYLE-KKNFIHRDLAARNCLVGENHLVKVADFGLSRLM 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 218 TN---TAGLANTFvgTYNYMSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPYlpPDQEetWSSVFELMEAIVDQP-PP 292
Cdd:cd05052  155 TGdtyTAHAGAKF--PIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATyGMSPY--PGID--LSQVYELLEKGYRMErPE 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 567218350 293 ALPsenfsPELSSFISTCLQKDPNSRSSAKEL---MEHPF 329
Cdd:cd05052  229 GCP-----PKVYELMRACWQWNPSDRPSFAEIhqaLETMF 263
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
74-329 3.67e-19

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: 86.17  E-value: 3.67e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVqLVQHKWTGQFFALKVIQLN-IDEAIRksiaqELKINQSS-QCPYLVNSYQSFYDNGAISLILEYMDGg 151
Cdd:cd13982    7 KVLGYGSEGTI-VFRGTFDGRPVAVKRLLPEfFDFADR-----EVQLLRESdEHPNVIRYFCTEKDRQFLYIALELCAA- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 152 SLADFLKSVKTIPESYLSA-----IFKQVLQGLIYLHHDKhIIHRDLKPSNLLI-----NHRGEVKITDFGVS---TVMT 218
Cdd:cd13982   80 SLQDLVESPRESKLFLRPGlepvrLLRQIASGLAHLHSLN-IVHRDLKPQNILIstpnaHGNVRAMISDFGLCkklDVGR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 219 NTAGLANTFVGTYNYMSPERIVGNKYGNKS---DIWSLGLVVLECAT-GKFPYLPPDQEETwssvfELMEAIVDQPPPaL 294
Cdd:cd13982  159 SSFSRRSGVAGTSGWIAPEMLSGSTKRRQTravDIFSLGCVFYYVLSgGSHPFGDKLEREA-----NILKGKYSLDKL-L 232
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 567218350 295 PSENFSPELSSFISTCLQKDPNSRSSAKELMEHPF 329
Cdd:cd13982  233 SLGEHGPEAQDLIERMIDFDPEKRPSAEEVLNHPF 267
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
76-326 4.85e-19

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: 85.56  E-value: 4.85e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVqlVQHKWTGQF-FALKVIQLNiDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLA 154
Cdd:cd05148   14 LGSGYFGEV--WEGLWKNRVrVAIKILKSD-DLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGEPVYIITELMEKGSLL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 155 DFLKSV--KTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVGTYN 232
Cdd:cd05148   91 AFLRSPegQVLPVASLIDMACQVAEGMAYLE-EQNSIHRDLAARNILVGEDLVCKVADFGLARLIKEDVYLSSDKKIPYK 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 233 YMSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPYLPPDQEETwssvFELMEAIVDQP-PPALPsenfsPELSSFISTC 310
Cdd:cd05148  170 WTAPEAASHGTFSTKSDVWSFGILLYEMFTyGQVPYPGMNNHEV----YDQITAGYRMPcPAKCP-----QEIYKIMLEC 240
                        250
                 ....*....|....*.
gi 567218350 311 LQKDPNSRSSAKELME 326
Cdd:cd05148  241 WAAEPEDRPSFKALRE 256
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
76-331 5.11e-19

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: 86.76  E-value: 5.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQ---LNIDEAIRksIAQELKINQSSQCPYLVN--------SYQSFYDngaISLI 144
Cdd:cd07859    8 IGKGSYGVVCSAIDTHTGEKVAIKKINdvfEHVSDATR--ILREIKLLRLLRHPDIVEikhimlppSRREFKD---IYVV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 145 LEYMDggslADFLKSVKT----IPESYLSAIFkQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTN- 219
Cdd:cd07859   83 FELME----SDLHQVIKAnddlTPEHHQFFLY-QLLRALKYIH-TANVFHRDLKPKNILANADCKLKICDFGLARVAFNd 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 220 --TAGLANTFVGTYNYMSPErIVGN---KYGNKSDIWSLGLVVLECATGKfPYLPpdqEETWSSVFELMEAIVDQPPP-- 292
Cdd:cd07859  157 tpTAIFWTDYVATRWYRAPE-LCGSffsKYTPAIDIWSIGCIFAEVLTGK-PLFP---GKNVVHQLDLITDLLGTPSPet 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 567218350 293 --------------------ALP-SENFS---PELSSFISTCLQKDPNSRSSAKELMEHPFLN 331
Cdd:cd07859  232 isrvrnekarrylssmrkkqPVPfSQKFPnadPLALRLLERLLAFDPKDRPTAEEALADPYFK 294
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
64-332 5.59e-19

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


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 85.60  E-value: 5.59e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  64 ELSLSDLDMVKFLGKGSSGVVQL--VQHKWTGQFF---ALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDN 138
Cdd:cd05049    1 HIKRDTIVLKRELGEGAFGKVFLgeCYNLEPEQDKmlvAVKTLKDASSPDARKDFEREAELLTNLQHENIVKFYGVCTEG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 139 GAISLILEYMDGGSLADFLKS--------------VKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRG 204
Cdd:cd05049   81 DPLLMVFEYMEHGDLNKFLRShgpdaaflasedsaPGELTLSQLLHIAVQIASGMVYLA-SQHFVHRDLATRNCLVGTNL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 205 EVKITDFGVS--TVMTNTAGLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPYLPPDQEEtwssVFE 281
Cdd:cd05049  160 VVKIGDFGMSrdIYSTDYYRVGGHTMLPIRWMPPESILYRKFTTESDVWSFGVVLWEIFTyGKQPWFQLSNTE----VIE 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 567218350 282 -LMEAIVDQPPPALPSENFSPELSsfistCLQKDPNSRSSAKELmeHPFLNK 332
Cdd:cd05049  236 cITQGRLLQRPRTCPSEVYAVMLG-----CWKREPQQRLNIKDI--HKRLQE 280
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
73-330 7.98e-19

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


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 86.08  E-value: 7.98e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  73 VKFLGKGSSGVVQLVQHKWTGQFFALKVI------------QLNIDEAIRKSIAQELkinqsSQCpylVNSYQSFYDNGA 140
Cdd:cd14134   17 LRLLGEGTFGKVLECWDRKRKRYVAVKIIrnvekyreaakiEIDVLETLAEKDPNGK-----SHC---VQLRDWFDYRGH 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 141 ISLILEYMdGGSLADFLKS--VKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLI----------NHRG---- 204
Cdd:cd14134   89 MCIVFELL-GPSLYDFLKKnnYGPFPLEHVQHIAKQLLEAVAFLH-DLKLTHTDLKPENILLvdsdyvkvynPKKKrqir 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 205 -----EVKITDFGVSTV--MTNTaglanTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATG-------------- 263
Cdd:cd14134  167 vpkstDIKLIDFGSATFddEYHS-----SIVSTRHYRAPEVILGLGWSYPCDVWSIGCILVELYTGellfqthdnlehla 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 264 -------KFPYL-------PPDQEET------WSSVFELMEAIVDQPPPALPSEN----FSPELSSFISTCLQKDPNSRS 319
Cdd:cd14134  242 mmerilgPLPKRmirrakkGAKYFYFyhgrldWPEGSSSGRSIKRVCKPLKRLMLlvdpEHRLLFDLIRKMLEYDPSKRI 321
                        330
                 ....*....|.
gi 567218350 320 SAKELMEHPFL 330
Cdd:cd14134  322 TAKEALKHPFF 332
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
74-339 1.41e-18

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: 85.54  E-value: 1.41e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVQHKWTGQFFALKVIQ---LNIDEAirKSIAQELKINQSSQCPY---LVN------SYQSFYDngaI 141
Cdd:cd07850    6 KPIGSGAQGIVCAAYDTVTGQNVAIKKLSrpfQNVTHA--KRAYRELVLMKLVNHKNiigLLNvftpqkSLEEFQD---V 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 142 SLILEYMDggslADFLKSVKT-IPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVmTNT 220
Cdd:cd07850   81 YLVMELMD----ANLCQVIQMdLDHERMSYLLYQMLCGIKHLH-SAGIIHRDLKPSNIVVKSDCTLKILDFGLART-AGT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 221 AGLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFELM----EAIVDQPPPA--- 293
Cdd:cd07850  155 SFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIRGTVLFPGTDHIDQWNKIIEQLgtpsDEFMSRLQPTvrn 234
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 567218350 294 ----------------LPSENFSPELSS-----------FISTCLQKDPNSRSSAKELMEHPFLNK-YNNSEIN 339
Cdd:cd07850  235 yvenrpkyagysfeelFPDVLFPPDSEEhnklkasqardLLSKMLVIDPEKRISVDDALQHPYINVwYDPSEVE 308
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
76-324 1.63e-18

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: 84.08  E-value: 1.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQ-LNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDngAISLILEYMDGGSLA 154
Cdd:cd14025    4 VGSGGFGQVYKVRHKHWKTWLAIKCPPsLHVDDSERMELLEEAKKMEMAKFRHILPVYGICSE--PVGLVMEYMETGSLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 155 DFLKSvKTIPESYLSAIFKQVLQGLIYLHHDK-HIIHRDLKPSNLLINHRGEVKITDFGVST---VMTNTAGLANTFVGT 230
Cdd:cd14025   82 KLLAS-EPLPWELRFRIIHETAVGMNFLHCMKpPLLHLDLKPANILLDAHYHVKISDFGLAKwngLSHSHDLSRDGLRGT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 231 YNYMSPERIV--GNKYGNKSDIWSLGLVVLECATGKFPYlppdqeETWSSVFELMEAIVDQPPPALP--SENFSPELSSF 306
Cdd:cd14025  161 IAYLPPERFKekNRCPDTKHDVYSFAIVIWGILTQKKPF------AGENNILHIMVKVVKGHRPSLSpiPRQRPSECQQM 234
                        250       260
                 ....*....|....*....|.
gi 567218350 307 IS---TCLQKDPNSRSSAKEL 324
Cdd:cd14025  235 IClmkRCWDQDPRKRPTFQDI 255
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
76-269 1.64e-18

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: 84.85  E-value: 1.64e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKV-----------IQLNIDEAIRK----SIAQELKINQSSQCPYLVnsyqsfydnga 140
Cdd:cd13988    1 LGQGATANVFRGRHKKTGDLYAVKVfnnlsfmrpldVQMREFEVLKKlnhkNIVKLFAIEEELTTRHKV----------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 141 isLILEYMDGGSLADFLKSVKT---IPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLL--INHRGEV--KITDFGV 213
Cdd:cd13988   70 --LVMELCPCGSLYTVLEEPSNaygLPESEFLIVLRDVVAGMNHLR-ENGIVHRDIKPGNIMrvIGEDGQSvyKLTDFGA 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 567218350 214 STVMTNTAGLANTFvGTYNYMSP---ERIV-----GNKYGNKSDIWSLGLVVLECATGKFPYLP 269
Cdd:cd13988  147 ARELEDDEQFVSLY-GTEEYLHPdmyERAVlrkdhQKKYGATVDLWSIGVTFYHAATGSLPFRP 209
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
76-332 2.00e-18

Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Titin, also called connectin, is a muscle-specific elastic protein and is the largest known protein to date. It contains multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains, and a single kinase domain near the C-terminus. It spans half of the sarcomere, the repeating contractile unit of striated muscle, and performs mechanical and catalytic functions. Titin contributes to the passive force generated when muscle is stretched during relaxation. Its kinase domain phosphorylates and regulates the muscle protein telethonin, which is required for sarcomere formation in differentiating myocytes. In addition, titin binds many sarcomere proteins and acts as a molecular scaffold for filament formation during myofibrillogenesis. The Titin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 84.14  E-value: 2.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLN-IDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDngaISLILEYMDGgslA 154
Cdd:cd14104    8 LGRGQFGIVHRCVETSSKKTYMAKFVKVKgADQVLVKKEISILNIARHRNILRLHESFESHEE---LVMIFEFISG---V 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 155 DFLKSVKT----IPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLL-INHRGE-VKITDFGVSTVMTNTAGLANTFV 228
Cdd:cd14104   82 DIFERITTarfeLNEREIVSYVRQVCEALEFLH-SKNIGHFDIRPENIIyCTRRGSyIKIIEFGQSRQLKPGDKFRLQYT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 229 gTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFELMEAIVDQPppalpSENFSPELSSFIS 308
Cdd:cd14104  161 -SAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAEYAFDDEA-----FKNISIEALDFVD 234
                        250       260
                 ....*....|....*....|....
gi 567218350 309 TCLQKDPNSRSSAKELMEHPFLNK 332
Cdd:cd14104  235 RLLVKERKSRMTAQEALNHPWLKQ 258
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
73-329 2.16e-18

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: 83.87  E-value: 2.16e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  73 VKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRK-----SIAQELKiNQSSQCPYLVNSYQSFYDNGAISLIL-E 146
Cdd:cd14037    8 EKYLAEGGFAHVYLVKTSNGGNRAALKRVYVNDEHDLNVckreiEIMKRLS-GHKNIVGYIDSSANRSGNGVYEVLLLmE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 147 YMDGGSLADFL-KSVKT-IPESYLSAIFKQVLQGLIYLHHDKH-IIHRDLKPSNLLINHRGEVKITDFGVSTV----MTN 219
Cdd:cd14037   87 YCKGGGVIDLMnQRLQTgLTESEILKIFCDVCEAVAAMHYLKPpLIHRDLKVENVLISDSGNYKLCDFGSATTkilpPQT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 220 TAGLA--------NTfvgTYNYMSPERI---VGNKYGNKSDIWSLGlvvleCATGKFPYLPPDQEETWSSvfelmeAIVD 288
Cdd:cd14037  167 KQGVTyveedikkYT---TLQYRAPEMIdlyRGKPITEKSDIWALG-----CLLYKLCFYTTPFEESGQL------AILN 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 567218350 289 ---QPPpalPSENFSPELSSFISTCLQKDPNSRSSAKELMEHPF 329
Cdd:cd14037  233 gnfTFP---DNSRYSKRLHKLIRYMLEEDPEKRPNIYQVSYEAF 273
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
131-331 2.37e-18

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: 85.08  E-value: 2.37e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 131 SYQSFYDngaISLILEYMDggslADFLKSVKT-IPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKIT 209
Cdd:cd07876   94 SLEEFQD---VYLVMELMD----ANLCQVIHMeLDHERMSYLLYQMLCGIKHLH-SAGIIHRDLKPSNIVVKSDCTLKIL 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 210 DFGVS-TVMTNTagLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFE------- 281
Cdd:cd07876  166 DFGLArTACTNF--MMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGSVIFQGTDHIDQWNKVIEqlgtpsa 243
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 567218350 282 -----LMEAIVDQ----------------PPPALPSENFSPELSS-----FISTCLQKDPNSRSSAKELMEHPFLN 331
Cdd:cd07876  244 efmnrLQPTVRNYvenrpqypgisfeelfPDWIFPSESERDKLKTsqardLLSKMLVIDPDKRISVDEALRHPYIT 319
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
71-330 2.87e-18

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


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 83.04  E-value: 2.87e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  71 DMVKFLGKGSSGVVQLVQHKWT-------GQFFALKVIqlnIDEAIRKSIAQELKI-----NQSSQCPYLVnsyqSFYDN 138
Cdd:cd14019    4 RIIEKIGEGTFSSVYKAEDKLHdlydrnkGRLVALKHI---YPTSSPSRILNELEClerlgGSNNVSGLIT----AFRNE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 139 GAISLILEYMDGGSLADFLKSVkTIPE--SYLSAIFKqVLQGLiylhHDKHIIHRDLKPSNLLIN-HRGEVKITDFGVST 215
Cdd:cd14019   77 DQVVAVLPYIEHDDFRDFYRKM-SLTDirIYLRNLFK-ALKHV----HSFGIIHRDVKPGNFLYNrETGKGVLVDFGLAQ 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 216 VMTNTAGLANTFVGTYNYMSPEriVGNKYGNKS---DIWSLGLVVLECATGKFP--YLPPDqeetwssvfelMEAIVDqp 290
Cdd:cd14019  151 REEDRPEQRAPRAGTRGFRAPE--VLFKCPHQTtaiDIWSAGVILLSILSGRFPffFSSDD-----------IDALAE-- 215
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 567218350 291 ppaLPSENFSPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14019  216 ---IATIFGSDEAYDLLDKLLELDPSKRITAEEALKHPFF 252
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
69-324 3.12e-18

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: 83.86  E-value: 3.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  69 DLDMVKFLGKGSSG-VVQLVQHKWTGQ----FFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISL 143
Cdd:cd05045    1 NLVLGKTLGEGEFGkVVKATAFRLKGRagytTVAVKMLKENASSSELRDLLSEFNLLKQVNHPHVIKLYGACSQDGPLLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 144 ILEYMDGGSLADFLKSVKTIPESYL--------SAIFK----------------QVLQGLIYLHHDKhIIHRDLKPSNLL 199
Cdd:cd05045   81 IVEYAKYGSLRSFLRESRKVGPSYLgsdgnrnsSYLDNpderaltmgdlisfawQISRGMQYLAEMK-LVHRDLAARNVL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 200 INHRGEVKITDFGVSTVMTNTAGLANTFVG--TYNYMSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPY--LPPDQee 274
Cdd:cd05045  160 VAEGRKMKISDFGLSRDVYEEDSYVKRSKGriPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYpgIAPER-- 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 567218350 275 twssVFELMEA--IVDQPppalpsENFSPELSSFISTCLQKDPNSRSSAKEL 324
Cdd:cd05045  238 ----LFNLLKTgyRMERP------ENCSEEMYNLMLTCWKQEPDKRPTFADI 279
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
68-326 3.20e-18

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: 83.37  E-value: 3.20e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  68 SDLDMVKFLGKGSSGVVQLvqHKWTGQF-FALKVIqlNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILE 146
Cdd:cd05114    4 SELTFMKELGSGLFGVVRL--GKWRAQYkVAIKAI--REGAMSEEDFIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 147 YMDGGSLADFLKSVK-TIPESYLSAIFKQVLQGLIYLHHDKHIiHRDLKPSNLLINHRGEVKITDFGVSTVMTN---TAG 222
Cdd:cd05114   80 FMENGCLLNYLRQRRgKLSRDMLLSMCQDVCEGMEYLERNNFI-HRDLAARNCLVNDTGVVKVSDFGMTRYVLDdqyTSS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 223 LANTFvgTYNYMSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPYlppdqeETWSSvFELMEAIVD-----QPPPAlps 296
Cdd:cd05114  159 SGAKF--PVKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTeGKMPF------ESKSN-YEVVEMVSRghrlyRPKLA--- 226
                        250       260       270
                 ....*....|....*....|....*....|
gi 567218350 297 enfSPELSSFISTCLQKDPNSRSSAKELME 326
Cdd:cd05114  227 ---SKSVYEVMYSCWHEKPEGRPTFADLLR 253
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
76-331 4.32e-18

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: 83.59  E-value: 4.32e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLAD 155
Cdd:cd07869   13 LGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTAIREASLLKGLKHANIVLLHDIIHTKETLTLVFEYVHTDLCQY 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 156 FLKSVKTIPESYLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVGTYNYMS 235
Cdd:cd07869   93 MDKHPGGLHPENVKLFLFQLLRGLSYIHQ-RYILHRDLKPQNLLISDTGELKLADFGLARAKSVPSHTYSNEVVTLWYRP 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 236 PERIVGN-KYGNKSDIWSLGLVVLECATG--KFPYLPPDQEETWSSVFELMEAIVDQPPPALPSENFSPELSSFIST--- 309
Cdd:cd07869  172 PDVLLGStEYSTCLDMWGVGCIFVEMIQGvaAFPGMKDIQDQLERIFLVLGTPNEDTWPGVHSLPHFKPERFTLYSPknl 251
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 567218350 310 -------------------CLQKDPNSRSSAKELMEHPFLN 331
Cdd:cd07869  252 rqawnklsyvnhaedlaskLLQCFPKNRLSAQAALSHEYFS 292
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
76-320 4.96e-18

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: 82.67  E-value: 4.96e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLAD 155
Cdd:cd05084    4 IGRGNFGEVFSGRLRADNTPVAVKSCRETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGGDFLT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 156 FLKSV-KTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVST-----VMTNTAGLANTFVg 229
Cdd:cd05084   84 FLRTEgPRLKVKELIRMVENAAAGMEYLE-SKHCIHRDLAARNCLVTEKNVLKISDFGMSReeedgVYAATGGMKQIPV- 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 230 tyNYMSPERIVGNKYGNKSDIWSLGLVVLEC-ATGKFPYLPPDQEETWssvfELMEAIVDQPPPalpsENFSPELSSFIS 308
Cdd:cd05084  162 --KWTAPEALNYGRYSSESDVWSFGILLWETfSLGAVPYANLSNQQTR----EAVEQGVRLPCP----ENCPDEVYRLME 231
                        250
                 ....*....|..
gi 567218350 309 TCLQKDPNSRSS 320
Cdd:cd05084  232 QCWEYDPRKRPS 243
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
76-330 5.52e-18

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: 83.15  E-value: 5.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEaIRKSIAQELK-INQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLA 154
Cdd:cd14173   10 LGEGAYARVQTCINLITNKEYAVKIIEKRPGH-SRSRVFREVEmLYQCQGHRNVLELIEFFEEEDKFYLVFEKMRGGSIL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 155 DFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGE---VKITDFGVST---VMTNTAGLAN--- 225
Cdd:cd14173   89 SHIHRRRHFNELEASVVVQDIASALDFLH-NKGIAHRDLKPENILCEHPNQvspVKICDFDLGSgikLNSDCSPISTpel 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 226 -TFVGTYNYMSPERI-----VGNKYGNKSDIWSLGLVVLECATGKFPYLPP-------DQEETWSSVFELMEAIVDQPPP 292
Cdd:cd14173  168 lTPCGSAEYMAPEVVeafneEASIYDKRCDLWSLGVILYIMLSGYPPFVGRcgsdcgwDRGEACPACQNMLFESIQEGKY 247
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 567218350 293 ALPSENF---SPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14173  248 EFPEKDWahiSCAAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
69-267 7.57e-18

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: 82.37  E-value: 7.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  69 DLDMVKFLGKGSSGVVqlVQHKWTGQFfALKVIQLNIDEAIR-KSIAQELKINQSSQCPYLVnSYQSFYDNGAISLILEY 147
Cdd:cd14150    1 EVSMLKRIGTGSFGTV--FRGKWHGDV-AVKILKVTEPTPEQlQAFKNEMQVLRKTRHVNIL-LFMGFMTRPNFAIITQW 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 148 MDGGSLADFLKSVKTIPESY-LSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANT 226
Cdd:cd14150   77 CEGSSLYRHLHVTETRFDTMqLIDVARQTAQGMDYLHA-KNIIHRDLKSNNIFLHEGLTVKIGDFGLATVKTRWSGSQQV 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 567218350 227 F--VGTYNYMSPERIV---GNKYGNKSDIWSLGLVVLECATGKFPY 267
Cdd:cd14150  156 EqpSGSILWMAPEVIRmqdTNPYSFQSDVYAYGVVLYELMSGTLPY 201
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
126-328 1.28e-17

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: 81.68  E-value: 1.28e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 126 PYLVNSYQSFYDNGAISLILEYMDGGSLADFL----KSVKTIPESYLSAIFKQVLQGLIYLhHDKHIIHRDLKPSNLLI- 200
Cdd:cd14051   60 PHVVRYYSAWAEDDHMIIQNEYCNGGSLADAIseneKAGERFSEAELKDLLLQVAQGLKYI-HSQNLVHMDIKPGNIFIs 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 201 --------------------NHRGEV---KITDFGVSTVMTNTAglantfV--GTYNYMsPERIVGNKYGN--KSDIWSL 253
Cdd:cd14051  139 rtpnpvsseeeeedfegeedNPESNEvtyKIGDLGHVTSISNPQ------VeeGDCRFL-ANEILQENYSHlpKADIFAL 211
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 567218350 254 GLVVLECATGKfpYLPPDQEEtWSSvfelmeaIVDQPPPALPseNFSPELSSFISTCLQKDPNSRSSAKELMEHP 328
Cdd:cd14051  212 ALTVYEAAGGG--PLPKNGDE-WHE-------IRQGNLPPLP--QCSPEFNELLRSMIHPDPEKRPSAAALLQHP 274
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
65-325 1.37e-17

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: 82.38  E-value: 1.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  65 LSLSDLDMVKFLGKGSSGVVqlVQHKWTGQF------FALKVIQLNIDEAIRKSIAQELKINQSSQCPYlVNSYQSFYDN 138
Cdd:cd05108    4 LKETEFKKIKVLGSGAFGTV--YKGLWIPEGekvkipVAIKELREATSPKANKEILDEAYVMASVDNPH-VCRLLGICLT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 139 GAISLILEYMDGGSLADFLKSVK-TIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVM 217
Cdd:cd05108   81 STVQLITQLMPFGCLLDYVREHKdNIGSQYLLNWCVQIAKGMNYLE-DRRLVHRDLAARNVLVKTPQHVKITDFGLAKLL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 218 TNTAGLANTFVGTY--NYMSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPY--LPPDQeetWSSVFELMEAIvDQPPP 292
Cdd:cd05108  160 GAEEKEYHAEGGKVpiKWMALESILHRIYTHQSDVWSYGVTVWELMTfGSKPYdgIPASE---ISSILEKGERL-PQPPI 235
                        250       260       270
                 ....*....|....*....|....*....|...
gi 567218350 293 AlpsenfSPELSSFISTCLQKDPNSRSSAKELM 325
Cdd:cd05108  236 C------TIDVYMIMVKCWMIDADSRPKFRELI 262
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
76-273 2.04e-17

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: 81.39  E-value: 2.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKwtGQFFALKVIQLNID---EAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGS 152
Cdd:cd14158   23 LGEGGFGVVFKGYIN--DKNVAVKKLAAMVDistEDLTKQFEQEIQVMAKCQHENLVELLGYSCDGPQLCLVYTYMPNGS 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 153 LADFLKSVK-TIPESYLSA--IFKQVLQGLIYLHHDKHIiHRDLKPSNLLINHRGEVKITDFGVS--------TVMTnta 221
Cdd:cd14158  101 LLDRLACLNdTPPLSWHMRckIAQGTANGINYLHENNHI-HRDIKSANILLDETFVPKISDFGLArasekfsqTIMT--- 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 567218350 222 glaNTFVGTYNYMSPERIVGnKYGNKSDIWSLGLVVLECATGkfpyLPPDQE 273
Cdd:cd14158  177 ---ERIVGTTAYMAPEALRG-EITPKSDIFSFGVVLLEIITG----LPPVDE 220
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
129-337 2.16e-17

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


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 82.31  E-value: 2.16e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 129 VNSYQSFYdngaisLILEYMdGGSLADFLKSVKtIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKI 208
Cdd:cd07880   89 LDRFHDFY------LVMPFM-GTDLGKLMKHEK-LSEDRIQFLVYQMLKGLKYIH-AAGIIHRDLKPGNLAVNEDCELKI 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 209 TDFGVStvmTNTAGLANTFVGTYNYMSPERIVG-NKYGNKSDIWSLGLVVLECATGKFPYLPPDQeetWSSVFELMEaIV 287
Cdd:cd07880  160 LDFGLA---RQTDSEMTGYVVTRWYRAPEVILNwMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDH---LDQLMEIMK-VT 232
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 567218350 288 DQPP-------------------PALPSENF-------SPELSSFISTCLQKDPNSRSSAKELMEHPFLNKYNNSE 337
Cdd:cd07880  233 GTPSkefvqklqsedaknyvkklPRFRKKDFrsllpnaNPLAVNVLEKMLVLDAESRITAAEALAHPYFEEFHDPE 308
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
76-326 2.38e-17

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: 80.57  E-value: 2.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLAD 155
Cdd:cd05041    3 IGRGNFGDVYRGVLKPDNTEVAVKTCRETLPPDLKRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGGSLLT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 156 FL-KSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVS-----TVMTNTAGLANTFVg 229
Cdd:cd05041   83 FLrKKGARLTVKQLLQMCLDAAAGMEYLE-SKNCIHRDLAARNCLVGENNVLKISDFGMSreeedGEYTVSDGLKQIPI- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 230 tyNYMSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPYLPPDQEETWssvfELMEAIVDQPPPALPSEnfspELSSFIS 308
Cdd:cd05041  161 --KWTAPEALNYGRYTSESDVWSFGILLWEIFSlGATPYPGMSNQQTR----EQIESGYRMPAPELCPE----AVYRLML 230
                        250
                 ....*....|....*...
gi 567218350 309 TCLQKDPNSRSSAKELME 326
Cdd:cd05041  231 QCWAYDPENRPSFSEIYN 248
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
64-318 3.01e-17

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


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 80.53  E-value: 3.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  64 ELSLSDLDMVKFLGKGSSGVVqlvqhkWTGQF-----FALKVIQ---LNIDEAIRksiaqELKINQSSQCPYLVNSYQSF 135
Cdd:cd05068    4 EIDRKSLKLLRKLGSGQFGEV------WEGLWnnttpVAVKTLKpgtMDPEDFLR-----EAQIMKKLRHPKLIQLYAVC 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 136 YDNGAISLILEYMDGGSLADFLKSVKT---IPEsyLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFG 212
Cdd:cd05068   73 TLEEPIYIITELMKHGSLLEYLQGKGRslqLPQ--LIDMAAQVASGMAYLE-SQNYIHRDLAARNVLVGENNICKVADFG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 213 VSTVMTNTaGLANTFVGT---YNYMSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPYlpPDQeeTWSSVFELMEAIVD 288
Cdd:cd05068  150 LARVIKVE-DEYEAREGAkfpIKWTAPEAANYNRFSIKSDVWSFGILLTEIVTyGRIPY--PGM--TNAEVLQQVERGYR 224
                        250       260       270
                 ....*....|....*....|....*....|
gi 567218350 289 QPPPAlpseNFSPELSSFISTCLQKDPNSR 318
Cdd:cd05068  225 MPCPP----NCPPQLYDIMLECWKADPMER 250
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
153-330 3.34e-17

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: 80.38  E-value: 3.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 153 LADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHR-GEVKITDFGVSTVMTNTagLANTFVGTY 231
Cdd:cd14102   92 LFDFITEKGALDEDTARGFFRQVLEAVRHCY-SCGVVHRDIKDENLLVDLRtGELKLIDFGSGALLKDT--VYTDFDGTR 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 232 NYMSPERIVGNKY-GNKSDIWSLGLVVLECATGKFPYlppDQEEtwssvfELMEAIVdqpppaLPSENFSPELSSFISTC 310
Cdd:cd14102  169 VYSPPEWIRYHRYhGRSATVWSLGVLLYDMVCGDIPF---EQDE------EILRGRL------YFRRRVSPECQQLIKWC 233
                        170       180
                 ....*....|....*....|
gi 567218350 311 LQKDPNSRSSAKELMEHPFL 330
Cdd:cd14102  234 LSLRPSDRPTLEQIFDHPWM 253
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
76-267 3.40e-17

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: 80.38  E-value: 3.40e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFF--ALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYqSFYDNGAISLILEYMDGGSL 153
Cdd:cd05115   12 LGSGNFGCVKKGVYKMRKKQIdvAIKVLKQGNEKAVRDEMMREAQIMHQLDNPYIVRMI-GVCEAEALMLVMEMASGGPL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 154 ADFLKSVK-TIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVM--TNTAGLANTFvGT 230
Cdd:cd05115   91 NKFLSGKKdEITVSNVVELMHQVSMGMKYLE-EKNFVHRDLAARNVLLVNQHYAKISDFGLSKALgaDDSYYKARSA-GK 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 567218350 231 Y--NYMSPERIVGNKYGNKSDIWSLGLVVLEC-ATGKFPY 267
Cdd:cd05115  169 WplKWYAPECINFRKFSSRSDVWSYGVTMWEAfSYGQKPY 208
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
70-326 3.73e-17

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: 80.71  E-value: 3.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  70 LDMVKFLGKGSSGVVQLVQHK----WTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNG--AISL 143
Cdd:cd05080    6 LKKIRDLGEGHFGKVSLYCYDptndGTGEMVAVKALKADCGPQHRSGWKQEIDILKTLYHENIVKYKGCCSEQGgkSLQL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 144 ILEYMDGGSLADFLKSVKtIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVM------ 217
Cdd:cd05080   86 IMEYVPLGSLRDYLPKHS-IGLAQLLLFAQQICEGMAYLH-SQHYIHRDLAARNVLLDNDRLVKIGDFGLAKAVpeghey 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 218 --TNTAGLANTFvgtynYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEetWSSVFELMEAIVDQPP---- 291
Cdd:cd05080  164 yrVREDGDSPVF-----WYAPECLKEYKFYYASDVWSFGVTLYELLTHCDSSQSPPTK--FLEMIGIAQGQMTVVRliel 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 567218350 292 ----PALPSENFSP-ELSSFISTCLQKDPNSRSSAKELME 326
Cdd:cd05080  237 lergERLPCPDKCPqEVYHLMKNCWETEASFRPTFENLIP 276
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
65-326 3.83e-17

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: 80.03  E-value: 3.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  65 LSLSDLDMVKFLGKGSSGVVQLVQHKwtGQFFALKVIQlniDEAIRKSIAQELKINQSSQCPYLVNSYQSFY-DNGAISL 143
Cdd:cd05082    3 LNMKELKLLQTIGKGEFGDVMLGDYR--GNKVAVKCIK---NDATAQAFLAEASVMTQLRHSNLVQLLGVIVeEKGGLYI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 144 ILEYMDGGSLADFLKSV--KTIPESYLSAIFKQVLQGLIYLHHDkHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTA 221
Cdd:cd05082   78 VTEYMAKGSLVDYLRSRgrSVLGGDCLLKFSLDVCEAMEYLEGN-NFVHRDLAARNVLVSEDNVAKVSDFGLTKEASSTQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 222 GLANTFVgtyNYMSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPY--LP-----PDQEETWSsvfelMEAivdqpPPA 293
Cdd:cd05082  157 DTGKLPV---KWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPYprIPlkdvvPRVEKGYK-----MDA-----PDG 223
                        250       260       270
                 ....*....|....*....|....*....|...
gi 567218350 294 LPsenfsPELSSFISTCLQKDPNSRSSAKELME 326
Cdd:cd05082  224 CP-----PAVYDVMKNCWHLDAAMRPSFLQLRE 251
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
76-332 3.97e-17

Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity.STRAD-beta is also referred to as ALS2CR2 (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 2 protein), since the human gene encoding it is located within the juvenile ALS2 critical region on chromosome 2q33-q34. It is not linked to the development of ALS2. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. The STRAD-beta subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270864 [Multi-domain]  Cd Length: 328  Bit Score: 81.07  E-value: 3.97e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGV--VQLVQHKWTGQFFALKVIQL-NIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGS 152
Cdd:cd08226    6 LGKGFCNLtsVYLARHTPTGTLVTVKITNLdNCSEEHLKALQNEVVLSHFFRHPNIMTHWTVFTEGSWLWVISPFMAYGS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 153 LADFLKSVKT--IPESYLSAIFKQVLQGLIYLHHDKHIiHRDLKPSNLLINHRGEVKITDF-GVSTVMTNtaGLANTFVg 229
Cdd:cd08226   86 ARGLLKTYFPegMNEALIGNILYGAIKALNYLHQNGCI-HRSVKASHILISGDGLVSLSGLsHLYSMVTN--GQRSKVV- 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 230 tYNY----------MSPERIVGNKYGN--KSDIWSLGLVVLECATGKFPYL-----------------------PPDQEE 274
Cdd:cd08226  162 -YDFpqfstsvlpwLSPELLRQDLHGYnvKSDIYSVGITACELARGQVPFQdmrrtqmllqklkgppyspldifPFPELE 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 567218350 275 ------------------TWSSVFELMEAIVDQPPpalPSENFSPELSSFISTCLQKDPNSRSSAKELMEHPFLNK 332
Cdd:cd08226  241 srmknsqsgmdsgigesvATSSMTRTMTSERLQTP---SSKTFSPAFHNLVELCLQQDPEKRPSASSLLSHSFFKQ 313
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
93-322 4.02e-17

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: 80.13  E-value: 4.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  93 GQFFALKVIQLNIDEaiRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLADFLkSVKTIP--ESYLSA 170
Cdd:cd13992   25 GRTVAIKHITFSRTE--KRTILQELNQLKELVHDNLNKFIGICINPPNIAVVTEYCTRGSLQDVL-LNREIKmdWMFKSS 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 171 IFKQVLQGLIYLHHDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVGTYN---YMSPERIVGNKYGN- 246
Cdd:cd13992  102 FIKDIVKGMNYLHSSSIGYHGRLKSSNCLVDSRWVVKLTDFGLRNLLEEQTNHQLDEDAQHKkllWTAPELLRGSLLEVr 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 247 ---KSDIWSLGLVVLECATGKFPYLPPDQEEtwssvfELMEAIVDQ-----PPPALPSENFSPELSSFISTCLQKDPNSR 318
Cdd:cd13992  182 gtqKGDVYSFAIILYEILFRSDPFALEREVA------IVEKVISGGnkpfrPELAVLLDEFPPRLVLLVKQCWAENPEKR 255

                 ....
gi 567218350 319 SSAK 322
Cdd:cd13992  256 PSFK 259
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
76-320 4.10e-17

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: 80.01  E-value: 4.10e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQ--LVQHKWTGQFFALKVIQ-LNIDEAIRKSIAQELKINQSSQCPYLVNSYqSFYDNGAISLILEYMDGGS 152
Cdd:cd05116    3 LGSGNFGTVKkgYYQMKKVVKTVAVKILKnEANDPALKDELLREANVMQQLDNPYIVRMI-GICEAESWMLVMEMAELGP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 153 LADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMT---NTAGLANTFVG 229
Cdd:cd05116   82 LNKFLQKNRHVTEKNITELVHQVSMGMKYLE-ESNFVHRDLAARNVLLVTQHYAKISDFGLSKALRadeNYYKAQTHGKW 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 230 TYNYMSPERIVGNKYGNKSDIWSLGLVVLEC-ATGKFPYLPPDQEETWSSV--FELMEAivdqpPPALPsenfsPELSSF 306
Cdd:cd05116  161 PVKWYAPECMNYYKFSSKSDVWSFGVLMWEAfSYGQKPYKGMKGNEVTQMIekGERMEC-----PAGCP-----PEMYDL 230
                        250
                 ....*....|....
gi 567218350 307 ISTCLQKDPNSRSS 320
Cdd:cd05116  231 MKLCWTYDVDERPG 244
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
130-337 4.11e-17

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: 81.49  E-value: 4.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 130 NSYQSFYdngaisLILEYMDGGsladfLKSVKTIP--ESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVK 207
Cdd:cd07879   90 DEFQDFY------LVMPYMQTD-----LQKIMGHPlsEDKVQYLVYQMLCGLKYIH-SAGIIHRDLKPGNLAVNEDCELK 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 208 ITDFGVS----TVMTNtaglantFVGTYNYMSPERIVGNKYGNKS-DIWSLGLVVLECATGKFPYLPPDQEETWSSVF-- 280
Cdd:cd07879  158 ILDFGLArhadAEMTG-------YVVTRWYRAPEVILNWMHYNQTvDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQILkv 230
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 567218350 281 ------ELMEAIVD-------QPPPALPSENFS-------PELSSFISTCLQKDPNSRSSAKELMEHPFLNKYNNSE 337
Cdd:cd07879  231 tgvpgpEFVQKLEDkaaksyiKSLPKYPRKDFStlfpkasPQAVDLLEKMLELDVDKRLTATEALEHPYFDSFRDAD 307
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
64-267 5.85e-17

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: 80.08  E-value: 5.85e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  64 ELSLSDLDMVKFLGKGSSGVVQlvQHKWTGQFfALKVIQLNID-----EAIRKSIAQELKINQSSqcpylVNSYQSFYDN 138
Cdd:cd14149    8 EIEASEVMLSTRIGSGSFGTVY--KGKWHGDV-AVKILKVVDPtpeqfQAFRNEVAVLRKTRHVN-----ILLFMGYMTK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 139 GAISLILEYMDGGSLADFLKSVKTIPESY-LSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLINHRGEVKITDFGVSTVM 217
Cdd:cd14149   80 DNLAIVTQWCEGSSLYKHLHVQETKFQMFqLIDIARQTAQGMDYLHA-KNIIHRDMKSNNIFLHEGLTVKIGDFGLATVK 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 567218350 218 TNTAG--LANTFVGTYNYMSPERIV---GNKYGNKSDIWSLGLVVLECATGKFPY 267
Cdd:cd14149  159 SRWSGsqQVEQPTGSILWMAPEVIRmqdNNPFSFQSDVYSYGIVLYELMTGELPY 213
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
110-264 6.16e-17

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 81.19  E-value: 6.16e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 110 RKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGgSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHDKhII 189
Cdd:PHA03212 127 RGGTATEAHILRAINHPSIIQLKGTFTYNKFTCLILPRYKT-DLYCYLAAKRNIAICDILAIERSVLRAIQYLHENR-II 204
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 567218350 190 HRDLKPSNLLINHRGEVKITDFGVSTVMTN-TAGLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGK 264
Cdd:PHA03212 205 HRDIKAENIFINHPGDVCLGDFGAACFPVDiNANKYYGWAGTIATNAPELLARDPYGPAVDIWSAGIVLFEMATCH 280
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
70-326 6.76e-17

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: 79.86  E-value: 6.76e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  70 LDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIqLNIDEAIRKSIAQELKI-NQSSQCPYLVNSYQSFY-------DNGAI 141
Cdd:cd14036    2 LRIKRVIAEGGFAFVYEAQDVGTGKEYALKRL-LSNEEEKNKAIIQEINFmKKLSGHPNIVQFCSAASigkeesdQGQAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 142 SLILEYMDGGSLADFLKSVKT----IPESYLSaIFKQVLQGLIYLHHDK-HIIHRDLKPSNLLINHRGEVKITDFGVSTV 216
Cdd:cd14036   81 YLLLTELCKGQLVDFVKKVEApgpfSPDTVLK-IFYQTCRAVQHMHKQSpPIIHRDLKIENLLIGNQGQIKLCDFGSATT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 217 MT---------NTAGLAN---TFVGTYNYMSPERI---VGNKYGNKSDIWSLGLVVLECATGKFPYlppdqEEtwSSVFE 281
Cdd:cd14036  160 EAhypdyswsaQKRSLVEdeiTRNTTPMYRTPEMIdlySNYPIGEKQDIWALGCILYLLCFRKHPF-----ED--GAKLR 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 567218350 282 LMEAIVDQPPPALPSENFSPelssFISTCLQKDPNSRSSAKELME 326
Cdd:cd14036  233 IINAKYTIPPNDTQYTVFHD----LIRSTLKVNPEERLSITEIVE 273
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
140-324 6.92e-17

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: 79.32  E-value: 6.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 140 AISLILEYMDGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMtn 219
Cdd:cd05060   69 PLMLVMELAPLGPLLKYLKKRREIPVSDLKELAHQVAMGMAYLE-SKHFVHRDLAARNVLLVNRHQAKISDFGMSRAL-- 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 220 taGLANTFV-----GTY--NYMSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPYlppdQEETWSSVFELMEAIVDQPP 291
Cdd:cd05060  146 --GAGSDYYrattaGRWplKWYAPECINYGKFSSKSDVWSYGVTLWEAFSyGAKPY----GEMKGPEVIAMLESGERLPR 219
                        170       180       190
                 ....*....|....*....|....*....|...
gi 567218350 292 PalpsENFSPELSSFISTCLQKDPNSRSSAKEL 324
Cdd:cd05060  220 P----EECPQEIYSIMLSCWKYRPEDRPTFSEL 248
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
115-318 7.87e-17

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: 78.86  E-value: 7.87e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 115 QELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLADFLKS--VKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRD 192
Cdd:cd05034   39 QEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTELMSKGSLLDYLRTgeGRALRLPQLIDMAAQIASGMAYLE-SRNYIHRD 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 193 LKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTfvGT---YNYMSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPYL 268
Cdd:cd05034  118 LAARNILVGENNVCKVADFGLARLIEDDEYTARE--GAkfpIKWTAPEAALYGRFTIKSDVWSFGILLYEIVTyGRVPYP 195
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 567218350 269 PPDQEEtwssVFELMEAIVDQPPPalpsENFSPELSSFISTCLQKDPNSR 318
Cdd:cd05034  196 GMTNRE----VLEQVERGYRMPKP----PGCPDELYDIMLQCWKKEPEER 237
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
67-331 9.14e-17

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: 79.69  E-value: 9.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  67 LSDLDMVKFLGKGSSGVVQLVqhkwtgqffALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILE 146
Cdd:cd05051   29 LSDLTSDDFIGNDNKDEPVLV---------AVKMLRPDASKNAREDFLKEVKIMSQLKDPNIVRLLGVCTRDEPLCMIVE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 147 YMDGGSLADFLKS------------VKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVS 214
Cdd:cd05051  100 YMENGDLNQFLQKheaetqgasatnSKTLSYGTLLYMATQIASGMKYLE-SLNFVHRDLATRNCLVGPNYTIKIADFGMS 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 215 TvmtntaglaNTFVGTY-----------NYMSPERIVGNKYGNKSDIWSLGLVVLECATgkFPYLPPDQEETWSSVFE-- 281
Cdd:cd05051  179 R---------NLYSGDYyriegravlpiRWMAWESILLGKFTTKSDVWAFGVTLWEILT--LCKEQPYEHLTDEQVIEna 247
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 567218350 282 -------LMEAIVDQPPpalpseNFSPELSSFISTCLQKDPNSRSSAKELmeHPFLN 331
Cdd:cd05051  248 geffrddGMEVYLSRPP------NCPKEIYELMLECWRRDEEDRPTFREI--HLFLQ 296
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
107-324 9.76e-17

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: 79.70  E-value: 9.76e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 107 EAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLADFLKS-------------VKTIPESYLSAIFK 173
Cdd:cd05093   48 DNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLNKFLRAhgpdavlmaegnrPAELTQSQMLHIAQ 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 174 QVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVS--TVMTNTAGLANTFVGTYNYMSPERIVGNKYGNKSDIW 251
Cdd:cd05093  128 QIAAGMVYLA-SQHFVHRDLATRNCLVGENLLVKIGDFGMSrdVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVW 206
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 567218350 252 SLGLVVLECAT-GKFPYLPPDQEETWSSVfelMEAIVDQPPPALPSENFSPELSsfistCLQKDPNSRSSAKEL 324
Cdd:cd05093  207 SLGVVLWEIFTyGKQPWYQLSNNEVIECI---TQGRVLQRPRTCPKEVYDLMLG-----CWQREPHMRLNIKEI 272
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
150-337 9.78e-17

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: 80.09  E-value: 9.78e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 150 GGSLADFLKSVKtIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVStvmTNTAGLANTFVG 229
Cdd:cd07878  103 GADLNNIVKCQK-LSDEHVQFLIYQLLRGLKYIH-SAGIIHRDLKPSNVAVNEDCELRILDFGLA---RQADDEMTGYVA 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 230 TYNYMSPERIVGNKYGNKS-DIWSLGLVVLECATGK--FP---YLppDQ-----EETWSSVFELMEAIVD-------QPP 291
Cdd:cd07878  178 TRWYRAPEIMLNWMHYNQTvDIWSVGCIMAELLKGKalFPgndYI--DQlkrimEVVGTPSPEVLKKISSeharkyiQSL 255
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 567218350 292 PALPSENFS-------PELSSFISTCLQKDPNSRSSAKELMEHPFLNKYNNSE 337
Cdd:cd07878  256 PHMPQQDLKkifrganPLAIDLLEKMLVLDSDKRISASEALAHPYFSQYHDPE 308
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
141-318 1.16e-16

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: 78.42  E-value: 1.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 141 ISLILEYMDGGSLADFLKSVK----TIPEsyLSAIFKQVLQGLIYLHHDKHIiHRDLKPSNLLINHRGEVKITDFGVSTV 216
Cdd:cd14203   64 IYIVTEFMSKGSLLDFLKDGEgkylKLPQ--LVDMAAQIASGMAYIERMNYI-HRDLRAANILVGDNLVCKIADFGLARL 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 217 MTN---TAGLANTFvgTYNYMSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPYLPPDQEEtwssVFELMEAIVDQP-P 291
Cdd:cd14203  141 IEDneyTARQGAKF--PIKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNRE----VLEQVERGYRMPcP 214
                        170       180
                 ....*....|....*....|....*..
gi 567218350 292 PALPsenfsPELSSFISTCLQKDPNSR 318
Cdd:cd14203  215 PGCP-----ESLHELMCQCWRKDPEER 236
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
137-326 1.24e-16

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: 79.00  E-value: 1.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 137 DNGAISLILEYMDGGSLADFLKSVK--TIPESYLS-----AIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGE---- 205
Cdd:cd05044   70 DNDPQYIILELMEGGDLLSYLRAARptAFTPPLLTlkdllSICVDVAKGCVYLE-DMHFVHRDLAARNCLVSSKDYrerv 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 206 VKITDFGVSTVMTNT-------AGLANTfvgtyNYMSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPYLPPDQEETWS 277
Cdd:cd05044  149 VKIGDFGLARDIYKNdyyrkegEGLLPV-----RWMAPESLVDGVFTTQSDVWAFGVLMWEILTlGQQPYPARNNLEVLH 223
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 567218350 278 SVFElmEAIVDQPPpalpseNFSPELSSFISTCLQKDPNSRSSAKELME 326
Cdd:cd05044  224 FVRA--GGRLDQPD------NCPDDLYELMLRCWSTDPEERPSFARILE 264
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
143-321 1.28e-16

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: 79.02  E-value: 1.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 143 LILEYMDGGSLADFLKSvKTIPESYLSAIFKQVLQGLIYLH--------HDKHIIHRDLKPSNLLINHRGEVKITDFGVS 214
Cdd:cd13998   70 LVTAFHPNGSL*DYLSL-HTIDWVSLCRLALSVARGLAHLHseipgctqGKPAIAHRDLKSKNILVKNDGTCCIADFGLA 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 215 TVMTNTAGL----ANTFVGTYNYMSPERIVG------NKYGNKSDIWSLGLVVLE----CATGKFP---YLPPDQEETWS 277
Cdd:cd13998  149 VRLSPSTGEednaNNGQVGTKRYMAPEVLEGainlrdFESFKRVDIYAMGLVLWEmasrCTDLFGIveeYKPPFYSEVPN 228
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 567218350 278 S-VFELMEAIV--DQPPPALPSENFS-PELSSFIST---CLQKDPNSRSSA 321
Cdd:cd13998  229 HpSFEDMQEVVvrDKQRPNIPNRWLShPGLQSLAETieeCWDHDAEARLTA 279
PK_NRBP1 cd14034
Pseudokinase domain of Nuclear Receptor Binding Protein 1; The pseudokinase domain shows ...
141-330 1.28e-16

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: 79.02  E-value: 1.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 141 ISLILEYMDGGSLADFLKSVK----TIPESYLSAIFKQVLQGLIYLHH-DKHIIHRDLKPSNLLINHRGEVKITDFGVST 215
Cdd:cd14034   89 VIFITEYMSSGSLKQFLKKTKknhkTMNEKAWKRWCTQILSALSYLHScDPPIIHGNLTCDTIFIQHNGLIKIGSVAPDT 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 216 VmTNTAGLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECAT------GKFPYLPpdqEETWSSVFELMEaivdq 289
Cdd:cd14034  169 I-NNHVKTCREEQKNLHFFAPEYGEVANVTTAVDIYSFGMCALEMAVleiqgnGESSYVP---QEAINSAIQLLE----- 239
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 567218350 290 pppalpsenfSPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14034  240 ----------DPLQREFIQKCLEVDPSKRPTARELLFHQAL 270
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
65-326 1.45e-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: 78.91  E-value: 1.45e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  65 LSLSDLDMVKFLGKGSSGVVqlVQHKWT--GQFF----ALKVIQLNIDEAIRKSIAQELKINQSSQCPYlVNSYQSFYDN 138
Cdd:cd05109    4 LKETELKKVKVLGSGAFGTV--YKGIWIpdGENVkipvAIKVLRENTSPKANKEILDEAYVMAGVGSPY-VCRLLGICLT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 139 GAISLILEYMDGGSLADFLKSVK-TIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVM 217
Cdd:cd05109   81 STVQLVTQLMPYGCLLDYVRENKdRIGSQDLLNWCVQIAKGMSYLE-EVRLVHRDLAARNVLVKSPNHVKITDFGLARLL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 218 --TNTAGLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPYLPPDQEEtwssVFELMEA--IVDQPPp 292
Cdd:cd05109  160 diDETEYHADGGKVPIKWMALESILHRRFTHQSDVWSYGVTVWELMTfGAKPYDGIPARE----IPDLLEKgeRLPQPP- 234
                        250       260       270
                 ....*....|....*....|....*....|....
gi 567218350 293 alpseNFSPELSSFISTCLQKDPNSRSSAKELME 326
Cdd:cd05109  235 -----ICTIDVYMIMVKCWMIDSECRPRFRELVD 263
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
88-330 1.83e-16

Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to Calcium/calmodulin-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized STKs with similarity to CaMKs, which are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. This uncharacterized subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 78.53  E-value: 1.83e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  88 QHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLADFLKSVKTIPESY 167
Cdd:cd14088   21 KDKTTGKLYTCKKFLKRDGRKVRKAAKNEINILKMVKHPNILQLVDVFETRKEYFIFLELATGREVFDWILDQGYYSERD 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 168 LSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLINHR---GEVKITDFGVSTVMTntaGLANTFVGTYNYMSPERIVGNKY 244
Cdd:cd14088  101 TSNVIRQVLEAVAYLHSLK-IVHRNLKLENLVYYNRlknSKIVISDFHLAKLEN---GLIKEPCGTPEYLAPEVVGRQRY 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 245 GNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFE-LMEAIV------DQPppalPSENFSPELSSFISTCLQKDPNS 317
Cdd:cd14088  177 GRPVDCWAIGVIMYILLSGNPPFYDEAEEDDYENHDKnLFRKILagdyefDSP----YWDDISQAAKDLVTRLMEVEQDQ 252
                        250
                 ....*....|...
gi 567218350 318 RSSAKELMEHPFL 330
Cdd:cd14088  253 RITAEEAISHEWI 265
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
71-332 2.13e-16

Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha, stabilized through ATP and MO25, may be needed to activate LKB1. A mutation which results in a truncation of a C-terminal part of the human STRAD-alpha pseudokinase domain and disrupts its association with LKB1, leads to PMSE (polyhydramnios, megalencephaly, symptomatic epilepsy) syndrome. Several splice variants of STRAD-alpha exist which exhibit different effects on the localization and activation of LKB1. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. The STRAD alpha subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173767 [Multi-domain]  Cd Length: 327  Bit Score: 79.22  E-value: 2.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  71 DMVKFLGKGSSG--VVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQ-ELKINQSSQCPYLVNSYQSFYDNGAISLILEY 147
Cdd:cd08227    1 ELLTVIGRGFEDlmTVNLARYKPTGEYVTVRRINLEACTNEMVTFLQgELHVSKLFNHPNIVPYRATFIADNELWVVTSF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 148 MDGGSLADFLKS--VKTIPESYLSAIFKQVLQGLIYLHHDKHIiHRDLKPSNLLINHRGEVKITDFGVSTVMTN---TAG 222
Cdd:cd08227   81 MAYGSAKDLICThfMDGMSELAIAYILQGVLKALDYIHHMGYV-HRSVKASHILISVDGKVYLSGLRSNLSMINhgqRLR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 223 LANTF----VGTYNYMSPERIVGN--KYGNKSDIWSLGLVVLECATGKFPY-------------------------LPPD 271
Cdd:cd08227  160 VVHDFpkysVKVLPWLSPEVLQQNlqGYDAKSDIYSVGITACELANGHVPFkdmpatqmlleklngtvpclldtttIPAE 239
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 567218350 272 QEETWSSVFELMEAIVDQP-----------PPALP-SENFSPELSSFISTCLQKDPNSRSSAKELMEHPFLNK 332
Cdd:cd08227  240 ELTMKPSRSGANSGLGESTtvstprpsngeSSSHPyNRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQ 312
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
143-324 2.37e-16

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: 78.34  E-value: 2.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 143 LILEYMDGGSLADFLKS-----------------VKTIPESYLS-----AIFKQVLQGLIYLHhDKHIIHRDLKPSNLLI 200
Cdd:cd05050   85 LLFEYMAYGDLNEFLRHrspraqcslshstssarKCGLNPLPLScteqlCIAKQVAAGMAYLS-ERKFVHRDLATRNCLV 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 201 NHRGEVKITDFGVSTVMTNT---AGLANTFVgTYNYMSPERIVGNKYGNKSDIWSLGLVVLEC-ATGKFPYLPPDQEETw 276
Cdd:cd05050  164 GENMVVKIADFGLSRNIYSAdyyKASENDAI-PIRWMPPESIFYNRYTTESDVWAYGVVLWEIfSYGMQPYYGMAHEEV- 241
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 567218350 277 ssVFELMEAIVDQPPPALPSenfspELSSFISTCLQKDPNSRSSAKEL 324
Cdd:cd05050  242 --IYYVRDGNVLSCPDNCPL-----ELYNLMRLCWSKLPSDRPSFASI 282
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
64-333 2.90e-16

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: 77.80  E-value: 2.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  64 ELSLSDLDMVKFLGKGSSGvvQLVQHKWTGQF-FALKVIQLNIDEAirKSIAQELKINQSSQCPYLVNSYqSFYDNGAIS 142
Cdd:cd05070    5 EIPRESLQLIKRLGNGQFG--EVWMGTWNGNTkVAIKTLKPGTMSP--ESFLEEAQIMKKLKHDKLVQLY-AVVSEEPIY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 143 LILEYMDGGSLADFLK--SVKTIPESYLSAIFKQVLQGLIYLHHDKHIiHRDLKPSNLLINHRGEVKITDFGVSTVMTN- 219
Cdd:cd05070   80 IVTEYMSKGSLLDFLKdgEGRALKLPNLVDMAAQVAAGMAYIERMNYI-HRDLRSANILVGNGLICKIADFGLARLIEDn 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 220 --TAGLANTFvgTYNYMSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPYLPPDQEEtwssVFELMEAIVDQPPPalps 296
Cdd:cd05070  159 eyTARQGAKF--PIKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNRE----VLEQVERGYRMPCP---- 228
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 567218350 297 ENFSPELSSFISTCLQKDPNSRSSAKELmeHPFLNKY 333
Cdd:cd05070  229 QDCPISLHELMIHCWKKDPEERPTFEYL--QGFLEDY 263
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
77-325 3.17e-16

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: 77.30  E-value: 3.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  77 GKGSSGVVqlVQHKWTGQFFALKVIQLNideairkSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLADF 156
Cdd:cd14060    2 GGGSFGSV--YRAIWVSQDKEVAVKKLL-------KIEKEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLFDY 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 157 LKSVKT--IPESYLSAIFKQVLQGLIYLHHDK--HIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLanTFVGTYN 232
Cdd:cd14060   73 LNSNESeeMDMDQIMTWATDIAKGMHYLHMEApvKVIHRDLKSRNVVIAADGVLKICDFGASRFHSHTTHM--SLVGTFP 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 233 YMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFELMEAivdqppPALPSeNFSPELSSFISTCLQ 312
Cdd:cd14060  151 WMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPFKGLEGLQVAWLVVEKNER------PTIPS-SCPRSFAELMRRCWE 223
                        250
                 ....*....|...
gi 567218350 313 KDPNSRSSAKELM 325
Cdd:cd14060  224 ADVKERPSFKQII 236
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
71-273 3.23e-16

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). They show speckled localization in the nucleus, apart from the nucleoles. They play roles in the regulation of many nuclear pathways including gene transcription, cell survival, proliferation, differentiation, development, and DNA damage response. Vertebrates contain three HIPKs (HIPK1-3) and mammals harbor an additional family member HIPK4, which does not contain a homeobox-interacting domain and is localized in the cytoplasm. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors and it regulates gene transcription during development and in DNA damage response. The HIPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 78.64  E-value: 3.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  71 DMVKFLGKGSSGVVQLVQHKWTGQFFALKVI--------QLNIDEAIRKSIAQElkinqSSQCPYLVNSYQSFYDNGAIS 142
Cdd:cd14211    2 EVLEFLGRGTFGQVVKCWKRGTNEIVAIKILknhpsyarQGQIEVSILSRLSQE-----NADEFNFVRAYECFQHKNHTC 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 143 LILEYMDGgSLADFLKSVK--TIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLI----NHRGEVKITDFGVSTV 216
Cdd:cd14211   77 LVFEMLEQ-NLYDFLKQNKfsPLPLKYIRPILQQVLTALLKLK-SLGLIHADLKPENIMLvdpvRQPYRVKVIDFGSASH 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 567218350 217 MTNTagLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGkFPYLPPDQE 273
Cdd:cd14211  155 VSKA--VCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLG-WPLYPGSSE 208
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
71-273 3.29e-16

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: 78.53  E-value: 3.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  71 DMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEA----IRKSIAQELKiNQSSQCPYLVNSYQSFYDNGAISLILE 146
Cdd:cd14229    3 EVLDFLGRGTFGQVVKCWKRGTNEIVAVKILKNHPSYArqgqIEVGILARLS-NENADEFNFVRAYECFQHRNHTCLVFE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 147 YMDGgSLADFLKSVK--TIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLL----INHRGEVKITDFGVSTVMTNT 220
Cdd:cd14229   82 MLEQ-NLYDFLKQNKfsPLPLKVIRPILQQVATALKKLK-SLGLIHADLKPENIMlvdpVRQPYRVKVIDFGSASHVSKT 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 567218350 221 agLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGkFPYLPPDQE 273
Cdd:cd14229  160 --VCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLG-WPLYPGALE 209
PK_NRBP1_like cd13984
Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The ...
144-330 4.64e-16

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: 76.81  E-value: 4.64e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 144 ILEYMDGGSLADFLKSV----KTIPESYLSAIFKQVLQGLIYLHH-DKHIIHRDLKPSNLLINHRGEVKITDFgVSTVMT 218
Cdd:cd13984   77 ITEYMSSGSLKQFLKKTkknhKTMNEKSWKRWCTQILSALSYLHScDPPIIHGNLTCDTIFIQHNGLIKIGSV-APDAIH 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 219 NTAGLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATgkfPYLPPDQEETWSSVFELMEAIVDQPppalpsen 298
Cdd:cd13984  156 NHVKTCREEHRNLHFFAPEYGYLEDVTTAVDIYSFGMCALEMAA---LEIQSNGEKVSANEEAIIRAIFSLE-------- 224
                        170       180       190
                 ....*....|....*....|....*....|..
gi 567218350 299 fSPELSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd13984  225 -DPLQKDFIRKCLSVAPQDRPSARDLLFHPVL 255
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
74-321 4.69e-16

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: 77.52  E-value: 4.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLVqhKWTGQFFALKVIqLNIDEAirkSIAQELKINQSSQCPYlvNSYQSFY-----DNGAIS---LIL 145
Cdd:cd14144    1 RSVGKGRYGEVWKG--KWRGEKVAVKIF-FTTEEA---SWFRETEIYQTVLMRH--ENILGFIaadikGTGSWTqlyLIT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 146 EYMDGGSLADFLKSVKTIPESYLSAIFKQVlQGLIYLHHD-------KHIIHRDLKPSNLLINHRGEVKITDFGVSTVM- 217
Cdd:cd14144   73 DYHENGSLYDFLRGNTLDTQSMLKLAYSAA-CGLAHLHTEifgtqgkPAIAHRDIKSKNILVKKNGTCCIADLGLAVKFi 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 218 --TNTAGLA-NTFVGTYNYMSPErIVGNKYGNKS-------DIWSLGLVVLE----CATG------KFPY---LPPDQEe 274
Cdd:cd14144  152 seTNEVDLPpNTRVGTKRYMAPE-VLDESLNRNHfdaykmaDMYSFGLVLWEiarrCISGgiveeyQLPYydaVPSDPS- 229
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 567218350 275 twssvFELMEAIV--DQPPPALPSENFSPE----LSSFISTCLQKDPNSRSSA 321
Cdd:cd14144  230 -----YEDMRRVVcvERRRPSIPNRWSSDEvlrtMSKLMSECWAHNPAARLTA 277
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
174-326 5.02e-16

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: 77.27  E-value: 5.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 174 QVLQGLIYLHHdKHIIHRDLKPSNLLI-----NHRGEVKITDFGVSTVMTNTAglANTFVGTYNYMSPERIVGN-KYGNK 247
Cdd:cd14000  120 QVADGLRYLHS-AMIIYRDLKSHNVLVwtlypNSAIIIKIADYGISRQCCRMG--AKGSEGTPGFRAPEIARGNvIYNEK 196
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 567218350 248 SDIWSLGLVVLECATGKFPYLppdQEETWSSVFELMEAIvdQPPPALPSENFSPELSSFISTCLQKDPNSRSSAKELME 326
Cdd:cd14000  197 VDVFSFGMLLYEILSGGAPMV---GHLKFPNEFDIHGGL--RPPLKQYECAPWPEVEVLMKKCWKENPQQRPTAVTVVS 270
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
141-338 5.67e-16

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: 78.21  E-value: 5.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 141 ISLILEYMDggslADFLKSVKT-IPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVmTN 219
Cdd:cd07874   97 VYLVMELMD----ANLCQVIQMeLDHERMSYLLYQMLCGIKHLH-SAGIIHRDLKPSNIVVKSDCTLKILDFGLART-AG 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 220 TAGLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFELM---------------- 283
Cdd:cd07874  171 TSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVIEQLgtpcpefmkklqptvr 250
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 567218350 284 EAIVDQP-------PPALPSENF----------SPELSSFISTCLQKDPNSRSSAKELMEHPFLNK-YNNSEI 338
Cdd:cd07874  251 NYVENRPkyagltfPKLFPDSLFpadsehnklkASQARDLLSKMLVIDPAKRISVDEALQHPYINVwYDPAEV 323
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
71-294 5.70e-16

Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and -Regulated Kinases 2 and 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of DYRK2 and DYRK3, and similar proteins. Drosophila DYRK2 interacts and phosphorylates the chromatin remodelling factor, SNR1 (Snf5-related 1), and also interacts with the essential chromatin component, trithorax. It may play a role in chromatin remodelling. Vertebrate DYRK2 phosphorylates and regulates the tumor suppressor p53 to induce apoptosis in response to DNA damage. It can also phosphorylate the transcription factor, nuclear factor of activated T cells (NFAT). DYRK2 is overexpressed in lung adenocarcinoma and esophageal carcinomas, and is a predictor for favorable prognosis in lung adenocarcinoma. DYRK3, also called regulatory erythroid kinase (REDK), is highly expressed in erythroid cells and the testis, and is also present in adult kidney and liver. It promotes cell survival by phosphorylating and activating SIRT1, an NAD(+)-dependent protein deacetylase, which promotes p53 deacetylation, resulting in the inhibition of apoptosis. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other S/T kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 78.25  E-value: 5.70e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  71 DMVKFLGKGSSG-VVQLVQHKwTGQFFALKVIQ------LNIDEAIRksIAQELKINQSSQCPYLVNSYQSFYDNGAISL 143
Cdd:cd14224   68 EVLKVIGKGSFGqVVKAYDHK-THQHVALKMVRnekrfhRQAAEEIR--ILEHLKKQDKDNTMNVIHMLESFTFRNHICM 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 144 ILEYMDGgSLADFLKSVKTIPESyLSAIFK---QVLQGLIYLHHDKhIIHRDLKPSNLLINHRGE--VKITDFGVSTVMT 218
Cdd:cd14224  145 TFELLSM-NLYELIKKNKFQGFS-LQLVRKfahSILQCLDALHRNK-IIHCDLKPENILLKQQGRsgIKVIDFGSSCYEH 221
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 567218350 219 NTAglaNTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGkFPYLPPDQEetwSSVFELMEAIVDQPPPAL 294
Cdd:cd14224  222 QRI---YTYIQSRFYRAPEVILGARYGMPIDMWSFGCILAELLTG-YPLFPGEDE---GDQLACMIELLGMPPQKL 290
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
68-318 6.55e-16

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: 76.83  E-value: 6.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  68 SDLDMVKFLGKGSSGVVQLVQHKWTGQ---FFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLI 144
Cdd:cd05066    4 SCIKIEKVIGAGEFGEVCSGRLKLPGKreiPVAIKTLKAGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTRSKPVMIV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 145 LEYMDGGSLADFLKSVK---TIPEsyLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTA 221
Cdd:cd05066   84 TEYMENGSLDAFLRKHDgqfTVIQ--LVGMLRGIASGMKYLS-DMGYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 222 GLANTFVG---TYNYMSPERIVGNKYGNKSDIWSLGLVVLEC-ATGKFPYLppdqEETWSSVFELMEAIVDQPPPAlpse 297
Cdd:cd05066  161 EAAYTTRGgkiPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVmSYGERPYW----EMSNQDVIKAIEEGYRLPAPM---- 232
                        250       260
                 ....*....|....*....|.
gi 567218350 298 NFSPELSSFISTCLQKDPNSR 318
Cdd:cd05066  233 DCPAALHQLMLDCWQKDRNER 253
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
71-273 6.91e-16

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: 77.82  E-value: 6.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  71 DMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEA----IRKSIAQELKINQSSQCPYlVNSYQSFYDNGAISLILE 146
Cdd:cd14228   18 EVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYArqgqIEVSILSRLSSENADEYNF-VRSYECFQHKNHTCLVFE 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 147 YMDGgSLADFLKSVK--TIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLL----INHRGEVKITDFGVSTVMTNt 220
Cdd:cd14228   97 MLEQ-NLYDFLKQNKfsPLPLKYIRPILQQVATALMKLK-SLGLIHADLKPENIMlvdpVRQPYRVKVIDFGSASHVSK- 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 567218350 221 aGLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGkFPYLPPDQE 273
Cdd:cd14228  174 -AVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLG-WPLYPGASE 224
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
141-329 7.15e-16

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


Pssm-ID: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 77.20  E-value: 7.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 141 ISLILEYMDGGSLADFLKSVKTIPESYLsaiFKQVLQGLIYLHhDKHIIHRDLKPSNLLINH-RGEVKITDFgvstvmtn 219
Cdd:cd14132   90 PSLIFEYVNNTDFKTLYPTLTDYDIRYY---MYELLKALDYCH-SKGIMHRDVKPHNIMIDHeKRKLRLIDW-------- 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 220 taGLA---------NTFVGTYNYMSPERIVGNKYGNKS-DIWSLGLVVLECATGKFPYLP----PDQEETWSSVF---EL 282
Cdd:cd14132  158 --GLAefyhpgqeyNVRVASRYYKGPELLVDYQYYDYSlDMWSLGCMLASMIFRKEPFFHghdnYDQLVKIAKVLgtdDL 235
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 283 MEaIVD----QPPPAL----------PSENF---------SPELSSFISTCLQKDPNSRSSAKELMEHPF 329
Cdd:cd14132  236 YA-YLDkygiELPPRLndilgrhskkPWERFvnsenqhlvTPEALDLLDKLLRYDHQERITAKEAMQHPY 304
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
143-322 7.73e-16

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: 77.02  E-value: 7.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 143 LILEYMDGGSLADFLKsVKTIPESYLSAIFKQVLQGLIYLHHDKH--------IIHRDLKPSNLLINHRGEVKITDFGVS 214
Cdd:cd14054   71 LVLEYAPKGSLCSYLR-ENTLDWMSSCRMALSLTRGLAYLHTDLRrgdqykpaIAHRDLNSRNVLVKADGSCVICDFGLA 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 215 TV------------MTNTAGLANtfVGTYNYMSPERIVG-------NKYGNKSDIWSLGLVVLECAT-------GKF--P 266
Cdd:cd14054  150 MVlrgsslvrgrpgAAENASISE--VGTLRYMAPEVLEGavnlrdcESALKQVDVYALGLVLWEIAMrcsdlypGESvpP 227
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 567218350 267 YLPPDQEETWSSV-FELMEAIVDQPP--PALPS--ENFSPELSSF---ISTCLQKDPNSRSSAK 322
Cdd:cd14054  228 YQMPYEAELGNHPtFEDMQLLVSREKarPKFPDawKENSLAVRSLketIEDCWDQDAEARLTAL 291
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
143-318 9.33e-16

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: 76.17  E-value: 9.33e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 143 LILEYMDGGSLADFLKSVKTIPESY-LSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTA 221
Cdd:cd05063   83 IITEYMENGALDKYLRDHDGEFSSYqLVGMLRGIAAGMKYLS-DMNYVHRDLAARNILVNSNLECKVSDFGLSRVLEDDP 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 222 GLANTFVG---TYNYMSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPYlppdqeetWS-SVFELMEAIVDQ---PPPA 293
Cdd:cd05063  162 EGTYTTSGgkiPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSfGERPY--------WDmSNHEVMKAINDGfrlPAPM 233
                        170       180
                 ....*....|....*....|....*.
gi 567218350 294 -LPSenfspELSSFISTCLQKDPNSR 318
Cdd:cd05063  234 dCPS-----AVYQLMLQCWQQDRARR 254
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
64-326 1.09e-15

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: 76.69  E-value: 1.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  64 ELSLSDLDMVKFLGKGSSGVV------QLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQS-SQCPYLVNSYQSFY 136
Cdd:cd05053    8 ELPRDRLTLGKPLGEGAFGQVvkaeavGLDNKPNEVVTVAVKMLKDDATEKDLSDLVSEMEMMKMiGKHKNIINLLGACT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 137 DNGAISLILEYMDGGSLADFLKSVKTIPESY----------------LSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLI 200
Cdd:cd05053   88 QDGPLYVVVEYASKGNLREFLRARRPPGEEAspddprvpeeqltqkdLVSFAYQVARGMEYLASKK-CIHRDLAARNVLV 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 201 NHRGEVKITDFGVSTVMTNTAGLANTFVG--TYNYMSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPYLPPDQEEtws 277
Cdd:cd05053  167 TEDNVMKIADFGLARDIHHIDYYRKTTNGrlPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEE--- 243
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 567218350 278 sVFELMEA--IVDQPPpalpseNFSPELSSFISTCLQKDPNSRSSAKELME 326
Cdd:cd05053  244 -LFKLLKEghRMEKPQ------NCTQELYMLMRDCWHEVPSQRPTFKQLVE 287
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
141-325 1.12e-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: 76.25  E-value: 1.12e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 141 ISLILEYMDGGSLADFLKSVKTIPE-SYLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTN 219
Cdd:cd14151   78 LAIVTQWCEGSSLYHHLHIIETKFEmIKLIDIARQTAQGMDYLHA-KSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSR 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 220 TAGLAN--TFVGTYNYMSPERIV---GNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEEtwsSVFELMEAIVDQPPPAL 294
Cdd:cd14151  157 WSGSHQfeQLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRD---QIIFMVGRGYLSPDLSK 233
                        170       180       190
                 ....*....|....*....|....*....|.
gi 567218350 295 PSENFSPELSSFISTCLQKDPNSRSSAKELM 325
Cdd:cd14151  234 VRSNCPKAMKRLMAECLKKKRDERPLFPQIL 264
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
138-326 2.87e-15

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: 75.77  E-value: 2.87e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 138 NGAISLILEYMDGGSLADFLKS-----------VKTIPESYLSaiFK-------QVLQGLIYLHhDKHIIHRDLKPSNLL 199
Cdd:cd05099   90 EGPLYVIVEYAAKGNLREFLRArrppgpdytfdITKVPEEQLS--FKdlvscayQVARGMEYLE-SRRCIHRDLAARNVL 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 200 INHRGEVKITDFGVSTVMTNTAGLANTFVGTY--NYMSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPYLPPDQEEtw 276
Cdd:cd05099  167 VTEDNVMKIADFGLARGVHDIDYYKKTSNGRLpvKWMAPEALFDRVYTHQSDVWSFGILMWEIFTlGGSPYPGIPVEE-- 244
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 567218350 277 ssVFELMEA--IVDQPPpalpseNFSPELSSFISTCLQKDPNSRSSAKELME 326
Cdd:cd05099  245 --LFKLLREghRMDKPS------NCTHELYMLMRECWHAVPTQRPTFKQLVE 288
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
72-266 3.12e-15

Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PRP4 phosphorylates a number of factors involved in the formation of active spliceosomes, which catalyze pre-mRNA splicing. It phosphorylates PRP6 and PRP31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), during spliceosomal complex formation. In fission yeast, PRP4 phosphorylates the splicing factor PRP1 (U5-102 kD in mammals). Thus, PRP4 plays a key role in regulating spliceosome assembly and pre-mRNA splicing. It also plays an important role in mitosis by acting as a spindle assembly checkpoint kinase that is required for chromosome alignment and the recruitment of the checkpoint proteins MPS1, MAD1, and MAD2 at kinetochores. The PRP4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 75.34  E-value: 3.12e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  72 MVKFLGKG-SSGVVQLVQHKWTGQFFALKVIQLNidEAIRKSIAQELKI---------NQSSQCPYLvnsYQSFYDNGAI 141
Cdd:cd14135    4 VYGYLGKGvFSNVVRARDLARGNQEVAIKIIRNN--ELMHKAGLKELEIlkklndadpDDKKHCIRL---LRHFEHKNHL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 142 SLILEYMDGgSLADFLK--------SVKTIpESYLsaifKQVLQGLIYLHHDKhIIHRDLKPSNLLINH-RGEVKITDFG 212
Cdd:cd14135   79 CLVFESLSM-NLREVLKkygknvglNIKAV-RSYA----QQLFLALKHLKKCN-ILHADIKPDNILVNEkKNTLKLCDFG 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 567218350 213 -VSTVMTN--TAGLANTFvgtynYMSPERIVGNKYGNKSDIWSLGLVVLECATGK--FP 266
Cdd:cd14135  152 sASDIGENeiTPYLVSRF-----YRAPEIILGLPYDYPIDMWSVGCTLYELYTGKilFP 205
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
71-273 3.52e-15

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: 75.90  E-value: 3.52e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  71 DMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEA----IRKSIAQELKiNQSSQCPYLVNSYQSFYDNGAISLILE 146
Cdd:cd14227   18 EVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYArqgqIEVSILARLS-TESADDYNFVRAYECFQHKNHTCLVFE 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 147 YMDGgSLADFLKSVK--TIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLI----NHRGEVKITDFGVSTVMTNt 220
Cdd:cd14227   97 MLEQ-NLYDFLKQNKfsPLPLKYIRPILQQVATALMKLK-SLGLIHADLKPENIMLvdpsRQPYRVKVIDFGSASHVSK- 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 567218350 221 aGLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGkFPYLPPDQE 273
Cdd:cd14227  174 -AVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLG-WPLYPGASE 224
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
64-326 3.81e-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: 75.05  E-value: 3.81e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  64 ELSLSDLDMVKFLGKGSSGvvQLVQHKWTG---------QFFALKVIQLNIDEAIRKSIAQELKINQS-SQCPYLVNSYQ 133
Cdd:cd05101   20 EFPRDKLTLGKPLGEGCFG--QVVMAEAVGidkdkpkeaVTVAVKMLKDDATEKDLSDLVSEMEMMKMiGKHKNIINLLG 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 134 SFYDNGAISLILEYMDGGSLADFLKS-----------VKTIPESYLSaiFK-------QVLQGLIYLHHDKhIIHRDLKP 195
Cdd:cd05101   98 ACTQDGPLYVIVEYASKGNLREYLRArrppgmeysydINRVPEEQMT--FKdlvsctyQLARGMEYLASQK-CIHRDLAA 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 196 SNLLINHRGEVKITDFGVSTVMTNTAGLANTFVGTY--NYMSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPYLPPDQ 272
Cdd:cd05101  175 RNVLVTENNVMKIADFGLARDINNIDYYKKTTNGRLpvKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTlGGSPYPGIPV 254
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 567218350 273 EEtwssVFELMEAIVDQPPPAlpseNFSPELSSFISTCLQKDPNSRSSAKELME 326
Cdd:cd05101  255 EE----LFKLLKEGHRMDKPA----NCTNELYMMMRDCWHAVPSQRPTFKQLVE 300
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
60-326 4.13e-15

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: 75.44  E-value: 4.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  60 PADD--ELSLSDLDMVKFLGKGSSGVVQL-----VQHKWTGQFFALKVIQLNiDEAIRKSIA---QELKINQS-SQCPYL 128
Cdd:cd05100    2 PADPkwELSRTRLTLGKPLGEGCFGQVVMaeaigIDKDKPNKPVTVAVKMLK-DDATDKDLSdlvSEMEMMKMiGKHKNI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 129 VNSYQSFYDNGAISLILEYMDGGSLADFLKSVK-----------TIPESYLSaiFK-------QVLQGLIYLHHDKhIIH 190
Cdd:cd05100   81 INLLGACTQDGPLYVLVEYASKGNLREYLRARRppgmdysfdtcKLPEEQLT--FKdlvscayQVARGMEYLASQK-CIH 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 191 RDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVGTY--NYMSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPY 267
Cdd:cd05100  158 RDLAARNVLVTEDNVMKIADFGLARDVHNIDYYKKTTNGRLpvKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPY 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 567218350 268 LPPDQEEtwssVFELMEAIVDQPPPAlpseNFSPELSSFISTCLQKDPNSRSSAKELME 326
Cdd:cd05100  238 PGIPVEE----LFKLLKEGHRMDKPA----NCTHELYMIMRECWHAVPSQRPTFKQLVE 288
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
97-324 4.55e-15

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: 74.83  E-value: 4.55e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  97 ALKVIQLNIDEAIRKSIAQELKI-NQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLADFLKSVKtipESYLS-----A 170
Cdd:cd05055   69 AVKMLKPTAHSSEREALMSELKImSHLGNHENIVNLLGACTIGGPILVITEYCCYGDLLNFLRRKR---ESFLTledllS 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 171 IFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVS-TVM--TNTAGLANTFVgTYNYMSPERIVGNKYGNK 247
Cdd:cd05055  146 FSYQVAKGMAFLA-SKNCIHRDLAARNVLLTHGKIVKICDFGLArDIMndSNYVVKGNARL-PVKWMAPESIFNCVYTFE 223
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 248 SDIWSLGLVVLECAT-GKFPY--LPPDqeetwSSVFELMEAIVDQPPPALPSEnfspELSSFISTCLQKDPNSRSSAKEL 324
Cdd:cd05055  224 SDVWSYGILLWEIFSlGSNPYpgMPVD-----SKFYKLIKEGYRMAQPEHAPA----EIYDIMKTCWDADPLKRPTFKQI 294
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
70-321 4.79e-15

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1b, also called Activin receptor-Like Kinase 6 (ALK6), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Mutations in BMPR1b that led to inhibition of chondrogenesis can cause Brachydactyly (BD) type A2, a dominant hand malformation characterized by shortening and lateral deviation of the index fingers. A point mutation in the BMPR1b kinase domain is also associated with the Booroola phenotype, characterized by precocious differentiation of ovarian follicles. BMPR1b belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1b, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271121 [Multi-domain]  Cd Length: 305  Bit Score: 74.70  E-value: 4.79e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  70 LDMVKFLGKGSSGVVQLvqHKWTGQFFALKVIqLNIDEA--IRKS-IAQELKINQSSQCPYLVNSYQSFYDNGAISLILE 146
Cdd:cd14219    7 IQMVKQIGKGRYGEVWM--GKWRGEKVAVKVF-FTTEEAswFRETeIYQTVLMRHENILGFIAADIKGTGSWTQLYLITD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 147 YMDGGSLADFLKSVKTIPESYLSAIFKQVlQGLIYLHHD-------KHIIHRDLKPSNLLINHRGEVKITDFGVSTVM-- 217
Cdd:cd14219   84 YHENGSLYDYLKSTTLDTKAMLKLAYSSV-SGLCHLHTEifstqgkPAIAHRDLKSKNILVKKNGTCCIADLGLAVKFis 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 218 -TNTAGLA-NTFVGTYNYMSPERIVGNKYGNK------SDIWSLGLVVLE----CATG------KFPY---LPPDQEetw 276
Cdd:cd14219  163 dTNEVDIPpNTRVGTKRYMPPEVLDESLNRNHfqsyimADMYSFGLILWEvarrCVSGgiveeyQLPYhdlVPSDPS--- 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 567218350 277 ssvFELMEAIV--DQPPPALPSENFSPE----LSSFISTCLQKDPNSRSSA 321
Cdd:cd14219  240 ---YEDMREIVciKRLRPSFPNRWSSDEclrqMGKLMTECWAHNPASRLTA 287
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
129-326 5.19e-15

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: 75.04  E-value: 5.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 129 VNSYQSFYDNG-----AISLILEymDGGSLADFLKSVKTIpESYLSAIFkQVLQGLIYLHHDKhIIHRDLKPSNLLINHR 203
Cdd:cd14207  142 VTSSESFASSGfqedkSLSDVEE--EEEDSGDFYKRPLTM-EDLISYSF-QVARGMEFLSSRK-CIHRDLAARNILLSEN 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 204 GEVKITDFGVST--------VMTNTAGLAntfvgtYNYMSPERIVGNKYGNKSDIWSLGLVVLEC-ATGKFPYLPPDQEE 274
Cdd:cd14207  217 NVVKICDFGLARdiyknpdyVRKGDARLP------LKWMAPESIFDKIYSTKSDVWSYGVLLWEIfSLGASPYPGVQIDE 290
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 567218350 275 TWSSvfELMEAIVDQPPpalpsENFSPELSSFISTCLQKDPNSRSSAKELME 326
Cdd:cd14207  291 DFCS--KLKEGIRMRAP-----EFATSEIYQIMLDCWQGDPNERPRFSELVE 335
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
143-327 6.01e-15

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: 74.23  E-value: 6.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 143 LILEYMDGGSLADFLKSVKTIPESYL----SAIfkqvlQGLIYLH------HDK-HIIHRDLKPSNLLINHRGEVKITDF 211
Cdd:cd14056   70 LITEYHEHGSLYDYLQRNTLDTEEALrlaySAA-----SGLAHLHteivgtQGKpAIAHRDLKSKNILVKRDGTCCIADL 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 212 GVSTVMTNTAGL----ANTFVGTYNYMSPERIVGNKYGN------KSDIWSLGLVVLE----CATGKFP--YLPPDQEET 275
Cdd:cd14056  145 GLAVRYDSDTNTidipPNPRVGTKRYMAPEVLDDSINPKsfesfkMADIYSFGLVLWEiarrCEIGGIAeeYQLPYFGMV 224
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 567218350 276 WSS-VFELMEAIV------DQPPPALPSENFSPELSSFISTCLQKDPNSRSSA----KELMEH 327
Cdd:cd14056  225 PSDpSFEEMRKVVcveklrPPIPNRWKSDPVLRSMVKLMQECWSENPHARLTAlrvkKTLAKL 287
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
108-324 6.28e-15

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: 74.28  E-value: 6.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 108 AIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLADFLKS--------VKTIPE--------SYLSAI 171
Cdd:cd05094   49 AARKDFQREAELLTNLQHDHIVKFYGVCGDGDPLIMVFEYMKHGDLNKFLRAhgpdamilVDGQPRqakgelglSQMLHI 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 172 FKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVS--TVMTNTAGLANTFVGTYNYMSPERIVGNKYGNKSD 249
Cdd:cd05094  129 ATQIASGMVYLA-SQHFVHRDLATRNCLVGANLLVKIGDFGMSrdVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESD 207
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 567218350 250 IWSLGLVVLECAT-GKFPYLPPDQEETWSSVfelMEAIVDQPPPALPSENFSPELSsfistCLQKDPNSRSSAKEL 324
Cdd:cd05094  208 VWSFGVILWEIFTyGKQPWFQLSNTEVIECI---TQGRVLERPRVCPKEVYDIMLG-----CWQREPQQRLNIKEI 275
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
76-292 7.73e-15

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: 74.59  E-value: 7.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVI--------QLNIDEAIRKSIAQELKINQSSqcpYLVNSYQSFYDNGAISLILEy 147
Cdd:cd14212    7 LGQGTFGQVVKCQDLKTNKLVAVKVLknkpayfrQAMLEIAILTLLNTKYDPEDKH---HIVRLLDHFMHHGHLCIVFE- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 148 MDGGSLADFLKSV--KTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLI--NHRGEVKITDFGvstvmtnTAGL 223
Cdd:cd14212   83 LLGVNLYELLKQNqfRGLSLQLIRKFLQQLLDALSVLK-DARIIHCDLKPENILLvnLDSPEIKLIDFG-------SACF 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 567218350 224 ANTFVGTY----NYMSPERIVGNKYGNKSDIWSLGLVVLECATGkFPYLPPDQEetwssvFELMEAIVDQ--PPP 292
Cdd:cd14212  155 ENYTLYTYiqsrFYRSPEVLLGLPYSTAIDMWSLGCIAAELFLG-LPLFPGNSE------YNQLSRIIEMlgMPP 222
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
76-324 8.18e-15

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: 73.87  E-value: 8.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQ----HKWTGQFFAL------------KVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNG 139
Cdd:cd05095   13 LGEGQFGEVHLCEaegmEKFMDKDFALevsenqpvlvavKMLRADANKNARNDFLKEIKIMSRLKDPNIIRLLAVCITDD 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 140 AISLILEYMDGGSLADFLK------------SVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVK 207
Cdd:cd05095   93 PLCMITEYMENGDLNQFLSrqqpegqlalpsNALTVSYSDLRFMAAQIASGMKYLS-SLNFVHRDLATRNCLVGKNYTIK 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 208 ITDFGVSTvmtntaglaNTFVGTY-----------NYMSPERIVGNKYGNKSDIWSLGLVVLECAT--GKFPYLPPDQEE 274
Cdd:cd05095  172 IADFGMSR---------NLYSGDYyriqgravlpiRWMSWESILLGKFTTASDVWAFGVTLWETLTfcREQPYSQLSDEQ 242
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 567218350 275 TWSSVFELMEaivDQPPPA-LPSENFSPE-LSSFISTCLQKDPNSRSSAKEL 324
Cdd:cd05095  243 VIENTGEFFR---DQGRQTyLPQPALCPDsVYKLMLSCWRRDTKDRPSFQEI 291
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
141-336 9.75e-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: 73.57  E-value: 9.75e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 141 ISLILEYMDGGSLADFLK--SVKTIPESYLSAIFKQVLQGLIYLHHDKHIiHRDLKPSNLLINHRGEVKITDFGVSTVMT 218
Cdd:cd05071   78 IYIVTEYMSKGSLLDFLKgeMGKYLRLPQLVDMAAQIASGMAYVERMNYV-HRDLRAANILVGENLVCKVADFGLARLIE 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 219 N---TAGLANTFvgTYNYMSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPYLPPDQEEtwssVFELMEAIVDQP-PPA 293
Cdd:cd05071  157 DneyTARQGAKF--PIKWTAPEAALYGRFTIKSDVWSFGILLTELTTkGRVPYPGMVNRE----VLDQVERGYRMPcPPE 230
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 567218350 294 LPSenfspELSSFISTCLQKDPNSRSSAKELmeHPFLNKYNNS 336
Cdd:cd05071  231 CPE-----SLHDLMCQCWRKEPEERPTFEYL--QAFLEDYFTS 266
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
141-267 1.19e-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: 73.14  E-value: 1.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 141 ISLILEYMDGGSLADFLKSVK--TIPESYLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMT 218
Cdd:cd05073   80 IYIITEFMAKGSLLDFLKSDEgsKQPLPKLIDFSAQIAEGMAFIEQ-RNYIHRDLRAANILVSASLVCKIADFGLARVIE 158
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 567218350 219 NTAGLANTFVG-TYNYMSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPY 267
Cdd:cd05073  159 DNEYTAREGAKfPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTyGRIPY 209
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
76-328 1.31e-14

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: 73.13  E-value: 1.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALK----VIQLNIDE--AIRKSIAQELKinqsSQCPYLVNSYQSFYDNGAISLILEYMD 149
Cdd:cd14138   13 IGSGEFGSVFKCVKRLDGCIYAIKrskkPLAGSVDEqnALREVYAHAVL----GQHSHVVRYYSAWAEDDHMLIQNEYCN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 150 GGSLADFL----KSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHR-----------------GEV-- 206
Cdd:cd14138   89 GGSLADAIsenyRIMSYFTEPELKDLLLQVARGLKYIH-SMSLVHMDIKPSNIFISRTsipnaaseegdedewasNKVif 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 207 KITDFGVSTVMTNtaglANTFVGTYNYMSPErIVGNKYGN--KSDIWSLGLVVLeCATGKFPYlpPDQEETWSsvfELME 284
Cdd:cd14138  168 KIGDLGHVTRVSS----PQVEEGDSRFLANE-VLQENYTHlpKADIFALALTVV-CAAGAEPL--PTNGDQWH---EIRQ 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 567218350 285 AIVDQPPPALpsenfSPELSSFISTCLQKDPNSRSSAKELMEHP 328
Cdd:cd14138  237 GKLPRIPQVL-----SQEFLDLLKVMIHPDPERRPSAVALVKHS 275
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
34-259 1.60e-14

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 73.76  E-value: 1.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  34 DGDLRVNKDGVRI-VSQSEPEVLSPIKPADDELSLS-DLDMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQlnideaiRK 111
Cdd:PHA03209  30 DGDLEYSDDDSASeSDDDDDDGLIPTKQKAREVVASlGYTVIKTLTPGSEGRVFVATKPGQPDPVVLKIGQ-------KG 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 112 SIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGgSLADFL-KSVKTIPESYLSAIFKQVLQGLIYLHHDKhIIH 190
Cdd:PHA03209 103 TTLIEAMLLQNVNHPSVIRMKDTLVSGAITCMVLPHYSS-DLYTYLtKRSRPLPIDQALIIEKQILEGLRYLHAQR-IIH 180
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 567218350 191 RDLKPSNLLINHRGEVKITDFGVS---TVMTNTAGLAntfvGTYNYMSPERIVGNKYGNKSDIWSLGLVVLE 259
Cdd:PHA03209 181 RDVKTENIFINDVDQVCIGDLGAAqfpVVAPAFLGLA----GTVETNAPEVLARDKYNSKADIWSAGIVLFE 248
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
131-315 1.72e-14

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: 73.93  E-value: 1.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 131 SYQSFYDngaISLILEYMDggslADFLKSVKT-IPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKIT 209
Cdd:cd07875   97 SLEEFQD---VYIVMELMD----ANLCQVIQMeLDHERMSYLLYQMLCGIKHLH-SAGIIHRDLKPSNIVVKSDCTLKIL 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 210 DFGVSTVmTNTAGLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFELMeaivdq 289
Cdd:cd07875  169 DFGLART-AGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGVLFPGTDHIDQWNKVIEQL------ 241
                        170       180
                 ....*....|....*....|....*.
gi 567218350 290 pppALPSENFSPELSSFISTCLQKDP 315
Cdd:cd07875  242 ---GTPCPEFMKKLQPTVRTYVENRP 264
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
143-324 1.94e-14

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: 72.40  E-value: 1.94e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 143 LILEYMDGGSLADFLKSvktiPESYLSAI-----FKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVM 217
Cdd:cd05033   82 IVTEYMENGSLDKFLRE----NDGKFTVTqlvgmLRGIASGMKYLS-EMNYVHRDLAARNILVNSDLVCKVSDFGLSRRL 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 218 TNTAGLANTFVG--TYNYMSPERIVGNKYGNKSDIWSLGLVVLE-CATGKFPYlppdqeETWSSVfELMEAIVD----QP 290
Cdd:cd05033  157 EDSEATYTTKGGkiPIRWTAPEAIAYRKFTSASDVWSFGIVMWEvMSYGERPY------WDMSNQ-DVIKAVEDgyrlPP 229
                        170       180       190
                 ....*....|....*....|....*....|....
gi 567218350 291 PPALPSenfspELSSFISTCLQKDPNSRSSAKEL 324
Cdd:cd05033  230 PMDCPS-----ALYQLMLDCWQKDRNERPTFSQI 258
STKc_SRPK3 cd14218
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs ...
72-330 2.16e-14

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK3 is highly expressed in the heart and skeletal muscles, and is controlled by a muscle-specific enhancer that is regulated by MEF2. It may play an important role in muscle development. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271120 [Multi-domain]  Cd Length: 365  Bit Score: 73.51  E-value: 2.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  72 MVKFLGKGSSGVVQLVQHKWTGQFFALKVI-------QLNIDE-----AIRKSIAQELKINQSSQcpyLVNSYQSFYDNG 139
Cdd:cd14218   14 VVRKLGWGHFSTVWLCWDIQRKRFVALKVVksavhytETAVDEikllkCVRDSDPSDPKRETIVQ---LIDDFKISGVNG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 140 A-ISLILEYMDGGSLADFLKS-VKTIPESYLSAIFKQVLQGLIYLHHDKHIIHRDLKPSNLLIN-HRGEVK--------- 207
Cdd:cd14218   91 VhVCMVLEVLGHQLLKWIIKSnYQGLPLPCVKSILRQVLQGLDYLHTKCKIIHTDIKPENILMCvDEGYVRrlaaeatiw 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 208 -----------ITDFGVSTVMTN-------------TAGLANTF---------VGTYNYMSPERIVGNKYGNKSDIWSLG 254
Cdd:cd14218  171 qqagapppsgsSVSFGASDFLVNplepqnadkirvkIADLGNACwvhkhftedIQTRQYRALEVLIGAEYGTPADIWSTA 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 255 LVVLECATGKFPYLP---PDQEETWSSVFELMEAIVDQPPPALPSENFSPE----------------------------- 302
Cdd:cd14218  251 CMAFELATGDYLFEPhsgEDYTRDEDHIAHIVELLGDIPPHFALSGRYSREyfnrrgelrhiknlkhwglyevlvekyew 330
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 567218350 303 -------LSSFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14218  331 pleqaaqFTDFLLPMMEFLPEKRATAAQCLQHPWL 365
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
143-326 2.63e-14

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


Pssm-ID: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 72.41  E-value: 2.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 143 LILEYMDGGSLADFLKSvKTIPESYLSAIFKQVLQGLIYLHHDKH--------IIHRDLKPSNLLINHRGEVKITDFGVS 214
Cdd:cd14055   76 LITAYHENGSLQDYLTR-HILSWEDLCKMAGSLARGLAHLHSDRTpcgrpkipIAHRDLKSSNILVKNDGTCVLADFGLA 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 215 TVMTNTAG---LANTF-VGTYNYMSPE----RIvgNKYGNKS----DIWSLGLVVLE----C-ATGKF-PYLPPDQEETW 276
Cdd:cd14055  155 LRLDPSLSvdeLANSGqVGTARYMAPEalesRV--NLEDLESfkqiDVYSMALVLWEmasrCeASGEVkPYELPFGSKVR 232
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 567218350 277 SS-VFELMEAIV--DQPPPALPSENFSPELSSFIST----CLQKDPNSRSSAKELME 326
Cdd:cd14055  233 ERpCVESMKDLVlrDRGRPEIPDSWLTHQGMCVLCDtiteCWDHDPEARLTASCVAE 289
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
71-257 2.70e-14

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: 72.97  E-value: 2.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  71 DMVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAI-----------------------------RKSIAQELKINQ 121
Cdd:cd13977    3 SLIREVGRGSYGVVYEAVVRRTGARVAVKKIRCNAPENVelalrefwalssiqrqhpnviqleecvlqRDGLAQRMSHGS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 122 SSQCPYLVNSYQSFydNGAISL----------ILEYMDGGSLADFLKSVKtiPESYLSAIFKQVLQGLIYLHHDKHIIHR 191
Cdd:cd13977   83 SKSDLYLLLVETSL--KGERCFdprsacylwfVMEFCDGGDMNEYLLSRR--PDRQTNTSFMLQLSSALAFLHRNQIVHR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 192 DLKPSNLLINH-RGE--VKITDFGVSTVMT----NTAGLAN-------TFVGTYNYMSPERIVGNkYGNKSDIWSLGLVV 257
Cdd:cd13977  159 DLKPDNILISHkRGEpiLKVADFGLSKVCSgsglNPEEPANvnkhflsSACGSDFYMAPEVWEGH-YTAKADIFALGIII 237
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
141-333 2.74e-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: 72.41  E-value: 2.74e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 141 ISLILEYMDGGSLADFLKSV--KTIPESYLSAIFKQVLQGLIYLHHDKHIiHRDLKPSNLLINHRGEVKITDFGVSTVMT 218
Cdd:cd05069   81 IYIVTEFMGKGSLLDFLKEGdgKYLKLPQLVDMAAQIADGMAYIERMNYI-HRDLRAANILVGDNLVCKIADFGLARLIE 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 219 N---TAGLANTFvgTYNYMSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPYLPPDQEEtwssVFELMEAIVDQPPPAL 294
Cdd:cd05069  160 DneyTARQGAKF--PIKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMVNRE----VLEQVERGYRMPCPQG 233
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 567218350 295 PSENfspeLSSFISTCLQKDPNSRSSAKELmeHPFLNKY 333
Cdd:cd05069  234 CPES----LHELMKLCWKKDPDERPTFEYI--QSFLEDY 266
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
143-321 3.46e-14

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: 71.98  E-value: 3.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 143 LILEYMDGGSLADFLKSvKTIPESYLSAIFKQVLQGLIYLHHD---------KHIIHRDLKPSNLLINHRGEVKITDFGV 213
Cdd:cd14053   70 LITEFHERGSLCDYLKG-NVISWNELCKIAESMARGLAYLHEDipatngghkPSIAHRDFKSKNVLLKSDLTACIADFGL 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 214 STVMTNTAGLANTF--VGTYNYMSPERIVGNKYGNKS-----DIWSLGLVVLE------CATGKFP-YLPPDQEETWS-- 277
Cdd:cd14053  149 ALKFEPGKSCGDTHgqVGTRRYMAPEVLEGAINFTRDaflriDMYAMGLVLWEllsrcsVHDGPVDeYQLPFEEEVGQhp 228
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 567218350 278 SVFELMEAIVDQP--PPALPSENFSPELSSFIST---CLQKDPNSRSSA 321
Cdd:cd14053  229 TLEDMQECVVHKKlrPQIRDEWRKHPGLAQLCETieeCWDHDAEARLSA 277
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
69-318 3.83e-14

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: 71.82  E-value: 3.83e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  69 DLDMVKF---LGKGSSGVVQLVQHKWTG---QFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAIS 142
Cdd:cd05065    2 DVSCVKIeevIGAGEFGEVCRGRLKLPGkreIFVAIKTLKSGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTKSRPVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 143 LILEYMDGGSLADFLK-SVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVM---- 217
Cdd:cd05065   82 IITEFMENGALDSFLRqNDGQFTVIQLVGMLRGIAAGMKYLS-EMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLeddt 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 218 ---TNTAGLANTFvgTYNYMSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPYlppdqeetWS-SVFELMEAIvDQ--- 289
Cdd:cd05065  161 sdpTYTSSLGGKI--PIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSyGERPY--------WDmSNQDVINAI-EQdyr 229
                        250       260       270
                 ....*....|....*....|....*....|.
gi 567218350 290 --PPPALPSenfspELSSFISTCLQKDPNSR 318
Cdd:cd05065  230 lpPPMDCPT-----ALHQLMLDCWQKDRNLR 255
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
96-266 5.64e-14

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: 71.40  E-value: 5.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  96 FALKVIQLNID---EAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLADFLK-SVKTIPESYLSAI 171
Cdd:cd14159   19 YAVKRLKEDSEldwSVVKNSFLTEVEKLSRFRHPNIVDLAGYSAQQGNYCLIYVYLPNGSLEDRLHcQVSCPCLSWSQRL 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 172 fkQVLQG----LIYLHHDK-HIIHRDLKPSNLLINHRGEVKITDFGV--------STVMTNTAGLANTFVGTYNYMSPER 238
Cdd:cd14159   99 --HVLLGtaraIQYLHSDSpSLIHGDVKSSNILLDAALNPKLGDFGLarfsrrpkQPGMSSTLARTQTVRGTLAYLPEEY 176
                        170       180
                 ....*....|....*....|....*...
gi 567218350 239 IVGNKYGNKSDIWSLGLVVLECATGKFP 266
Cdd:cd14159  177 VKTGTLSVEIDVYSFGVVLLELLTGRRA 204
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
64-326 6.12e-14

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: 71.54  E-value: 6.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  64 ELSLSDLDMVKFLGKGSSGVVQ--LVQHKWTGQF---FALKVIqlNIDEAIRKSIA--QELKINQSSQCPYLVNSYQSFY 136
Cdd:cd05061    2 EVSREKITLLRELGQGSFGMVYegNARDIIKGEAetrVAVKTV--NESASLRERIEflNEASVMKGFTCHHVVRLLGVVS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 137 DNGAISLILEYMDGGSLADFLKSVKTIPES---YLSAIFKQVLQ-------GLIYLHHDKhIIHRDLKPSNLLINHRGEV 206
Cdd:cd05061   80 KGQPTLVVMELMAHGDLKSYLRSLRPEAENnpgRPPPTLQEMIQmaaeiadGMAYLNAKK-FVHRDLAARNCMVAHDFTV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 207 KITDFGVSTVMTNTAGLANTFVGTY--NYMSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPYLPPDQEETWSSVFElm 283
Cdd:cd05061  159 KIGDFGMTRDIYETDYYRKGGKGLLpvRWMAPESLKDGVFTTSSDMWSFGVVLWEITSlAEQPYQGLSNEQVLKFVMD-- 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 567218350 284 EAIVDQPppalpsENFSPELSSFISTCLQKDPNSRSSAKELME 326
Cdd:cd05061  237 GGYLDQP------DNCPERVTDLMRMCWQFNPKMRPTFLEIVN 273
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
73-267 8.63e-14

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


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 70.36  E-value: 8.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  73 VKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKinQSSQCPYLVNsyqsFYDNG--------AISLI 144
Cdd:cd14017    5 VKKIGGGGFGEIYKVRDVVDGEEVAMKVESKSQPKQVLKMEVAVLK--KLQGKPHFCR----LIGCGrterynyiVMTLL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 145 leymdGGSLADFLKSVK--TIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLInHRGEVK-----ITDFGVSTVM 217
Cdd:cd14017   79 -----GPNLAELRRSQPrgKFSVSTTLRLGIQILKAIEDIH-EVGFLHRDVKPSNFAI-GRGPSDertvyILDFGLARQY 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 567218350 218 TNTAGLANT-------FVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPY 267
Cdd:cd14017  152 TNKDGEVERpprnaagFRGTVRYASVNAHRNKEQGRRDDLWSWFYMLIEFVTGQLPW 208
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
74-321 8.81e-14

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: 70.84  E-value: 8.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVQLvqHKWTGQFFALKVIqLNIDEA--IRKS-IAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDG 150
Cdd:cd14220    1 RQIGKGRYGEVWM--GKWRGEKVAVKVF-FTTEEAswFRETeIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHEN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 151 GSLADFLKSVKTIPESYLSAIFKQVLqGLIYLHHDKH-------IIHRDLKPSNLLINHRGEVKITDFGVSTVM---TNT 220
Cdd:cd14220   78 GSLYDFLKCTTLDTRALLKLAYSAAC-GLCHLHTEIYgtqgkpaIAHRDLKSKNILIKKNGTCCIADLGLAVKFnsdTNE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 221 AGLA-NTFVGTYNYMSPEriVGNKYGNK--------SDIWSLGLVVLE----CATG------KFPY---LPPDQEetwss 278
Cdd:cd14220  157 VDVPlNTRVGTKRYMAPE--VLDESLNKnhfqayimADIYSFGLIIWEmarrCVTGgiveeyQLPYydmVPSDPS----- 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 567218350 279 vFELMEAIV--DQPPPALPSENFSPE----LSSFISTCLQKDPNSRSSA 321
Cdd:cd14220  230 -YEDMREVVcvKRLRPTVSNRWNSDEclraVLKLMSECWAHNPASRLTA 277
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
73-267 9.21e-14

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: 70.72  E-value: 9.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  73 VKFLGKGSSGVVQLVQHK-WTGQFfALKVIQLN--IDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMD 149
Cdd:cd14026    2 LRYLSRGAFGTVSRARHAdWRVTV-AIKCLKLDspVGDSERNCLLKEAEILHKARFSYILPILGICNEPEFLGIVTEYMT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 150 GGSLADFLKSVKTIPESYLS---AIFKQVLQGLIYLHH-DKHIIHRDLKPSNLLINHRGEVKITDFGVST--VMTNTAGL 223
Cdd:cd14026   81 NGSLNELLHEKDIYPDVAWPlrlRILYEIALGVNYLHNmSPPLLHHDLKTQNILLDGEFHVKIADFGLSKwrQLSISQSR 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 567218350 224 ANTFV---GTYNYMSPERIVGNKYGN---KSDIWSLGLVVLECATGKFPY 267
Cdd:cd14026  161 SSKSApegGTIIYMPPEEYEPSQKRRasvKHDIYSYAIIMWEVLSRKIPF 210
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
128-326 9.95e-14

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: 70.81  E-value: 9.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 128 LVNSYQSFYDNGAISLILEYMDGGSLADFLKSVK-----------TIPESYLS-----AIFKQVLQGLIYLHhDKHIIHR 191
Cdd:cd05098   81 IINLLGACTQDGPLYVIVEYASKGNLREYLQARRppgmeycynpsHNPEEQLSskdlvSCAYQVARGMEYLA-SKKCIHR 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 192 DLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVGTY--NYMSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPYL 268
Cdd:cd05098  160 DLAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRLpvKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTlGGSPYP 239
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 269 PPDQEEtwssVFELMEA--IVDQPppalpsENFSPELSSFISTCLQKDPNSRSSAKELME 326
Cdd:cd05098  240 GVPVEE----LFKLLKEghRMDKP------SNCTNELYMMMRDCWHAVPSQRPTFKQLVE 289
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
71-330 1.06e-13

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK1 plays a role in neuronal differentiation. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 71.04  E-value: 1.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  71 DMVKFLGKGSSG-VVQLVQHKWTGQFFALKVIQlNID---EAIRKSIA--QELKINQSSQCPYLVNSYQSFYDNGAISLI 144
Cdd:cd14213   15 EIVDTLGEGAFGkVVECIDHKMGGMHVAVKIVK-NVDryrEAARSEIQvlEHLNTTDPNSTFRCVQMLEWFDHHGHVCIV 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 145 LEYMdGGSLADFLK--SVKTIPESYLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLINH------------RGE----- 205
Cdd:cd14213   94 FELL-GLSTYDFIKenSFLPFPIDHIRNMAYQICKSVNFLHHNK-LTHTDLKPENILFVQsdyvvkynpkmkRDErtlkn 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 206 --VKITDFGVSTVMTNTAglaNTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETwssvFELM 283
Cdd:cd14213  172 pdIKVVDFGSATYDDEHH---STLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFQTHDSKEH----LAMM 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 284 EAIVDQPPPAL--------------------------------PSENF-------SPELSSFISTCLQKDPNSRSSAKEL 324
Cdd:cd14213  245 ERILGPLPKHMiqktrkrkyfhhdqldwdehssagryvrrrckPLKEFmlsqdvdHEQLFDLIQKMLEYDPAKRITLDEA 324

                 ....*.
gi 567218350 325 MEHPFL 330
Cdd:cd14213  325 LKHPFF 330
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
76-327 1.08e-13

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: 70.20  E-value: 1.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNideAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLAD 155
Cdd:cd14155    1 IGSGFFSEVYKVRHRTSGQVMALKMNTLS---SNRANMLREVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGGNLEQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 156 FLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRG---EVKITDFGVSTVMTNTA--GLANTFVGT 230
Cdd:cd14155   78 LLDSNEPLSWTVRVKLALDIARGLSYLH-SKGIFHRDLTSKNCLIKRDEngyTAVVGDFGLAEKIPDYSdgKEKLAVVGS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 231 YNYMSPERIVGNKYGNKSDIWSLGLVVLECaTGKFPYLP---PDQEETWSSVFELMEAIVDQPPPALpsenfspelsSFI 307
Cdd:cd14155  157 PYWMAPEVLRGEPYNEKADVFSYGIILCEI-IARIQADPdylPRTEDFGLDYDAFQHMVGDCPPDFL----------QLA 225
                        250       260
                 ....*....|....*....|
gi 567218350 308 STCLQKDPNSRSSAKELMEH 327
Cdd:cd14155  226 FNCCNMDPKSRPSFHDIVKT 245
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
70-326 1.22e-13

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: 70.34  E-value: 1.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  70 LDMVKFLGKGSSGVVQLVQHK----WTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNG--AISL 143
Cdd:cd05079    6 LKRIRDLGEGHFGKVELCRYDpegdNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGgnGIKL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 144 ILEYMDGGSLADFL-KSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAG 222
Cdd:cd05079   86 IMEFLPSGSLKEYLpRNKNKINLKQQLKYAVQICKGMDYLG-SRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKE 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 223 ---LANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLE----CATGKFP---YL----PPDQEETWSSVFELMEAIVD 288
Cdd:cd05079  165 yytVKDDLDSPVFWYAPECLIQSKFYIASDVWSFGVTLYElltyCDSESSPmtlFLkmigPTHGQMTVTRLVRVLEEGKR 244
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 567218350 289 QPPPAlpseNFSPELSSFISTCLQKDPNSRSSAKELME 326
Cdd:cd05079  245 LPRPP----NCPEEVYQLMRKCWEFQPSKRTTFQNLIE 278
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
69-325 1.78e-13

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: 69.69  E-value: 1.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  69 DLDMVKFLGKGSSGVVqlvqHK--WTGQFfALKVIQLNI--DEAIrKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLI 144
Cdd:cd14063    1 ELEIKEVIGKGRFGRV----HRgrWHGDV-AIKLLNIDYlnEEQL-EAFKEEVAAYKNTRHDNLVLFMGACMDPPHLAIV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 145 LEYMDGGSLADFLKSVKT-IPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHrGEVKITDFGVSTV--MTNTA 221
Cdd:cd14063   75 TSLCKGRTLYSLIHERKEkFDFNKTVQIAQQICQGMGYLH-AKGIIHKDLKSKNIFLEN-GRVVITDFGLFSLsgLLQPG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 222 GLANTFVGTYN---YMSPErIVGN-----------KYGNKSDIWSLGLVVLECATGKFPY--LPPDqeetwSSVFELMEA 285
Cdd:cd14063  153 RREDTLVIPNGwlcYLAPE-IIRAlspdldfeeslPFTKASDVYAFGTVWYELLAGRWPFkeQPAE-----SIIWQVGCG 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 567218350 286 IvdQPPPALPSenFSPELSSFISTCLQKDPNSRSSAKELM 325
Cdd:cd14063  227 K--KQSLSQLD--IGREVKDILMQCWAYDPEKRPTFSDLL 262
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
70-321 2.12e-13

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: 69.78  E-value: 2.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  70 LDMVKFLGKGSSGVVQLVQhkWTGQFFALKVIQlNIDEairKSIAQELKI------NQSSQCPYLVNSYQSFYDNGAISL 143
Cdd:cd14142    7 ITLVECIGKGRYGEVWRGQ--WQGESVAVKIFS-SRDE---KSWFRETEIyntvllRHENILGFIASDMTSRNSCTQLWL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 144 ILEYMDGGSLADFLKSVKTIPESYLsAIFKQVLQGLIYLHHD-------KHIIHRDLKPSNLLINHRGEVKITDFGVS-- 214
Cdd:cd14142   81 ITHYHENGSLYDYLQRTTLDHQEML-RLALSAASGLVHLHTEifgtqgkPAIAHRDLKSKNILVKSNGQCCIADLGLAvt 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 215 -TVMTNTAGLA-NTFVGTYNYMSPE------RIVGNKYGNKSDIWSLGLVVLE----CATGKF--PYLPPDQEETWSS-V 279
Cdd:cd14142  160 hSQETNQLDVGnNPRVGTKRYMAPEvldetiNTDCFESYKRVDIYAFGLVLWEvarrCVSGGIveEYKPPFYDVVPSDpS 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 567218350 280 FELMEAIV--DQPPPALPSENFS-PELSSF---ISTCLQKDPNSRSSA 321
Cdd:cd14142  240 FEDMRKVVcvDQQRPNIPNRWSSdPTLTAMaklMKECWYQNPSARLTA 287
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
76-212 2.21e-13

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


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 66.70  E-value: 2.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKVIQLNIDEaIRKSIAQELKINQSSQCPYL--VNSYQSFYDNGAISLILEYMDGGSL 153
Cdd:cd13968    1 MGEGASAKVFWAEGECTTIGVAVKIGDDVNNE-EGEDLESEMDILRRLKGLELniPKVLVTEDVDGPNILLMELVKGGTL 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 567218350 154 ADFLKSVkTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFG 212
Cdd:cd13968   80 IAYTQEE-ELDEKDVESIMYQLAECMRLLH-SFHLIHRDLNNDNILLSEDGNVKLIDFG 136
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
91-324 2.65e-13

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: 69.16  E-value: 2.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  91 WTGQFFALKVIQLNIDEAIRkSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLADFLK--SVKtipesyL 168
Cdd:cd14042   28 YKGNLVAIKKVNKKRIDLTR-EVLKELKHMRDLQHDNLTRFIGACVDPPNICILTEYCPKGSLQDILEneDIK------L 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 169 SAIFKQ-----VLQGLIYLHhDKHII-HRDLKPSNLLINHRGEVKITDFGVSTVMTNTaglaNTFVGTYNY------MSP 236
Cdd:cd14042  101 DWMFRYslihdIVKGMHYLH-DSEIKsHGNLKSSNCVVDSRFVLKITDFGLHSFRSGQ----EPPDDSHAYyakllwTAP 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 237 E--RIVG-NKYGN-KSDIWSLGLVVLECATGKFPYlppdqeetWSSVFEL--MEAIV------DQPP--PALPSENFSPE 302
Cdd:cd14042  176 EllRDPNpPPPGTqKGDVYSFGIILQEIATRQGPF--------YEEGPDLspKEIIKkkvrngEKPPfrPSLDELECPDE 247
                        250       260
                 ....*....|....*....|..
gi 567218350 303 LSSFISTCLQKDPNSRSSAKEL 324
Cdd:cd14042  248 VLSLMQRCWAEDPEERPDFSTL 269
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
76-266 2.92e-13

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: 69.02  E-value: 2.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQHKWTGQFFALKViqlnideairksiaqELKINQSSQCPYLVNSYQSF---------YDNGAIS---- 142
Cdd:cd14016    8 IGSGSFGEVYLGIDLKTGEEVAIKI---------------EKKDSKHPQLEYEAKVYKLLqggpgiprlYWFGQEGdynv 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 143 LILEYMdGGSLADFLK------SVKTIpesylSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLI---NHRGEVKITDFGV 213
Cdd:cd14016   73 MVMDLL-GPSLEDLFNkcgrkfSLKTV-----LMLADQMISRLEYLHS-KGYIHRDIKPENFLMglgKNSNKVYLIDFGL 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 567218350 214 STV-MTNTAGL------ANTFVGTYNYMSperiVGNKYGN----KSDIWSLGLVVLECATGKFP 266
Cdd:cd14016  146 AKKyRDPRTGKhipyreGKSLTGTARYAS----INAHLGIeqsrRDDLESLGYVLIYFLKGSLP 205
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
78-330 3.64e-13

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


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 68.79  E-value: 3.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  78 KGSSGVVQLVQHKWTGQFFALKVIQLNIDEaiRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLADFL 157
Cdd:cd14110   13 RGRFSVVRQCEEKRSGQMLAAKIIPYKPED--KQLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELCSGPELLYNL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 158 KSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTAGLANTFVGTY-NYMSP 236
Cdd:cd14110   91 AERNSYSEAEVTDYLWQILSAVDYLH-SRRILHLDLRSENMIITEKNLLKIVDLGNAQPFNQGKVLMTDKKGDYvETMAP 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 237 ERIVGNKYGNKSDIWSLGLVVLECATGKFPYlppDQEETWSSVFELMEAIVdqpppalpseNFS---PELS----SFIST 309
Cdd:cd14110  170 ELLEGQGAGPQTDIWAIGVTAFIMLSADYPV---SSDLNWERDRNIRKGKV----------QLSrcyAGLSggavNFLKS 236
                        250       260
                 ....*....|....*....|.
gi 567218350 310 CLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14110  237 TLCAKPWGRPTASECLQNPWL 257
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
64-267 3.92e-13

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


Pssm-ID: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 68.89  E-value: 3.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  64 ELSLSDLDMVKFLGKGSSGVVqlvqhkWTGQFF-----------ALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSY 132
Cdd:cd05091    2 EINLSAVRFMEELGEDRFGKV------YKGHLFgtapgeqtqavAIKTLKDKAEGPLREEFRHEAMLRSRLQHPNIVCLL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 133 QSFYDNGAISLILEYMDGGSLADFL---------------KSVKTI--PESYLSaIFKQVLQGLIYLHhDKHIIHRDLKP 195
Cdd:cd05091   76 GVVTKEQPMSMIFSYCSHGDLHEFLvmrsphsdvgstdddKTVKSTlePADFLH-IVTQIAAGMEYLS-SHHVVHKDLAT 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 567218350 196 SNLLINHRGEVKITDFGV--STVMTNTAGLANTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLEC-ATGKFPY 267
Cdd:cd05091  154 RNVLVFDKLNVKISDLGLfrEVYAADYYKLMGNSLLPIRWMSPEAIMYGKFSIDSDIWSYGVVLWEVfSYGLQPY 228
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
170-265 5.75e-13

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 69.72  E-value: 5.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 170 AIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNT-AGLANTFVGTYNYMSPERIVGNKYGNKS 248
Cdd:PHA03210 271 AIMKQLLCAVEYIH-DKKLIHRDIKLENIFLNCDGKIVLGDFGTAMPFEKErEAFDYGWVGTVATNSPEILAGDGYCEIT 349
                         90
                 ....*....|....*..
gi 567218350 249 DIWSLGLVVLECATGKF 265
Cdd:PHA03210 350 DIWSCGLILLDMLSHDF 366
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
76-326 6.49e-13

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: 67.75  E-value: 6.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQlvQHKWT---GQFF-----ALKVIQLNIDEAIrKSIAQELKINQSSQCPYLVNSYQSFYDNgAISLILEY 147
Cdd:cd05040    3 LGDGSFGVVR--RGEWTtpsGKVIqvavkCLKSDVLSQPNAM-DDFLKEVNAMHSLDHPNLIRLYGVVLSS-PLMMVTEL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 148 MDGGSLADFLKSVKTI-PESYLSAIFKQVLQGLIYLHHdKHIIHRDLKPSNLLINHRGEVKITDFGVSTVMTNTaglANT 226
Cdd:cd05040   79 APLGSLLDRLRKDQGHfLISTLCDYAVQIANGMAYLES-KRFIHRDLAARNILLASKDKVKIGDFGLMRALPQN---EDH 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 227 FVGTYN------YMSPERIVGNKYGNKSDIWSLGLVVLECatgkFPYlppdQEETWSSV--FELMEAIvDQPPPALPSEN 298
Cdd:cd05040  155 YVMQEHrkvpfaWCAPESLKTRKFSHASDVWMFGVTLWEM----FTY----GEEPWLGLngSQILEKI-DKEGERLERPD 225
                        250       260
                 ....*....|....*....|....*....
gi 567218350 299 FSPE-LSSFISTCLQKDPNSRSSAKELME 326
Cdd:cd05040  226 DCPQdIYNVMLQCWAHKPADRPTFVALRD 254
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
71-330 7.04e-13

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK2 plays a role in hepatic insulin signaling and glucose metabolism. It is induced by the insulin/Akt pathway as part of the hepatic refeeding reponse, and it directly phosphorylates the SR domain of PGC-1alpha, which results in decreased gluconeogenic gene expression and glucose output. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 68.89  E-value: 7.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  71 DMVKFLGKGSSG-VVQLVQHKWTGQFFALKVIQlNID---EAIRKSIAQELKINQS--SQCPYLVNSYQSFYDNGAISLI 144
Cdd:cd14215   15 EIVSTLGEGTFGrVVQCIDHRRGGARVALKIIK-NVEkykEAARLEINVLEKINEKdpENKNLCVQMFDWFDYHGHMCIS 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 145 LEYMdGGSLADFLKSVKTIPESY--LSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLI------------NHRGE----- 205
Cdd:cd14215   94 FELL-GLSTFDFLKENNYLPYPIhqVRHMAFQVCQAVKFLHDNK-LTHTDLKPENILFvnsdyeltynleKKRDErsvks 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 206 --VKITDFGVSTVMTNTAglaNTFVGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETwssvFELM 283
Cdd:cd14215  172 taIRVVDFGSATFDHEHH---STIVSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNREH----LAMM 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 284 EAIVDQPPPAL--------------------------PSENFSP-------------ELSSFISTCLQKDPNSRSSAKEL 324
Cdd:cd14215  245 ERILGPIPSRMirktrkqkyfyhgrldwdentsagryVRENCKPlrryltseaeehhQLFDLIESMLEYEPSKRLTLAAA 324

                 ....*.
gi 567218350 325 MEHPFL 330
Cdd:cd14215  325 LKHPFF 330
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
65-324 8.11e-13

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: 67.87  E-value: 8.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  65 LSLSDLDMVKFLGKGSSGVVQLVQHKWTG-----QFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNG 139
Cdd:cd05046    2 FPRSNLQEITTLGRGEFGEVFLAKAKGIEeeggeTLVLVKALQKTKDENLQSEFRRELDMFRKLSHKNVVRLLGLCREAE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 140 AISLILEYMDGGSLADFLKSVKTIPESYLS---------AIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITD 210
Cdd:cd05046   82 PHYMILEYTDLGDLKQFLRATKSKDEKLKPpplstkqkvALCTQIALGMDHLS-NARFVHRDLAARNCLVSSQREVKVSL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 211 FGVSTVMTNTA--GLANTFVgTYNYMSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPYLPPDQEETwssVFELMEAIV 287
Cdd:cd05046  161 LSLSKDVYNSEyyKLRNALI-PLRWLAPEAVQEDDFSTKSDVWSFGVLMWEVFTqGELPFYGLSDEEV---LNRLQAGKL 236
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 567218350 288 DQPPPalpsENFSPELSSFISTCLQKDPNSRSSAKEL 324
Cdd:cd05046  237 ELPVP----EGCPSRLYKLMTRCWAVNPKDRPSFSEL 269
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
143-326 9.78e-13

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


Pssm-ID: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 67.73  E-value: 9.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 143 LILEYMDGGSLADFLKSVKT------IPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTV 216
Cdd:cd05075   84 VILPFMKHGDLHSFLLYSRLgdcpvyLPTQMLVKFMTDIASGMEYLS-SKNFIHRDLAARNCMLNENMNVCVADFGLSKK 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 217 MTNtaglantfvGTY-----------NYMSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPYlpPDQEEtwSSVFELME 284
Cdd:cd05075  163 IYN---------GDYyrqgriskmpvKWIAIESLADRVYTTKSDVWSFGVTMWEIATrGQTPY--PGVEN--SEIYDYLR 229
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 567218350 285 A--IVDQPPPALPSenfspeLSSFISTCLQKDPNSRSSAKELME 326
Cdd:cd05075  230 QgnRLKQPPDCLDG------LYELMSSCWLLNPKDRPSFETLRC 267
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
137-324 1.02e-12

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: 67.48  E-value: 1.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 137 DNGAISLILEYMDGGSLADFLKSVKTIPESYLSAIFK--------QVLQGLIYLHHdKHIIHRDLKPSNLLINHRGEVKI 208
Cdd:cd05043   79 DGEKPMVLYPYMNWGNLKLFLQQCRLSEANNPQALSTqqlvhmalQIACGMSYLHR-RGVIHKDIAARNCVIDDELQVKI 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 209 TDFGVSTvmtntaglaNTFVGTYN-----------YMSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPYLPPDqeetw 276
Cdd:cd05043  158 TDNALSR---------DLFPMDYHclgdnenrpikWMSLESLVNKEYSSASDVWSFGVLLWELMTlGQTPYVEID----- 223
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 567218350 277 ssVFELMEAIVDQPPPALPSeNFSPELSSFISTCLQKDPNSRSSAKEL 324
Cdd:cd05043  224 --PFEMAAYLKDGYRLAQPI-NCPDELFAVMACCWALDPEERPSFQQL 268
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
151-330 1.45e-12

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


Pssm-ID: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 66.60  E-value: 1.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 151 GSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLIN--HRGEVKITDFGVSTVMTNTAGLANTFV 228
Cdd:cd14022   69 GDMHSFVRTCKKLREEEAARLFYQIASAVAHCH-DGGLVLRDLKLRKFVFKdeERTRVKLESLEDAYILRGHDDSLSDKH 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 229 GTYNYMSPE--RIVGNKYGNKSDIWSLGLVVLECATGKFPYlpPDQEEtwSSVFELMEAIVDQPPPALpsenfSPELSSF 306
Cdd:cd14022  148 GCPAYVSPEilNTSGSYSGKAADVWSLGVMLYTMLVGRYPF--HDIEP--SSLFSKIRRGQFNIPETL-----SPKAKCL 218
                        170       180
                 ....*....|....*....|....
gi 567218350 307 ISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14022  219 IRSILRREPSERLTSQEILDHPWF 242
COG2112 COG2112
Predicted Ser/Thr protein kinase [Signal transduction mechanisms];
73-211 1.49e-12

Predicted Ser/Thr protein kinase [Signal transduction mechanisms];


Pssm-ID: 441715 [Multi-domain]  Cd Length: 225  Bit Score: 66.20  E-value: 1.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  73 VKFLGKGSSGVVqlVQHKWTGQFFALKVIQLNideAIRKSIAQELKINQssqcpyLVNSYQSF---YDNGAISLILEYMD 149
Cdd:COG2112   45 LRLLGKGYRGVV--FLGKLGGKKVALKIRRTD---SPRPSLKKEAEILK------KANGAGVGpklYDYGRDFLVMEYIE 113
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 567218350 150 GGSLADFLKSvktIPESYLSAIFKQVLQGLIYLhHDKHIIHRDL-KPSNLLINHRGEVKITDF 211
Cdd:COG2112  114 GEPLKDWLEN---LDKEELRKVIRELLEAAYLL-DRIGIDHGELsRPGKHVIVDKGRPYIIDF 172
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
76-318 1.67e-12

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: 66.75  E-value: 1.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSGVVQLVQhKWTGQF-FALKVIqLNIDEAIRKSIAQELKINQS-SQCPYLVNSYQSFYDNG-------AISLILE 146
Cdd:cd13975    8 LGRGQYGVVYACD-SWGGHFpCALKSV-VPPDDKHWNDLALEFHYTRSlPKHERIVSLHGSVIDYSygggssiAVLLIME 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 147 YMDGgSLADFLKSVKTIPESYLSAIfkQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVStvmTNTAGLANT 226
Cdd:cd13975   86 RLHR-DLYTGIKAGLSLEERLQIAL--DVVEGIRFLH-SQGLVHRDIKLKNVLLDKKNRAKITDLGFC---KPEAMMSGS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 227 FVGTYNYMSPERIVGnKYGNKSDIWSLGLVVLECATGKFPyLP------PDQEETWSSVFElmeaivDQPPPALPseNFS 300
Cdd:cd13975  159 IVGTPIHMAPELFSG-KYDNSVDVYAFGILFWYLCAGHVK-LPeafeqcASKDHLWNNVRK------GVRPERLP--VFD 228
                        250
                 ....*....|....*...
gi 567218350 301 PELSSFISTCLQKDPNSR 318
Cdd:cd13975  229 EECWNLMEACWSGDPSQR 246
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
151-332 1.75e-12

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


Pssm-ID: 214801  Cd Length: 176  Bit Score: 65.11  E-value: 1.75e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350   151 GSLADFLKSVKT-IPESYLSAIFKQVLQGLIYLHHDKhiihrdlKPSNLLINHRGEVKItdFGVSTVMTNtaglANTFVG 229
Cdd:smart00750   1 VSLADILEVRGRpLNEEEIWAVCLQCLGALRELHRQA-------KSGNILLTWDGLLKL--DGSVAFKTP----EQSRPD 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350   230 TYnYMSPERIVGNKYGNKSDIWSLGLVVLECATGKfpyLPPDQEETWS----SVFELMEAivDQPPPALPSENFS--PEL 303
Cdd:smart00750  68 PY-FMAPEVIQGQSYTEKADIYSLGITLYEALDYE---LPYNEERELSaileILLNGMPA--DDPRDRSNLEGVSaaRSF 141
                          170       180
                   ....*....|....*....|....*....
gi 567218350   304 SSFISTCLQKDPNSRSSAKELMEHPFLNK 332
Cdd:smart00750 142 EDFMRLCASRLPQRREAANHYLAHCRALF 170
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
138-327 1.83e-12

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


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 67.13  E-value: 1.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 138 NGAISLILEYMDGGSLADFLKSVKTI-------------PESYLSAIFK-------------QVLQGLIYLHHDKhIIHR 191
Cdd:cd05054   84 GGPLMVIVEFCKFGNLSNYLRSKREEfvpyrdkgardveEEEDDDELYKepltledlicysfQVARGMEFLASRK-CIHR 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 192 DLKPSNLLINHRGEVKITDFGVST--------VMTNTAGLAntfvgtYNYMSPERIVGNKYGNKSDIWSLGLVVLEC-AT 262
Cdd:cd05054  163 DLAARNILLSENNVVKICDFGLARdiykdpdyVRKGDARLP------LKWMAPESIFDKVYTTQSDVWSFGVLLWEIfSL 236
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 567218350 263 GKFPYLPPDQEETWSSvfELMEAIVDQPPpalpsENFSPELSSFISTCLQKDPNSRSSAKELMEH 327
Cdd:cd05054  237 GASPYPGVQMDEEFCR--RLKEGTRMRAP-----EYTTPEIYQIMLDCWHGEPKERPTFSELVEK 294
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
126-328 1.85e-12

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


Pssm-ID: 271041 [Multi-domain]  Cd Length: 274  Bit Score: 66.87  E-value: 1.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 126 PYLVNSYQSFYDNGAISLILEYMDGGSLADFL----KSVKTIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLIN 201
Cdd:cd14139   60 PHVVRYYSAWAEDDHMIIQNEYCNGGSLQDAIsentKSGNHFEEPELKDILLQVSMGLKYIH-NSGLVHLDIKPSNIFIC 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 202 HRGEV----------------------KITDFGVSTVMTNtaglANTFVGTYNYMSPErIVGNKYGN--KSDIWSLGLVV 257
Cdd:cd14139  139 HKMQSssgvgeevsneedeflsanvvyKIGDLGHVTSINK----PQVEEGDSRFLANE-ILQEDYRHlpKADIFALGLTV 213
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 567218350 258 LeCATGKFPYlpPDQEETWssvfelmEAIVDQPPPALPSEnFSPELSSFISTCLQKDPNSRSSAKELMEHP 328
Cdd:cd14139  214 A-LAAGAEPL--PTNGAAW-------HHIRKGNFPDVPQE-LPESFSSLLKNMIQPDPEQRPSATALARHT 273
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
184-327 1.87e-12

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


Pssm-ID: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 67.05  E-value: 1.87e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 184 HDKHIIHRDLKPSNLLINHRG-EVKITDFGVSTVMTNTAGLANTFVGTYNYMSPERIVGNKY-GNKSDIWSLGLVVLECA 261
Cdd:cd13974  149 HKKNIVHRDLKLGNMVLNKRTrKITITNFCLGKHLVSEDDLLKDQRGSPAYISPDVLSGKPYlGKPSDMWALGVVLFTML 228
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 567218350 262 TGKFPYLPpdqeetwSSVFELMEAIvDQPPPALPSEN-FSPELSSFISTCLQKDPNSRSSAKELMEH 327
Cdd:cd13974  229 YGQFPFYD-------SIPQELFRKI-KAAEYTIPEDGrVSENTVCLIRKLLVLNPQKRLTASEVLDS 287
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
137-321 2.92e-12

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: 66.31  E-value: 2.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 137 DNGAIS---LILEYMDGGSLADFLKSVKTIPESYLSAIFkQVLQGLIYLHHD-------KHIIHRDLKPSNLLINHRGEV 206
Cdd:cd14143   61 DNGTWTqlwLVSDYHEHGSLFDYLNRYTVTVEGMIKLAL-SIASGLAHLHMEivgtqgkPAIAHRDLKSKNILVKKNGTC 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 207 KITDFGVST---VMTNTAGLA-NTFVGTYNYMSPErIVGNKYGNKS-------DIWSLGLVVLE----CATG------KF 265
Cdd:cd14143  140 CIADLGLAVrhdSATDTIDIApNHRVGTKRYMAPE-VLDDTINMKHfesfkraDIYALGLVFWEiarrCSIGgihedyQL 218
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 567218350 266 PY---LPPDQ--EETWSSVFElmeaivDQPPPALPSENFSPE----LSSFISTCLQKDPNSRSSA 321
Cdd:cd14143  219 PYydlVPSDPsiEEMRKVVCE------QKLRPNIPNRWQSCEalrvMAKIMRECWYANGAARLTA 277
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
76-264 2.96e-12

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. Mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A was previously called minibrain kinase homolog (MNBH) or dual-specificity YAK1-related kinase. It phosphorylates various substrates and is involved in many cellular events. It phosphorylates and inhibits the transcription factors, nuclear factor of activated T cells (NFAT) and forkhead in rhabdomyosarcoma (FKHR). It regulates neuronal differentiation by targetting CREB (cAMP response element-binding protein). It also targets many endocytic proteins including dynamin and amphiphysin and may play a role in the endocytic pathway. The gene encoding DYRK1A is located in the DSCR (Down syndrome critical region) of human chromosome 21 and DYRK1A has been implicated in the pathogenesis of DS. DYRK1B, also called minibrain-related kinase (MIRK), is highly expressed in muscle and plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 66.96  E-value: 2.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  76 LGKGSSG-VVQLVQHKwTGQFFALKVI--------QLNIDEAIRKSIAQELKINQSsqcpYLVNSYQSFYDNGAISLILE 146
Cdd:cd14226   21 IGKGSFGqVVKAYDHV-EQEWVAIKIIknkkaflnQAQIEVRLLELMNKHDTENKY----YIVRLKRHFMFRNHLCLVFE 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 147 YMDGgSLADFLKSVKTIPESyLSAIFK---QVLQGLIYLHH-DKHIIHRDLKPSN-LLIN-HRGEVKITDFGVSTVMTNT 220
Cdd:cd14226   96 LLSY-NLYDLLRNTNFRGVS-LNLTRKfaqQLCTALLFLSTpELSIIHCDLKPENiLLCNpKRSAIKIIDFGSSCQLGQR 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 567218350 221 aglantfvgTYNYM------SPERIVGNKYGNKSDIWSLGLVVLECATGK 264
Cdd:cd14226  174 ---------IYQYIqsrfyrSPEVLLGLPYDLAIDMWSLGCILVEMHTGE 214
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
79-326 3.85e-12

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: 66.06  E-value: 3.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  79 GSSGVVQLVQHKWTGQFFALKVIQLNID---EAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYMDGGSLAD 155
Cdd:cd14160    2 GEGEIFEVYRVRIGNRSYAVKLFKQEKKmqwKKHWKRFLSELEVLLLFQHPNILELAAYFTETEKFCLVYPYMQNGTLFD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 156 FLKSVK-TIPESYLS--AIFKQVLQGLIYLHHDK--HIIHRDLKPSNLLINHRGEVKITDFGV-----------STVMTN 219
Cdd:cd14160   82 RLQCHGvTKPLSWHEriNILIGIAKAIHYLHNSQpcTVICGNISSANILLDDQMQPKLTDFALahfrphledqsCTINMT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 220 TAGLANTFvgtynYMSPERIVGNKYGNKSDIWSLGLVVLECATG-KFPYLPPDQEETWSSVFELME--------AIVDQP 290
Cdd:cd14160  162 TALHKHLW-----YMPEEYIRQGKLSVKTDVYSFGIVIMEVLTGcKVVLDDPKHLQLRDLLHELMEkrgldsclSFLDLK 236
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 567218350 291 PPALPsENFSPELSSFISTCLQKDPNSRSSAKELME 326
Cdd:cd14160  237 FPPCP-RNFSAKLFRLAGRCTATKAKLRPDMDEVLQ 271
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
91-318 5.36e-12

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: 65.26  E-value: 5.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  91 WTGQFFALKVIQLN---IDEAIRKSIAQELKINQSSQCPYLVNSYQSfydnGAISLILEYMDGGSLADFLKSvKTIP--E 165
Cdd:cd14045   28 YDGRTVAIKKIAKKsftLSKRIRKEVKQVRELDHPNLCKFIGGCIEV----PNVAIITEYCPKGSLNDVLLN-EDIPlnW 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 166 SYLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKITDFGVSTvMTNTAGLANTfvGTYN------YMSPERI 239
Cdd:cd14045  103 GFRFSFATDIARGMAYLHQHK-IYHGRLKSSNCVIDDRWVCKIADYGLTT-YRKEDGSENA--SGYQqrlmqvYLPPENH 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 240 VGNKY--GNKSDIWSLGLVVLECATGKfpylPPDQEETWSsvfelMEAIVDQPPPALPS---ENFSP---ELSSFISTCL 311
Cdd:cd14045  179 SNTDTepTQATDVYSYAIILLEIATRN----DPVPEDDYS-----LDEAWCPPLPELISgktENSCPcpaDYVELIRRCR 249

                 ....*..
gi 567218350 312 QKDPNSR 318
Cdd:cd14045  250 KNNPAQR 256
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
64-325 7.08e-12

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: 65.05  E-value: 7.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  64 ELSLSDLDMVKFLGKGS-----SGVVQLVQHKWTGQFFALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDN 138
Cdd:cd05062    2 EVAREKITMSRELGQGSfgmvyEGIAKGVVKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 139 GAISLILEYMDGGSLADFLKSVKTIPESY-------LSAIFK---QVLQGLIYLHHDKhIIHRDLKPSNLLINHRGEVKI 208
Cdd:cd05062   82 QPTLVIMELMTRGDLKSYLRSLRPEMENNpvqappsLKKMIQmagEIADGMAYLNANK-FVHRDLAARNCMVAEDFTVKI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 209 TDFGVSTVMTNTAGLANTFVGTY--NYMSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPYLPPDQEETWSSVFElmEA 285
Cdd:cd05062  161 GDFGMTRDIYETDYYRKGGKGLLpvRWMSPESLKDGVFTTYSDVWSFGVVLWEIATlAEQPYQGMSNEQVLRFVME--GG 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 567218350 286 IVDQPppalpsENFSPELSSFISTCLQKDPNSRSSAKELM 325
Cdd:cd05062  239 LLDKP------DNCPDMLFELMRMCWQYNPKMRPSFLEII 272
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
65-324 7.61e-12

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: 65.47  E-value: 7.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  65 LSLSDLDMVKFLGKGSSGVVqlVQHKWTGQF------FALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYdN 138
Cdd:cd05110    4 LKETELKRVKVLGSGAFGTV--YKGIWVPEGetvkipVAIKILNETTGPKANVEFMDEALIMASMDHPHLVRLLGVCL-S 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 139 GAISLILEYMDGGSLADFLKSVK-TIPESYLSAIFKQVLQGLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTVM 217
Cdd:cd05110   81 PTIQLVTQLMPHGCLLDYVHEHKdNIGSQLLLNWCVQIAKGMMYLE-ERRLVHRDLAARNVLVKSPNHVKITDFGLARLL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 218 TNTAGLANTFVGTY--NYMSPERIVGNKYGNKSDIWSLGLVVLECAT-GKFPYLP-PDQEetwssVFELMEAIVDQPPPA 293
Cdd:cd05110  160 EGDEKEYNADGGKMpiKWMALECIHYRKFTHQSDVWSYGVTIWELMTfGGKPYDGiPTRE-----IPDLLEKGERLPQPP 234
                        250       260       270
                 ....*....|....*....|....*....|.
gi 567218350 294 LpsenFSPELSSFISTCLQKDPNSRSSAKEL 324
Cdd:cd05110  235 I----CTIDVYMVMVKCWMIDADSRPKFKEL 261
STKc_SRPK1 cd14216
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs ...
72-274 7.73e-12

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK1 binds with high affinity the alternative splicing factor, SRSF1 (serine/arginine-rich splicing factor 1), and regiospecifically phosphorylates 10-12 serines in its RS domain. It plays a role in the regulation of pre-mRNA splicing, chromatin structure, and germ cell development. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271118 [Multi-domain]  Cd Length: 349  Bit Score: 65.82  E-value: 7.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  72 MVKFLGKGSSGVVQLVQHKWTGQFFALKVIQLNidEAIRKSIAQELKINQS-----------SQCPYLVNSYQSFYDNGA 140
Cdd:cd14216   14 VIRKLGWGHFSTVWLSWDIQGKRFVAMKVVKSA--EHYTETALDEIKLLKSvrnsdpndpnrEMVVQLLDDFKISGVNGT 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 141 -ISLILEYMDGGSLADFLKS-VKTIPESYLSAIFKQVLQGLIYLHHDKHIIHRDLKPSNLLIN----------------- 201
Cdd:cd14216   92 hICMVFEVLGHHLLKWIIKSnYQGLPLPCVKKIIRQVLQGLDYLHTKCRIIHTDIKPENILLSvneqyirrlaaeatewq 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 202 -------------HRGEVKITDFGvstvmtNTAGLANTF---VGTYNYMSPERIVGNKYGNKSDIWSLGLVVLECATGKF 265
Cdd:cd14216  172 rnflvnplepknaEKLKVKIADLG------NACWVHKHFtedIQTRQYRSLEVLIGSGYNTPADIWSTACMAFELATGDY 245

                 ....*....
gi 567218350 266 PYLPPDQEE 274
Cdd:cd14216  246 LFEPHSGED 254
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
137-267 8.12e-12

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: 64.47  E-value: 8.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 137 DNGAISLILEYMDGGSLADFLKSVKTI--PESYLSaIFKQVLQGLIYLHHDKH-IIHRDLKPSNLLINHRGEVKITDFGV 213
Cdd:cd14064   63 DPSQFAIVTQYVSGGSLFSLLHEQKRVidLQSKLI-IAVDVAKGMEYLHNLTQpIIHRDLNSHNILLYEDGHAVVADFGE 141
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 567218350 214 STV--------MTNTAglantfvGTYNYMSPERIVGN-KYGNKSDIWSLGLVVLECATGKFPY 267
Cdd:cd14064  142 SRFlqsldednMTKQP-------GNLRWMAPEVFTQCtRYSIKADVFSYALCLWELLTGEIPF 197
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
74-324 9.61e-12

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: 64.26  E-value: 9.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350  74 KFLGKGSSGVVqlvqhkWTGQF-----FALKVIQLNIDEAIRKSIAQELKINQSSQCPYLVNSYQSFYDNGAISLILEYM 148
Cdd:cd05085    2 ELLGKGNFGEV------YKGTLkdktpVAVKTCKEDLPQELKIKFLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 149 DGGSLADFLKSVKTipESYLSAIFKQVLQ---GLIYLHhDKHIIHRDLKPSNLLINHRGEVKITDFGVSTV----MTNTA 221
Cdd:cd05085   76 PGGDFLSFLRKKKD--ELKTKQLVKFSLDaaaGMAYLE-SKNCIHRDLAARNCLVGENNALKISDFGMSRQeddgVYSSS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 222 GLANTFVgtyNYMSPERIVGNKYGNKSDIWSLGLVVLEC-ATGKFPYLPPDQEETWSSVFELMEAIVDQPPPAlpsenfs 300
Cdd:cd05085  153 GLKQIPI---KWTAPEALNYGRYSSESDVWSFGILLWETfSLGVCPYPGMTNQQAREQVEKGYRMSAPQRCPE------- 222
                        250       260
                 ....*....|....*....|....
gi 567218350 301 pELSSFISTCLQKDPNSRSSAKEL 324
Cdd:cd05085  223 -DIYKIMQRCWDYNPENRPKFSEL 245
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
143-327 1.17e-11

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: 64.33  E-value: 1.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 143 LILEYMDGGSLADFLKSVKTIPES-------YLSAIFKQVLQGLIYLhHDKHIIHRDLKPSNLLINHRGE---VKITDFG 212
Cdd:cd05036   86 ILLELMAGGDLKSFLRENRPRPEQpssltmlDLLQLAQDVAKGCRYL-EENHFIHRDIAARNCLLTCKGPgrvAKIGDFG 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 213 VSTVMTNT-----AGLANTFVgtyNYMSPERIVGNKYGNKSDIWSLGLVVLEC-ATGKFPYlpPDQEETwssvfELMEAI 286
Cdd:cd05036  165 MARDIYRAdyyrkGGKAMLPV---KWMPPEAFLDGIFTSKTDVWSFGVLLWEIfSLGYMPY--PGKSNQ-----EVMEFV 234
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 567218350 287 VD----QPPPALPSENFspelsSFISTCLQKDPNSRSSAKELMEH 327
Cdd:cd05036  235 TSggrmDPPKNCPGPVY-----RIMTQCWQHIPEDRPNFSTILER 274
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
149-330 1.42e-11

Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB1 interacts directly with the mitogen activated protein kinase (MAPK) kinase MKK4, an activator of JNK. It regulates vascular smooth muscle cell proliferation and chemotaxis through the JNK signaling pathway. It is found to be down-regulated in human acute myeloid leukaemia (AML) and may play a role in the pathogenesis of the disease. It has also been identified as a potential biomarker for antibody-mediated allograft failure. TRB1 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB1 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 63.91  E-value: 1.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 149 DGGSLADFLKSVKTIPESYLSAIFKQVLQGLIYLHHDKhIIHRDLKPSNLLIN--HRGEVKITDFGVSTVMTNTAGLANT 226
Cdd:cd14023   67 DFGDMHSYVRSCKRLREEEAARLFKQIVSAVAHCHQSA-IVLGDLKLRKFVFSdeERTQLRLESLEDTHIMKGEDDALSD 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567218350 227 FVGTYNYMSPE--RIVGNKYGNKSDIWSLGLVVLECATGKFPYLPPDQEETWSSVFELMEAIVDqpppalpseNFSPELS 304
Cdd:cd14023  146 KHGCPAYVSPEilNTTGTYSGKSADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPD---------HVSPKAR 216
                        170       180
                 ....*....|....*....|....*.
gi 567218350 305 SFISTCLQKDPNSRSSAKELMEHPFL 330
Cdd:cd14023  217 CLIRSLLRREPSERLTAPEILLHPWF 242
 
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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