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Conserved domains on  [gi|148839316|ref|NP_003148|]
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serine/threonine-protein kinase Nek4 isoform 1 [Homo sapiens]

Protein Classification

serine/threonine-protein kinase Nek4( domain architecture ID 10169494)

serine/threonine-protein kinase Nek4 (Never In Mitosis gene A (NIMA)-related kinase 4) catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates, and is required for normal cell cycle arrest in response to double-stranded DNA damage

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
5-261 0e+00

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: 550.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   5 AYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLYIVMG 84
Cdd:cd08223    1 EYQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKAAEQEAKLLSKLKHPNIVSYKESFEGEDGFLYIVMG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGGDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMAS 164
Cdd:cd08223   81 FCEGGDLYTRLKEQKGVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLESSSDMAT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 TLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPRDYSPELAELIRTMLSK 244
Cdd:cd08223  161 TLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEGKLPPMPKQYSPELGELIKAMLHQ 240
                        250
                 ....*....|....*..
gi 148839316 245 RPEERPSVRSILRQPYI 261
Cdd:cd08223  241 DPEKRPSVKRILRQPYI 257
 
Name Accession Description Interval E-value
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
5-261 0e+00

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: 550.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   5 AYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLYIVMG 84
Cdd:cd08223    1 EYQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKAAEQEAKLLSKLKHPNIVSYKESFEGEDGFLYIVMG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGGDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMAS 164
Cdd:cd08223   81 FCEGGDLYTRLKEQKGVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLESSSDMAT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 TLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPRDYSPELAELIRTMLSK 244
Cdd:cd08223  161 TLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEGKLPPMPKQYSPELGELIKAMLHQ 240
                        250
                 ....*....|....*..
gi 148839316 245 RPEERPSVRSILRQPYI 261
Cdd:cd08223  241 DPEKRPSVKRILRQPYI 257
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
6-261 3.93e-92

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 290.20  E-value: 3.93e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316     6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSrERRAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGF 85
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKK-DRERILREIKILKKLKHPNIVRLYDVFED-EDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316    86 CEGGDLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHcDMAST 165
Cdd:smart00220  79 CEGGDLFDLLKKRGR--LSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPG-EKLTT 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   166 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPR---DYSPELAELIRTML 242
Cdd:smart00220 156 FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPpewDISPEAKDLIRKLL 235
                          250
                   ....*....|....*....
gi 148839316   243 SKRPEERPSVRSILRQPYI 261
Cdd:smart00220 236 VKDPEKRLTAEEALQHPFF 254
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
6-257 5.56e-73

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 247.23  E-value: 5.56e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAA-EQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMG 84
Cdd:COG0515    9 YRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARERfRREARALARLNHPNIVRVYDVGEE-DGRPYLVME 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGGDLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVL-ENHCDMA 163
Cdd:COG0515   88 YVEGESLADLLRRRGP--LPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALgGATLTQT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 164 STLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPR---DYSPELAELIRT 240
Cdd:COG0515  166 GTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSElrpDLPPALDAIVLR 245
                        250
                 ....*....|....*...
gi 148839316 241 MLSKRPEERP-SVRSILR 257
Cdd:COG0515  246 ALAKDPEERYqSAAELAA 263
Pkinase pfam00069
Protein kinase domain;
6-261 7.23e-54

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 185.91  E-value: 7.23e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316    6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGlLYIVMGF 85
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDN-LYLVLEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   86 CEGGDLYRKLKEQKGqlLPENQVVEWFVQiamalqylhekhilhrdlktqnvfltrtniikvgdlgIARVLENHCDMaST 165
Cdd:pfam00069  80 VEGGSLFDLLSEKGA--FSEREAKFIMKQ-------------------------------------ILEGLESGSSL-TT 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  166 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKL--PPMPRDYSPELAELIRTMLS 243
Cdd:pfam00069 120 FVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYafPELPSNLSEEAKDLLKKLLK 199
                         250
                  ....*....|....*...
gi 148839316  244 KRPEERPSVRSILRQPYI 261
Cdd:pfam00069 200 KDPSKRLTATQALQHPWF 217
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
10-270 2.31e-46

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 173.52  E-value: 2.31e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLL------SQLK-HPNIVTYKESWEGGDGLLYIV 82
Cdd:PTZ00283  38 RVLGSGATGTVLCAKRVSDGEPFAVKVVDMEGMSEADKNRAQAEVCCLlncdffSIVKcHEDFAKKDPRNPENVLMIALV 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  83 MGFCEGGDLYRKLKE--QKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHC 160
Cdd:PTZ00283 118 LDYANAGDLRQEIKSraKTNRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDFGFSKMYAATV 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 161 --DMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPRDYSPELAELI 238
Cdd:PTZ00283 198 sdDVGRTFCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGENMEEVMHKTLAGRYDPLPPSISPEMQEIV 277
                        250       260       270
                 ....*....|....*....|....*....|..
gi 148839316 239 RTMLSKRPEERPSVRSILRQPYIKRQISFFLE 270
Cdd:PTZ00283 278 TALLSSDPKRRPSSSKLLNMPICKLFISGLLE 309
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
53-250 7.12e-34

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 137.62  E-value: 7.12e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  53 EAQLLSQLKHPNIVTYKESWEGGdGLLYIVMGFCEGGDLyRKLKEQKGQLLPEnQVVEWFVQIAMALQYLHEKHILHRDL 132
Cdd:NF033483  57 EAQSAASLSHPNIVSVYDVGEDG-GIPYIVMEYVDGRTL-KDYIREHGPLSPE-EAVEIMIQILSALEHAHRNGIVHRDI 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 133 KTQNVFLTRTNIIKVGDLGIARVL-ENHCDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMAT---------- 201
Cdd:NF033483 134 KPQNILITKDGRVKVTDFGIARALsSTTMTQTNSVLGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTgrppfdgdsp 213
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 148839316 202 ----LKHaFNakdmnslvyriiegKLPPMPRDY----SPELAELIRTMLSKRPEERP 250
Cdd:NF033483 214 vsvaYKH-VQ--------------EDPPPPSELnpgiPQSLDAVVLKATAKDPDDRY 255
 
Name Accession Description Interval E-value
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
5-261 0e+00

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: 550.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   5 AYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLYIVMG 84
Cdd:cd08223    1 EYQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKAAEQEAKLLSKLKHPNIVSYKESFEGEDGFLYIVMG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGGDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMAS 164
Cdd:cd08223   81 FCEGGDLYTRLKEQKGVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLESSSDMAT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 TLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPRDYSPELAELIRTMLSK 244
Cdd:cd08223  161 TLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEGKLPPMPKQYSPELGELIKAMLHQ 240
                        250
                 ....*....|....*..
gi 148839316 245 RPEERPSVRSILRQPYI 261
Cdd:cd08223  241 DPEKRPSVKRILRQPYI 257
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
6-261 2.38e-157

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: 459.24  E-value: 2.38e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGF 85
Cdd:cd08215    2 YEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMSEKEREEALNEVKLLSKLKHPNIVKYYESFEE-NGKLCIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGGDLYRKLKEQK--GQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMA 163
Cdd:cd08215   81 ADGGDLAQKIKKQKkkGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISKVLESTTDLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 164 STLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPRDYSPELAELIRTMLS 243
Cdd:cd08215  161 KTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYPPIPSQYSSELRDLVNSMLQ 240
                        250
                 ....*....|....*...
gi 148839316 244 KRPEERPSVRSILRQPYI 261
Cdd:cd08215  241 KDPEKRPSANEILSSPFI 258
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
6-261 8.72e-115

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: 349.49  E-value: 8.72e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGF 85
Cdd:cd08218    2 YVRIKKIGEGSFGKALLVKSKEDGKQYVIKEINISKMSPKEREESRKEVAVLSKMKHPNIVQYQESFEE-NGNLYIVMDY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGGDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMAST 165
Cdd:cd08218   81 CDGGDLYKRINAQRGVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVLNSTVELART 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPRDYSPELAELIRTMLSKR 245
Cdd:cd08218  161 CIGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKIIRGSYPPVPSRYSYDLRSLVSQLFKRN 240
                        250
                 ....*....|....*.
gi 148839316 246 PEERPSVRSILRQPYI 261
Cdd:cd08218  241 PRDRPSINSILEKPFI 256
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
9-259 5.72e-98

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: 305.49  E-value: 5.72e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGdGLLYIVMGFCEG 88
Cdd:cd08529    5 LNKLGKGSFGVVYKVVRKVDGRVYALKQIDISRMSRKMREEAIDEARVLSKLNSPYVIKYYDSFVDK-GKLNIVMEYAEN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  89 GDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTLIG 168
Cdd:cd08529   84 GDLHSLIKSQRGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAKILSDTTNFAQTIVG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 169 TPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPRDYSPELAELIRTMLSKRPEE 248
Cdd:cd08529  164 TPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKYPPISASYSQDLSQLIDSCLTKDYRQ 243
                        250
                 ....*....|.
gi 148839316 249 RPSVRSILRQP 259
Cdd:cd08529  244 RPDTTELLRNP 254
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
5-261 2.49e-93

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: 293.68  E-value: 2.49e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   5 AYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTY------KESweggdGL 78
Cdd:cd08217    1 DYEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDYGKMSEKEKQQLVSEVNILRELKHPNIVRYydrivdRAN-----TT 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  79 LYIVMGFCEGGDL---YRKLKEQKgQLLPENQVVEWFVQIAMALQYLHEKH-----ILHRDLKTQNVFLTRTNIIKVGDL 150
Cdd:cd08217   76 LYIVMEYCEGGDLaqlIKKCKKEN-QYIPEEFIWKIFTQLLLALYECHNRSvgggkILHRDLKPANIFLDSDNNVKLGDF 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 151 GIARVLENHCDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPRDY 230
Cdd:cd08217  155 GLARVLSHDSSFAKTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAANQLELAKKIKEGKFPRIPSRY 234
                        250       260       270
                 ....*....|....*....|....*....|.
gi 148839316 231 SPELAELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd08217  235 SSELNEVIKSMLNVDPDKRPSVEELLQLPLI 265
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
6-256 2.86e-92

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: 290.72  E-value: 2.86e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSrERRAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGF 85
Cdd:cd08219    2 YNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIRLPKSSS-AVEDSRKEAVLLAKMKHPNIVAFKESFEA-DGHLYIVMEY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGGDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMAST 165
Cdd:cd08219   80 CDGGDLMQKIKLQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSPGAYACT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPRDYSPELAELIRTMLSKR 245
Cdd:cd08219  160 YVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGSYKPLPSHYSYELRSLIKQMFKRN 239
                        250
                 ....*....|.
gi 148839316 246 PEERPSVRSIL 256
Cdd:cd08219  240 PRSRPSATTIL 250
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
6-261 3.93e-92

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 290.20  E-value: 3.93e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316     6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSrERRAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGF 85
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKK-DRERILREIKILKKLKHPNIVRLYDVFED-EDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316    86 CEGGDLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHcDMAST 165
Cdd:smart00220  79 CEGGDLFDLLKKRGR--LSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPG-EKLTT 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   166 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPR---DYSPELAELIRTML 242
Cdd:smart00220 156 FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPpewDISPEAKDLIRKLL 235
                          250
                   ....*....|....*....
gi 148839316   243 SKRPEERPSVRSILRQPYI 261
Cdd:smart00220 236 VKDPEKRLTAEEALQHPFF 254
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
6-261 3.47e-90

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: 285.47  E-value: 3.47e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLV---KHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLyIV 82
Cdd:cd08222    2 YRVVRKLGSGNFGTVYLVsdlKATADEELKVLKEISVGELQPDETVDANREAKLLSKLDHPAIVKFHDSFVEKESFC-IV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  83 MGFCEGGDLYRKLKE--QKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLtRTNIIKVGDLGIARVLENHC 160
Cdd:cd08222   81 TEYCEGGDLDDKISEykKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFL-KNNVIKVGDFGISRILMGTS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 161 DMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPRDYSPELAELIRT 240
Cdd:cd08222  160 DLATTFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVEGETPSLPDKYSKELNAIYSR 239
                        250       260
                 ....*....|....*....|.
gi 148839316 241 MLSKRPEERPSVRSILRQPYI 261
Cdd:cd08222  240 MLNKDPALRPSAAEILKIPFI 260
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
6-261 1.27e-88

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: 281.08  E-value: 1.27e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGF 85
Cdd:cd08225    2 YEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKEKEASKKEVILLAKMKHPNIVTFFASFQE-NGRLFIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGGDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNII-KVGDLGIARVLENHCDMAS 164
Cdd:cd08225   81 CDGGDLMKRINRQRGVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVaKLGDFGIARQLNDSMELAY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 TLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPRDYSPELAELIRTMLSK 244
Cdd:cd08225  161 TCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNNLHQLVLKICQGYFAPISPNFSRDLRSLISQLFKV 240
                        250
                 ....*....|....*..
gi 148839316 245 RPEERPSVRSILRQPYI 261
Cdd:cd08225  241 SPRDRPSITSILKRPFL 257
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
9-259 1.79e-87

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii CNK2 has both cilliary and cell cycle functions. It influences flagellar length through promoting flagellar disassembly, and it regulates cell size, through influencing the size threshold at which cells commit to mitosis. This subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes CNK1, and -2. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 278.12  E-value: 1.79e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDgLLYIVMGFCEG 88
Cdd:cd08530    5 LKKLGKGSYGSVYKVKRLSDNQVYALKEVNLGSLSQKEREDSVNEIRLLASVNHPNIIRYKEAFLDGN-RLCIVMEYAPF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  89 GDLYRKLKEQK--GQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENhcDMASTL 166
Cdd:cd08530   84 GDLSKLISKRKkkRRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISKVLKK--NLAKTQ 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 167 IGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPRDYSPELAELIRTMLSKRP 246
Cdd:cd08530  162 IGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQELRYKVCRGKFPPIPPVYSQDLQQIIRSLLQVNP 241
                        250
                 ....*....|...
gi 148839316 247 EERPSVRSILRQP 259
Cdd:cd08530  242 KKRPSCDKLLQSP 254
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
5-261 7.92e-83

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: 265.83  E-value: 7.92e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   5 AYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLyIVMG 84
Cdd:cd08221    1 HYIPVRVLGRGAFGEAVLYRKTEDNSLVVWKEVNLSRLSEKERRDALNEIDILSLLNHDNIITYYNHFLDGESLF-IEME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGGDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMAS 164
Cdd:cd08221   80 YCNGGNLHDKIAQQKNQLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVLDSESSMAE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 TLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPRDYSPELAELIRTMLSK 244
Cdd:cd08221  160 SIVGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFDATNPLRLAVKIVQGEYEDIDEQYSEEIIQLVHDCLHQ 239
                        250
                 ....*....|....*..
gi 148839316 245 RPEERPSVRSILRQPYI 261
Cdd:cd08221  240 DPEDRPTAEELLERPLL 256
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
6-261 1.99e-77

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: 251.58  E-value: 1.99e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGF 85
Cdd:cd08220    2 YEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIPVEQMTKEERQAALNEVKVLSMLHHPNIIEYYESFLE-DKALMIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGGDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTR-TNIIKVGDLGIARVLeNHCDMAS 164
Cdd:cd08220   81 APGGTLFEYIQQRKGSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKkRTVVKIGDFGISKIL-SSKSKAY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 TLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPRDYSPELAELIRTMLSK 244
Cdd:cd08220  160 TVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMRGTFAPISDRYSEELRHLILSMLHL 239
                        250
                 ....*....|....*..
gi 148839316 245 RPEERPSVRSILRQPYI 261
Cdd:cd08220  240 DPNKRPTLSEIMAQPII 256
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
9-258 9.61e-74

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: 241.72  E-value: 9.61e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRE-RRAAEQEAQLLSQLKHPNIVT---YKESweggDGLLYIVMG 84
Cdd:cd14014    5 VRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEfRERFLREARALARLSHPNIVRvydVGED----DGRPYIVME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGGDLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVL-ENHCDMA 163
Cdd:cd14014   81 YVEGGSLADLLRERGP--LPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALgDSGLTQT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 164 STLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPR---DYSPELAELIRT 240
Cdd:cd14014  159 GSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPlnpDVPPALDAIILR 238
                        250
                 ....*....|....*....
gi 148839316 241 MLSKRPEERP-SVRSILRQ 258
Cdd:cd14014  239 ALAKDPEERPqSAAELLAA 257
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
12-258 4.85e-73

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: 239.87  E-value: 4.85e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRN-ASSRERRAAEQEAQLLSQLKHPNIVTYKESW-EGGDglLYIVMGFCEGG 89
Cdd:cd08224    8 IGKGQFSVVYRARCLLDGRLVALKKVQIFEmMDAKARQDCLKEIDLLQQLNHPNIIKYLASFiENNE--LNIVLELADAG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  90 DLYRKLKE--QKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTLI 167
Cdd:cd08224   86 DLSRLIKHfkKQKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGLGRFFSSKTTAAHSLV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 168 GTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMN--SLVYRIIEGKLPPMPRD-YSPELAELIRTMLSK 244
Cdd:cd08224  166 GTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYGEKMNlySLCKKIEKCEYPPLPADlYSQELRDLVAACIQP 245
                        250
                 ....*....|....
gi 148839316 245 RPEERPSVRSILRQ 258
Cdd:cd08224  246 DPEKRPDISYVLDV 259
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
6-257 5.56e-73

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 247.23  E-value: 5.56e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAA-EQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMG 84
Cdd:COG0515    9 YRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARERfRREARALARLNHPNIVRVYDVGEE-DGRPYLVME 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGGDLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVL-ENHCDMA 163
Cdd:COG0515   88 YVEGESLADLLRRRGP--LPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALgGATLTQT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 164 STLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPR---DYSPELAELIRT 240
Cdd:COG0515  166 GTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSElrpDLPPALDAIVLR 245
                        250
                 ....*....|....*...
gi 148839316 241 MLSKRPEERP-SVRSILR 257
Cdd:COG0515  246 ALAKDPEERYqSAAELAA 263
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
10-261 1.10e-68

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: 227.79  E-value: 1.10e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESwEGGDGLLYIVMGFCEGG 89
Cdd:cd06606    6 ELLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEELEALEREIRILSSLKHPNIVRYLGT-ERTENTLNIFLEYVPGG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  90 DLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMAS--TLI 167
Cdd:cd06606   85 SLASLLKKFGK--LPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKRLAEIATGEGtkSLR 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 168 GTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAF-NAKDMNSLVYRIIEGK-LPPMPRDYSPELAELIRTMLSKR 245
Cdd:cd06606  163 GTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWsELGNPVAALFKIGSSGePPPIPEHLSEEAKDFLRKCLQRD 242
                        250
                 ....*....|....*.
gi 148839316 246 PEERPSVRSILRQPYI 261
Cdd:cd06606  243 PKKRPTADELLQHPFL 258
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
13-259 2.97e-67

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: 222.53  E-value: 2.97e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  13 GKGSYGEVTLVKHRRDGKQYVIKKLNLRNaSSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLlYIVMGFCEGGDLY 92
Cdd:cd00180    2 GKGSFGKVYKARDKETGKKVAVKVIPKEK-LKKLLEELLREIEILKKLNHPNIVKLYDVFETENFL-YLVMEYCEGGSLK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  93 RKLKEQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTLIG--TP 170
Cdd:cd00180   80 DLLKENKGPL-SEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKTTGGttPP 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 171 YYMSPELFSNKPYNYKSDVWALGCCVYEMatlkhafnakdmnslvyriiegklppmprdysPELAELIRTMLSKRPEERP 250
Cdd:cd00180  159 YYAPPELLGGRYYGPKVDIWSLGVILYEL--------------------------------EELKDLIRRMLQYDPKKRP 206

                 ....*....
gi 148839316 251 SVRSILRQP 259
Cdd:cd00180  207 SAKELLEHL 215
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
6-259 6.86e-66

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: 220.43  E-value: 6.86e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDgLLYIVMGF 85
Cdd:cd05117    2 YELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDK-NLYLVMEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGGDLYRKLKEQKgqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNI---IKVGDLGIARVLENHCDM 162
Cdd:cd05117   81 CTGGELFDRIVKKG--SFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPdspIKIIDFGLAKIFEEGEKL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 163 aSTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKL---PPMPRDYSPELAELIR 239
Cdd:cd05117  159 -KTVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYsfdSPEWKNVSEEAKDLIK 237
                        250       260
                 ....*....|....*....|
gi 148839316 240 TMLSKRPEERPSVRSILRQP 259
Cdd:cd05117  238 RLLVVDPKKRLTAAEALNHP 257
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
12-256 9.07e-65

Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway.


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 217.02  E-value: 9.07e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRrdGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKesweG---GDGLLYIVMGFCEG 88
Cdd:cd13999    1 IGSGSFGEVYKGKWR--GTDVAIKKLKVEDDNDELLKEFRREVSILSKLRHPNIVQFI----GaclSPPPLCIVTEYMPG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  89 GDLYRKLKEQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTLIG 168
Cdd:cd13999   75 GSLYDLLHKKKIPL-SWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKMTGVVG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 169 TPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAF-NAKDMNSLVYRIIEGKLPPMPRDYSPELAELIRTMLSKRPE 247
Cdd:cd13999  154 TPRWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFkELSPIQIAAAVVQKGLRPPIPPDCPPELSKLIKRCWNEDPE 233

                 ....*....
gi 148839316 248 ERPSVRSIL 256
Cdd:cd13999  234 KRPSFSEIV 242
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
6-261 7.14e-64

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: 214.76  E-value: 7.14e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRnaSSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLlYIVMGF 85
Cdd:cd05122    2 FEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLE--SKEKKESILNEIAILKKCKHPNIVKYYGSYLKKDEL-WIVMEF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGGDLYRKLKEqKGQLLPENQVVewFV--QIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDmA 163
Cdd:cd05122   79 CSGGSLKDLLKN-TNKTLTEQQIA--YVckEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQLSDGKT-R 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 164 STLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIieGKLPPM----PRDYSPELAELIR 239
Cdd:cd05122  155 NTFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLI--ATNGPPglrnPKKWSKEFKDFLK 232
                        250       260
                 ....*....|....*....|..
gi 148839316 240 TMLSKRPEERPSVRSILRQPYI 261
Cdd:cd05122  233 KCLQKDPEKRPTAEQLLKHPFI 254
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
9-260 1.82e-59

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: 202.75  E-value: 1.82e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDgLLYIVMGFCEG 88
Cdd:cd14003    5 GKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETEN-KIYLVMEYASG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  89 GDLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMaSTLIG 168
Cdd:cd14003   84 GELFDYIVNNGR--LSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNEFRGGSLL-KTFCG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 169 TPYYMSPELFSNKPYN-YKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKlPPMPRDYSPELAELIRTMLSKRPE 247
Cdd:cd14003  161 TPAYAAPEVLLGRKYDgPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGK-YPIPSHLSPDARDLIRRMLVVDPS 239
                        250
                 ....*....|...
gi 148839316 248 ERPSVRSILRQPY 260
Cdd:cd14003  240 KRITIEEILNHPW 252
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
12-249 2.84e-58

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: 199.28  E-value: 2.84e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRNAssRERRAAEQ---EAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGFCEG 88
Cdd:cd05123    1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEI--IKRKEVEHtlnERNILERVNHPFIVKLHYAFQT-EEKLYLVLDYVPG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  89 GDLYRKLKEQKgqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTLIG 168
Cdd:cd05123   78 GELFSHLSKEG--RFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSDGDRTYTFCG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 169 TPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLpPMPRDYSPELAELIRTMLSKRPEE 248
Cdd:cd05123  156 TPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPL-KFPEYVSPEAKSLISGLLQKDPTK 234

                 .
gi 148839316 249 R 249
Cdd:cd05123  235 R 235
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
13-261 5.19e-58

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: 199.32  E-value: 5.19e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  13 GKGSYGEVTLVKHRRDGKQYVIKKLN---LRNASSRERRAAEQEAQL---------LSQLKHPNIVTYKESWEGGDGL-L 79
Cdd:cd14008    2 GRGSFGKVKLALDTETGQLYAIKIFNksrLRKRREGKNDRGKIKNALddvrreiaiMKKLDHPNIVRLYEVIDDPESDkL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  80 YIVMGFCEGGDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENH 159
Cdd:cd14008   82 YLVLEYCEGGPVMELDSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGVSEMFEDG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 160 CDMASTLIGTPYYMSPELF--SNKPYN-YKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLP-PMPRDYSPELA 235
Cdd:cd14008  162 NDTLQKTAGTPAFLAPELCdgDSKTYSgKAADIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQNDEfPIPPELSPELK 241
                        250       260
                 ....*....|....*....|....*.
gi 148839316 236 ELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd14008  242 DLLRRMLEKDPEKRITLKEIKEHPWV 267
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
9-262 1.00e-57

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: 198.20  E-value: 1.00e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLrNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGFCEG 88
Cdd:cd06623    6 VKVLGQGSSGVVYKVRHKPTGKIYALKKIHV-DGDEEFRKQLLRELKTLRSCESPYVVKCYGAFYK-EGEISIVLEYMDG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  89 GDLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLH-EKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTLI 167
Cdd:cd06623   84 GSLADLLKKVGK--IPEPVLAYIARQILKGLDYLHtKRHIIHRDIKPSNLLINSKGEVKIADFGISKVLENTLDQCNTFV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 168 GTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNS---LVYRIIEGKLPPMP-RDYSPELAELIRTMLS 243
Cdd:cd06623  162 GTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPGQPSffeLMQAICDGPPPSLPaEEFSPEFRDFISACLQ 241
                        250
                 ....*....|....*....
gi 148839316 244 KRPEERPSVRSILRQPYIK 262
Cdd:cd06623  242 KDPKKRPSAAELLQHPFIK 260
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
9-262 5.49e-57

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: 195.77  E-value: 5.49e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRE-----RRaaeqEAQLLSQLKHPNIV-TYKESWEggDGLLYIV 82
Cdd:cd14007    5 GKPLGKGKFGNVYLAREKKSGFIVALKVISKSQLQKSGlehqlRR----EIEIQSHLRHPNILrLYGYFED--KKRIYLI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  83 MGFCEGGDLYRKLKEQKgqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHcdM 162
Cdd:cd14007   79 LEYAPNGELYKELKKQK--RFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWSVHAPSN--R 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 163 ASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLpPMPRDYSPELAELIRTML 242
Cdd:cd14007  155 RKTFCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDI-KFPSSVSPEAKDLISKLL 233
                        250       260
                 ....*....|....*....|
gi 148839316 243 SKRPEERPSVRSILRQPYIK 262
Cdd:cd14007  234 QKDPSKRLSLEQVLNHPWIK 253
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
3-257 2.25e-56

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: 194.86  E-value: 2.25e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   3 LAAYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNL-RNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYI 81
Cdd:cd08228    1 LANFQIEKKIGRGQFSEVYRATCLLDRKPVALKKVQIfEMMDAKARQDCVKEIDLLKQLNHPNVIKYLDSFIE-DNELNI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  82 VMGFCEGGDLYRKLK--EQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENH 159
Cdd:cd08228   80 VLELADAGDLSQMIKyfKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 160 CDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMN--SLVYRIIEGKLPPMPRD-YSPELAE 236
Cdd:cd08228  160 TTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNlfSLCQKIEQCDYPPLPTEhYSEKLRE 239
                        250       260
                 ....*....|....*....|.
gi 148839316 237 LIRTMLSKRPEERPSVRSILR 257
Cdd:cd08228  240 LVSMCIYPDPDQRPDIGYVHQ 260
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
9-258 1.37e-55

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: 192.89  E-value: 1.37e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAaEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGFCEG 88
Cdd:cd13996   11 IELLGSGGFGSVYKVRNKVDGVTYAIKKIRLTEKSSASEKV-LREVKALAKLNHPNIVRYYTAWVE-EPPLYIQMELCEG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  89 GDLY----RKLKEQKGQllpENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLT-RTNIIKVGDLGIARVLENHCDMA 163
Cdd:cd13996   89 GTLRdwidRRNSSSKND---RKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDnDDLQVKIGDFGLATSIGNQKREL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 164 --------------STLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMAtlkHAFN-----AKDMNSLVyriiEGKLP 224
Cdd:cd13996  166 nnlnnnnngntsnnSVGIGTPLYASPEQLDGENYNEKADIYSLGIILFEML---HPFKtamerSTILTDLR----NGILP 238
                        250       260       270
                 ....*....|....*....|....*....|....
gi 148839316 225 PMPRDYSPELAELIRTMLSKRPEERPSVRSILRQ 258
Cdd:cd13996  239 ESFKAKHPKEADLIQSLLSKNPEERPSAEQLLRS 272
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
10-261 5.24e-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: 187.99  E-value: 5.24e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAA---EQEAQLLSQLKHPNIVTYKESwEGGDGLLYIVMGFC 86
Cdd:cd06632    6 QLLGSGSFGSVYEGFNGDTGDFFAVKEVSLVDDDKKSRESVkqlEQEIALLSKLRHPNIVQYYGT-EREEDNLYIFLEYV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  87 EGGDLYRKLkeQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHcDMASTL 166
Cdd:cd06632   85 PGGSIHKLL--QRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHVEAF-SFAKSF 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 167 IGTPYYMSPELFS--NKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRII-EGKLPPMPRDYSPELAELIRTMLS 243
Cdd:cd06632  162 KGSPYWMAPEVIMqkNSGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIGnSGELPPIPDHLSPDAKDFIRLCLQ 241
                        250
                 ....*....|....*...
gi 148839316 244 KRPEERPSVRSILRQPYI 261
Cdd:cd06632  242 RDPEDRPTASQLLEHPFV 259
Pkinase pfam00069
Protein kinase domain;
6-261 7.23e-54

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 185.91  E-value: 7.23e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316    6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGlLYIVMGF 85
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDN-LYLVLEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   86 CEGGDLYRKLKEQKGqlLPENQVVEWFVQiamalqylhekhilhrdlktqnvfltrtniikvgdlgIARVLENHCDMaST 165
Cdd:pfam00069  80 VEGGSLFDLLSEKGA--FSEREAKFIMKQ-------------------------------------ILEGLESGSSL-TT 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  166 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKL--PPMPRDYSPELAELIRTMLS 243
Cdd:pfam00069 120 FVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYafPELPSNLSEEAKDLLKKLLK 199
                         250
                  ....*....|....*...
gi 148839316  244 KRPEERPSVRSILRQPYI 261
Cdd:pfam00069 200 KDPSKRLTATQALQHPWF 217
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
12-261 1.18e-52

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: 183.97  E-value: 1.18e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGkQYV-IKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDgLLYIVMGFCEGGD 90
Cdd:cd06627    8 IGRGAFGSVYKGLNLNTG-EFVaIKQISLEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKD-SLYIILEYVENGS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  91 LYRKLKeqKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIA-RVLENHcDMASTLIGT 169
Cdd:cd06627   86 LASIIK--KFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVAtKLNEVE-KDENSVVGT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 170 PYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLvYRIIEGKLPPMPRDYSPELAELIRTMLSKRPEE 248
Cdd:cd06627  163 PYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPyYDLQPMAAL-FRIVQDDHPPLPENISPELRDFLLQCFQKDPTL 241
                        250
                 ....*....|...
gi 148839316 249 RPSVRSILRQPYI 261
Cdd:cd06627  242 RPSAKELLKHPWL 254
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
6-252 1.47e-52

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: 184.24  E-value: 1.47e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLV-KHRRDGKQYVIKKLNLRNASSRERRAAEQEA--QLLS-------QLKHPNIVTYKESWEGG 75
Cdd:cd08528    2 YAVLELLGSGAFGCVYKVrKKSNGQTLLALKEINMTNPAFGRTEQERDKSvgDIISevniikeQLRHPNIVRYYKTFLEN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  76 DGLlYIVMGFCEG---GDLYRKLKEQKGQLlPENQVVEWFVQIAMALQYLH-EKHILHRDLKTQNVFLTRTNIIKVGDLG 151
Cdd:cd08528   82 DRL-YIVMELIEGaplGEHFSSLKEKNEHF-TEDRIWNIFVQMVLALRYLHkEKQIVHRDLKPNNIMLGEDDKVTITDFG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 152 IARVLENHCDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPRD-Y 230
Cdd:cd08528  160 LAKQKGPESSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIVEAEYEPLPEGmY 239
                        250       260
                 ....*....|....*....|..
gi 148839316 231 SPELAELIRTMLSKRPEERPSV 252
Cdd:cd08528  240 SDDITFVIRSCLTPDPEARPDI 261
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
6-261 1.72e-52

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: 183.52  E-value: 1.72e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQY---VIKKLNLRNASSRERraAEQEAQLLSQLKHPNIVTYKESWEGGDGLlYIV 82
Cdd:cd14099    3 YRRGKFLGKGGFAKCYEVTDMSTGKVYagkVVPKSSLTKPKQREK--LKSEIKIHRSLKHPNIVKFHDCFEDEENV-YIL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  83 MGFCEGGDLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDM 162
Cdd:cd14099   80 LELCSNGSLMELLKRRKA--LTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAARLEYDGER 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 163 ASTLIGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEG--KLPPMPrDYSPELAELIR 239
Cdd:cd14099  158 KKTLCGTPNYIAPEvLEKKKGHSFEVDIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNeySFPSHL-SISDEAKDLIR 236
                        250       260
                 ....*....|....*....|..
gi 148839316 240 TMLSKRPEERPSVRSILRQPYI 261
Cdd:cd14099  237 SMLQPDPTKRPSLDEILSHPFF 258
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
3-252 2.20e-52

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: 184.46  E-value: 2.20e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   3 LAAYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRN-ASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYI 81
Cdd:cd08229   23 LANFRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIFDlMDAKARADCIKEIDLLKQLNHPNVIKYYASFIE-DNELNI 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  82 VMGFCEGGDLYRKLKEQKGQ--LLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENH 159
Cdd:cd08229  102 VLELADAGDLSRMIKHFKKQkrLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSK 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 160 CDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMN--SLVYRIIEGKLPPMPRD-YSPELAE 236
Cdd:cd08229  182 TTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNlySLCKKIEQCDYPPLPSDhYSEELRQ 261
                        250
                 ....*....|....*.
gi 148839316 237 LIRTMLSKRPEERPSV 252
Cdd:cd08229  262 LVNMCINPDPEKRPDI 277
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
9-258 2.72e-52

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: 183.08  E-value: 2.72e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316    9 LRVVGKGSYGEV---TLVKHRRDGKQYV-IKKLNlRNASSRERRAAEQEAQLLSQLKHPNIVTYKesweG---GDGLLYI 81
Cdd:pfam07714   4 GEKLGEGAFGEVykgTLKGEGENTKIKVaVKTLK-EGADEEEREDFLEEASIMKKLDHPNIVKLL----GvctQGEPLYI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   82 VMGFCEGGDLYRKLKEQKGQLLPEnQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCD 161
Cdd:pfam07714  79 VTEYMPGGDLLDFLRKHKRKLTLK-DLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDIYDDDY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  162 MASTLIG-TPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATL-KHAFNAKDMNSLVYRIIEGKLPPMPRDYSPELAELI 238
Cdd:pfam07714 158 YRKRGGGkLPIkWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLgEQPYPGMSNEEVLEFLEDGYRLPQPENCPDELYDLM 237
                         250       260
                  ....*....|....*....|
gi 148839316  239 RTMLSKRPEERPSVRSILRQ 258
Cdd:pfam07714 238 KQCWAYDPEDRPTFSELVED 257
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
12-249 6.31e-52

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: 181.65  E-value: 6.31e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDgLLYIVMGFCEGGDL 91
Cdd:cd14009    1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNKKLQENLESEIAILKSIKHPNIVRLYDVQKTED-FIYLVLEYCAGGDL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  92 YRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTN---IIKVGDLGIARVLENHcDMASTLIG 168
Cdd:cd14009   80 SQYIRKRGR--LPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGddpVLKIADFGFARSLQPA-SMAETLCG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 169 TPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKL---PPMPRDYSPELAELIRTMLSKR 245
Cdd:cd14009  157 SPLYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIERSDAvipFPIAAQLSPDCKDLLRRLLRRD 236

                 ....
gi 148839316 246 PEER 249
Cdd:cd14009  237 PAER 240
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
8-259 1.20e-51

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: 181.04  E-value: 1.20e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   8 YLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLK-HPNIVTYKESWEGGdGLLYIVMGFC 86
Cdd:cd13997    4 ELEQIGSGSFSEVFKVRSKVDGCLYAVKKSKKPFRGPKERARALREVEAHAALGqHPNIVRYYSSWEEG-GHLYIQMELC 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  87 EGGDLYRKLKEQ-KGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASt 165
Cdd:cd13997   83 ENGSLQDALEELsPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATRLETSGDVEE- 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 liGTPYYMSPELFSNKP-YNYKSDVWALGCCVYEMATlkhAFNAKDMNSLVYRIIEGKLPPMPRD-YSPELAELIRTMLS 243
Cdd:cd13997  162 --GDSRYLAPELLNENYtHLPKADIFSLGVTVYEAAT---GEPLPRNGQQWQQLRQGKLPLPPGLvLSQELTRLLKVMLD 236
                        250
                 ....*....|....*.
gi 148839316 244 KRPEERPSVRSILRQP 259
Cdd:cd13997  237 PDPTRRPTADQLLAHD 252
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
10-258 7.59e-51

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: 179.27  E-value: 7.59e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYV---IKKLNLrNASSRERRAAEQEAQLLSQLKHPNIV------TYKESweggdglLY 80
Cdd:cd00192    1 KKLGEGAFGEVYKGKLKGGDGKTVdvaVKTLKE-DASESERKDFLKEARVMKKLGHPNVVrllgvcTEEEP-------LY 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  81 IVMGFCEGGDLYRKLKEQKGQL-------LPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIA 153
Cdd:cd00192   73 LVMEYMEGGDLLDFLRKSRPVFpspepstLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 154 RVLENHcDMASTLIGTP---YYMSPELFSNKPYNYKSDVWALGCCVYEMATL-KHAFNAKDMNSLVYRIIEGKLPPMPRD 229
Cdd:cd00192  153 RDIYDD-DYYRKKTGGKlpiRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTLgATPYPGLSNEEVLEYLRKGYRLPKPEN 231
                        250       260
                 ....*....|....*....|....*....
gi 148839316 230 YSPELAELIRTMLSKRPEERPSVRSILRQ 258
Cdd:cd00192  232 CPDELYELMLSCWQLDPEDRPTFSELVER 260
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
9-258 1.23e-50

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: 178.51  E-value: 1.23e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316     9 LRVVGKGSYGEV---TLVKHRRDGKQYV-IKKLNlRNASSRERRAAEQEAQLLSQLKHPNIVTYKesweG---GDGLLYI 81
Cdd:smart00221   4 GKKLGEGAFGEVykgTLKGKGDGKEVEVaVKTLK-EDASEQQIEEFLREARIMRKLDHPNIVKLL----GvctEEEPLMI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316    82 VMGFCEGGDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCD 161
Cdd:smart00221  79 VMEYMPGGDLLDYLRKNRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDY 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   162 MASTLIGTPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATL-KHAFNAKDMNSLVYRIIEGKLPPMPRDYSPELAELIR 239
Cdd:smart00221 159 YKVKGGKLPIrWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLgEEPYPGMSNAEVLEYLKKGYRLPKPPNCPPELYKLML 238
                          250
                   ....*....|....*....
gi 148839316   240 TMLSKRPEERPSVRSILRQ 258
Cdd:smart00221 239 QCWAEDPEDRPTFSELVEI 257
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
6-263 1.38e-50

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: 178.98  E-value: 1.38e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLrNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLlYIVMGF 85
Cdd:cd06609    3 FTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDL-EEAEDEIEDIQQEIQFLSQCDSPYITKYYGSFLKGSKL-WIIMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGGDLYRKLKEQKgqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMAST 165
Cdd:cd06609   81 CGGGSVLDLLKPGP---LDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSGQLTSTMSKRNT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPRD-YSPELAELIRTMLSK 244
Cdd:cd06609  158 FVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLSDLHPMRVLFLIPKNNPPSLEGNkFSKPFKDFVELCLNK 237
                        250
                 ....*....|....*....
gi 148839316 245 RPEERPSVRSILRQPYIKR 263
Cdd:cd06609  238 DPKERPSAKELLKHKFIKK 256
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
9-258 2.57e-49

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 174.64  E-value: 2.57e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316     9 LRVVGKGSYGEV---TLVKHRRDGKQYV-IKKLNlRNASSRERRAAEQEAQLLSQLKHPNIVTYKesweG---GDGLLYI 81
Cdd:smart00219   4 GKKLGEGAFGEVykgKLKGKGGKKKVEVaVKTLK-EDASEQQIEEFLREARIMRKLDHPNVVKLL----GvctEEEPLYI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316    82 VMGFCEGGDLYRKLKEQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCD 161
Cdd:smart00219  79 VMEYMEGGDLLSYLRKNRPKL-SLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDY 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   162 MASTLIGTPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATL-KHAFNAKDMNSLVYRIIEGKLPPMPRDYSPELAELIR 239
Cdd:smart00219 158 YRKRGGKLPIrWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLgEQPYPGMSNEEVLEYLKNGYRLPQPPNCPPELYDLML 237
                          250
                   ....*....|....*....
gi 148839316   240 TMLSKRPEERPSVRSILRQ 258
Cdd:smart00219 238 QCWAEDPEDRPTFSELVEI 256
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
6-262 3.35e-49

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: 174.32  E-value: 3.35e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASsreRRAAEQEAQLLSQLKHPNIVTYKESWEGGDgLLYIVMGF 85
Cdd:cd06614    2 YKNLEKIGEGASGEVYKATDRATGKEVAIKKMRLRKQN---KELIINEILIMKECKHPNIVDYYDSYLVGD-ELWVVMEY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGGDLyRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMAST 165
Cdd:cd06614   78 MDGGSL-TDIITQNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAAQLTKEKSKRNS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMA--TLKHaFNAKDMNSLvYRIIEGKLPPM--PRDYSPELAELIRTM 241
Cdd:cd06614  157 VVGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAegEPPY-LEEPPLRAL-FLITTKGIPPLknPEKWSPEFKDFLNKC 234
                        250       260
                 ....*....|....*....|.
gi 148839316 242 LSKRPEERPSVRSILRQPYIK 262
Cdd:cd06614  235 LVKDPEKRPSAEELLQHPFLK 255
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
6-261 1.43e-48

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: 172.44  E-value: 1.43e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGF 85
Cdd:cd14002    3 YHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPKRGKSEKELRNLRQEIEILRKLNHPNIIEMLDSFET-KKEFVVVTEY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGgDLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMAST 165
Cdd:cd14002   82 AQG-ELFQILEDDGT--LPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARAMSCNTLVLTS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLpPMPRDYSPELAELIRTMLSKR 245
Cdd:cd14002  159 IKGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIVKDPV-KWPSNMSPEFKSFLQGLLNKD 237
                        250
                 ....*....|....*.
gi 148839316 246 PEERPSVRSILRQPYI 261
Cdd:cd14002  238 PSKRLSWPDLLEHPFV 253
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
6-261 1.84e-48

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: 172.37  E-value: 1.84e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQ--YVIKKLNLRNASS--RER---RaaeqEAQLLSQLKHPNIVTYKESWEGGdGL 78
Cdd:cd14080    2 YRLGKTIGEGSYSKVKLAEYTKSGLKekVACKIIDKKKAPKdfLEKflpR----ELEILRKLRHPNIIQVYSIFERG-SK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  79 LYIVMGFCEGGDLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVL-- 156
Cdd:cd14080   77 VFIFMEYAEHGDLLEYIQKRGA--LSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFARLCpd 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 157 ENHCDMASTLIGTPYYMSPELFSNKPYNYK-SDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKL--PPMPRDYSPE 233
Cdd:cd14080  155 DDGDVLSKTFCGSAAYAAPEILQGIPYDPKkYDIWSLGVILYIMLCGSMPFDDSNIKKMLKDQQNRKVrfPSSVKKLSPE 234
                        250       260
                 ....*....|....*....|....*...
gi 148839316 234 LAELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd14080  235 CKDLIDQLLEPDPTKRATIEEILNHPWL 262
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
11-261 4.23e-48

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: 171.29  E-value: 4.23e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  11 VVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSrerrAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGFCEGGD 90
Cdd:cd06612   10 KLGEGSYGSVYKAIHKETGQVVAIKVVPVEEDLQ----EIIKEISILKQCDSPYIVKYYGSYFK-NTDLWIVMEYCGAGS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  91 LyRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTLIGTP 170
Cdd:cd06612   85 V-SDIMKITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLTDTMAKRNTVIGTP 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 171 YYMSPELFSNKPYNYKSDVWALGCCVYEMATLK------HAFNAKDMnslvyriIEGKLPPM---PRDYSPELAELIRTM 241
Cdd:cd06612  164 FWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKppysdiHPMRAIFM-------IPNKPPPTlsdPEKWSPEFNDFVKKC 236
                        250       260
                 ....*....|....*....|
gi 148839316 242 LSKRPEERPSVRSILRQPYI 261
Cdd:cd06612  237 LVKDPEERPSAIQLLQHPFI 256
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
4-264 6.34e-48

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: 171.50  E-value: 6.34e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   4 AAYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLrNASSRERRAAEQEAQLLSQLKH---PNIVTYKESWEGGDGLlY 80
Cdd:cd06917    1 SLYRRLELVGRGSYGAVYRGYHVKTGRVVALKVLNL-DTDDDDVSDIQKEVALLSQLKLgqpKNIIKYYGSYLKGPSL-W 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  81 IVMGFCEGGDLYRKLKEQKgqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHC 160
Cdd:cd06917   79 IIMDYCEGGSIRTLMRAGP---IAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQNS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 161 DMASTLIGTPYYMSPELFSN-KPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMP-RDYSPELAELI 238
Cdd:cd06917  156 SKRSTFVGTPYWMAPEVITEgKYYDTKADIWSLGITTYEMATGNPPYSDVDALRAVMLIPKSKPPRLEgNGYSPLLKEFV 235
                        250       260
                 ....*....|....*....|....*.
gi 148839316 239 RTMLSKRPEERPSVRSILRQPYIKRQ 264
Cdd:cd06917  236 AACLDEEPKDRLSADELLKSKWIKQH 261
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
10-270 2.31e-46

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 173.52  E-value: 2.31e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLL------SQLK-HPNIVTYKESWEGGDGLLYIV 82
Cdd:PTZ00283  38 RVLGSGATGTVLCAKRVSDGEPFAVKVVDMEGMSEADKNRAQAEVCCLlncdffSIVKcHEDFAKKDPRNPENVLMIALV 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  83 MGFCEGGDLYRKLKE--QKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHC 160
Cdd:PTZ00283 118 LDYANAGDLRQEIKSraKTNRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDFGFSKMYAATV 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 161 --DMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPRDYSPELAELI 238
Cdd:PTZ00283 198 sdDVGRTFCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGENMEEVMHKTLAGRYDPLPPSISPEMQEIV 277
                        250       260       270
                 ....*....|....*....|....*....|..
gi 148839316 239 RTMLSKRPEERPSVRSILRQPYIKRQISFFLE 270
Cdd:PTZ00283 278 TALLSSDPKRRPSSSKLLNMPICKLFISGLLE 309
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
12-261 1.08e-45

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: 164.79  E-value: 1.08e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRNasSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDgLLYIVMGFCEGG-- 89
Cdd:cd06613    8 IGSGTYGDVYKARNIATGELAAVKVIKLEP--GDDFEIIQQEISMLKECRHPNIVAYFGSYLRRD-KLWIVMEYCGGGsl 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  90 -DLYRKLKEqkgqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTLIG 168
Cdd:cd06613   85 qDIYQVTGP-----LSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQLTATIAKRKSFIG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 169 TPYYMSPELFSNK---PYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLVYRIIEGKLPPMPRD---YSPELAELIRTM 241
Cdd:cd06613  160 TPYWMAPEVAAVErkgGYDGKCDIWALGITAIELAELQPPmFDLHPMRALFLIPKSNFDPPKLKDkekWSPDFHDFIKKC 239
                        250       260
                 ....*....|....*....|
gi 148839316 242 LSKRPEERPSVRSILRQPYI 261
Cdd:cd06613  240 LTKNPKKRPTATKLLQHPFV 259
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
10-261 1.33e-45

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: 164.35  E-value: 1.33e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRE-RRAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGFCEG 88
Cdd:cd14081    7 KTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKESvLMKVEREIAIMKLIEHPNVLKLYDVYEN-KKYLYLVLEYVSG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  89 GDLYRKLKEqKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARvLENHCDMASTLIG 168
Cdd:cd14081   86 GELFDYLVK-KGRL-TEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMAS-LQPEGSLLETSCG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 169 TPYYMSPELFSNKPYN-YKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKlPPMPRDYSPELAELIRTMLSKRPE 247
Cdd:cd14081  163 SPHYACPEVIKGEKYDgRKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGV-FHIPHFISPDAQDLLRRMLEVNPE 241
                        250
                 ....*....|....
gi 148839316 248 ERPSVRSILRQPYI 261
Cdd:cd14081  242 KRITIEEIKKHPWF 255
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
11-261 3.30e-45

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: 163.63  E-value: 3.30e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  11 VVGKGSYGEVTLVKHRRDGKQYVIKKLNLrnaSSRERRAAEQEAQLLSQL-KHPNIVTY-----KESWEGGDGLLYIVMG 84
Cdd:cd06608   13 VIGEGTYGKVYKARHKKTGQLAAIKIMDI---IEDEEEEIKLEINILRKFsNHPNIATFygafiKKDPPGGDDQLWLVME 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGG---DLYRKLKeQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCD 161
Cdd:cd06608   90 YCGGGsvtDLVKGLR-KKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGVSAQLDSTLG 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 162 MASTLIGTPYYMSPELFS-----NKPYNYKSDVWALGCCVYEMATLKHAFNakDMNSL--VYRIIEGKLPPM--PRDYSP 232
Cdd:cd06608  169 RRNTFIGTPYWMAPEVIAcdqqpDASYDARCDVWSLGITAIELADGKPPLC--DMHPMraLFKIPRNPPPTLksPEKWSK 246
                        250       260
                 ....*....|....*....|....*....
gi 148839316 233 ELAELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd06608  247 EFNDFISECLIKNYEQRPFTEELLEHPFI 275
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
9-249 3.91e-45

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: 163.90  E-value: 3.91e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRN-ASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGFCE 87
Cdd:cd05580    6 LKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKiIKLKQVEHVLNEKRILSEVRHPFIVNLLGSFQD-DRNLYMVMEYVP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  88 GGDLYRKLKeqKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCdmaSTLI 167
Cdd:cd05580   85 GGELFSLLR--RSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKRVKDRT---YTLC 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 168 GTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLpPMPRDYSPELAELIRTMLSKRPE 247
Cdd:cd05580  160 GTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGKI-RFPSFFDPDAKDLIKRLLVVDLT 238

                 ..
gi 148839316 248 ER 249
Cdd:cd05580  239 KR 240
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
6-261 4.87e-45

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: 162.81  E-value: 4.87e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRER-RAAEQEAQLLSQLKHPNIVTYKESWEGGDGLlYIVMG 84
Cdd:cd05578    2 FQILRVIGKGSFGKVCIVQKKDTKKMFAMKYMNKQKCIEKDSvRNVLNELEILQELEHPFLVNLWYSFQDEEDM-YMVVD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGGDLYRKLkeQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHcDMAS 164
Cdd:cd05578   81 LLLGGDLRYHL--QQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATKLTDG-TLAT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 TLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKD--MNSLVYRIIEGKLPPMPRDYSPELAELIRTML 242
Cdd:cd05578  158 STSGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEIHSrtSIEEIRAKFETASVLYPAGWSEEAIDLINKLL 237
                        250       260
                 ....*....|....*....|
gi 148839316 243 SKRPEERPSVRSILRQ-PYI 261
Cdd:cd05578  238 ERDPQKRLGDLSDLKNhPYF 257
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
8-263 1.06e-44

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: 162.13  E-value: 1.06e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   8 YLRVVGKGSYGEVTLVKHRRDGkQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGFCE 87
Cdd:cd06605    5 YLGELGEGNGGVVSKVRHRPSG-QIMAVKVIRLEIDEALQKQILRELDVLHKCNSPYIVGFYGAFYS-EGDISICMEYMD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  88 GGDLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKH-ILHRDLKTQNVFLTRTNIIKVGDLGIARVLENhcDMASTL 166
Cdd:cd06605   83 GGSLDKILKEVGR--IPERILGKIAVAVVKGLIYLHEKHkIIHRDVKPSNILVNSRGQVKLCDFGVSGQLVD--SLAKTF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 167 IGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAF---NAKDMNS---LVYRIIEGKLPPMPRD-YSPELAELIR 239
Cdd:cd06605  159 VGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPYpppNAKPSMMifeLLSYIVDEPPPLLPSGkFSPDFQDFVS 238
                        250       260
                 ....*....|....*....|....
gi 148839316 240 TMLSKRPEERPSVRSILRQPYIKR 263
Cdd:cd06605  239 QCLQKDPTERPSYKELMEHPFIKR 262
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
9-256 1.51e-44

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: 162.15  E-value: 1.51e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAeQEAQLLSQLKHPNIVTYKESW-EGGDglLYIVMGFCE 87
Cdd:cd14046   11 LQVLGKGAFGQVVKVRNKLDGRYYAIKKIKLRSESKNNSRIL-REVMLLSRLNHQHVVRYYQAWiERAN--LYIQMEYCE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  88 GGDLYRKLKEqkGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTLI 167
Cdd:cd14046   88 KSTLRDLIDS--GLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLATSNKLNVELATQDI 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 168 ------------------GTPYYMSPELFSNKP--YNYKSDVWALGCCVYEMAtlkHAFNAKDMNSLVYRIIEGK---LP 224
Cdd:cd14046  166 nkstsaalgssgdltgnvGTALYVAPEVQSGTKstYNEKVDMYSLGIIFFEMC---YPFSTGMERVQILTALRSVsieFP 242
                        250       260       270
                 ....*....|....*....|....*....|...
gi 148839316 225 P-MPRDYSPELAELIRTMLSKRPEERPSVRSIL 256
Cdd:cd14046  243 PdFDDNKHSKQAKLIRWLLNHDPAKRPSAQELL 275
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
6-261 1.86e-44

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: 161.88  E-value: 1.86e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNA-----SSRERraaeqEAQLLSQLKHPNIVTYKESwEGGDGLLY 80
Cdd:cd07829    1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIRLDNEeegipSTALR-----EISLLKELKHPNIVKLLDV-IHTENKLY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  81 IVMGFCEGgDLyRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHC 160
Cdd:cd07829   75 LVFEYCDQ-DL-KKYLDKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLARAFGIPL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 161 DMASTLIGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIE-----------------GK 222
Cdd:cd07829  153 RTYTHEVVTLWYRAPEiLLGSKHYSTAVDIWSVGCIFAELITGKPLFPGDSEIDQLFKIFQilgtpteeswpgvtklpDY 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 148839316 223 LPPMPR-----------DYSPELAELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd07829  233 KPTFPKwpkndlekvlpRLDPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
12-257 3.58e-44

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: 160.73  E-value: 3.58e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRNassrerRAAEQEAQLLSQLKHPNIVTYKESWEGGDGL------------- 78
Cdd:cd14047   14 IGSGGFGQVFKAKHRIDGKTYAIKRVKLNN------EKAEREVKALAKLDHPNIVRYNGCWDGFDYDpetsssnssrskt 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  79 --LYIVMGFCEGGDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVL 156
Cdd:cd14047   88 kcLFIQMEFCEKGTLESWIEKRNGEKLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGKVKIGDFGLVTSL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 157 ENHCDMASTLiGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKdmNSLVYRIIEGKLPPMPRDYSPELAE 236
Cdd:cd14047  168 KNDGKRTKSK-GTLSYMSPEQISSQDYGKEVDIYALGLILFELLHVCDSAFEK--SKFWTDLRNGILPDIFDKRYKIEKT 244
                        250       260
                 ....*....|....*....|.
gi 148839316 237 LIRTMLSKRPEERPSVRSILR 257
Cdd:cd14047  245 IIKKMLSKKPEDRPNASEILR 265
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
10-261 4.25e-44

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: 160.16  E-value: 4.25e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKesweggdGL------LYIVM 83
Cdd:cd06626    6 NKIGEGTFGKVYTAVNLDTGELMAMKEIRFQDNDPKTIKEIADEMKVLEGLDHPNLVRYY-------GVevhreeVYIFM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  84 GFCEGGDLYRKLKEqkGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMA 163
Cdd:cd06626   79 EYCQEGTLEELLRH--GRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAVKLKNNTTTM 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 164 S-----TLIGTPYYMSPELF-SNKPYNYK--SDVWALGCCVYEMATLKHAFNAKDMN-SLVYRIIEGKLPPMPRD--YSP 232
Cdd:cd06626  157 ApgevnSLVGTPAYMAPEVItGNKGEGHGraADIWSLGCVVLEMATGKRPWSELDNEwAIMYHVGMGHKPPIPDSlqLSP 236
                        250       260
                 ....*....|....*....|....*....
gi 148839316 233 ELAELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd06626  237 EGKDFLSRCLESDPKKRPTASELLDHPFI 265
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
12-260 6.34e-44

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: 159.77  E-value: 6.34e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGevTLVKHRRDG--KQYVIKKLNlrnASSRERRAaeQEAQLLSQLKHPNIVTYKESWEGGDGLlYIVMGFCEGG 89
Cdd:cd14010    8 IGRGKHS--VVYKGRRKGtiEFVAIKCVD---KSKRPEVL--NEVRLTHELKHPNVLKFYEWYETSNHL-WLVVEYCTGG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  90 DLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVL------------- 156
Cdd:cd14010   80 DLETLLRQDGN--LPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLARREgeilkelfgqfsd 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 157 ---ENHCDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPRDY--- 230
Cdd:cd14010  158 egnVNKVSKKQAKRGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFVAESFTELVEKILNEDPPPPPPKVssk 237
                        250       260       270
                 ....*....|....*....|....*....|.
gi 148839316 231 -SPELAELIRTMLSKRPEERPSVRSILRQPY 260
Cdd:cd14010  238 pSPDFKSLLKGLLEKDPAKRLSWDELVKHPF 268
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
6-273 1.57e-43

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 164.80  E-value: 1.57e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNaSSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLyIVMGF 85
Cdd:PTZ00267  69 YVLTTLVGRNPTTAAFVATRGSDPKEKVVAKFVMLN-DERQAAYARSELHCLAACDHFGIVKHFDDFKSDDKLL-LIMEY 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGGDLYRKLKEQKGQLLP--ENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHC--D 161
Cdd:PTZ00267 147 GSGGDLNKQIKQRLKEHLPfqEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQYSDSVslD 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 162 MASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPRDYSPELAELIRTM 241
Cdd:PTZ00267 227 VASSFCGTPYYLAPELWERKRYSKKADMWSLGVILYELLTLHRPFKGPSQREIMQQVLYGKYDPFPCPVSSGMKALLDPL 306
                        250       260       270
                 ....*....|....*....|....*....|..
gi 148839316 242 LSKRPEERPSVRSILRQPYIKRQISFFLEATK 273
Cdd:PTZ00267 307 LSKNPALRPTTQQLLHTEFLKYVANLFQDIVR 338
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
10-261 1.78e-43

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: 158.71  E-value: 1.78e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAA------EQEAQLLSQLKHPNIVTYKESWEGGDGLlYIVM 83
Cdd:cd14084   12 RTLGSGACGEVKLAYDKSTCKKVAIKIINKRKFTIGSRREInkprniETEIEILKKLSHPCIIKIEDFFDAEDDY-YIVL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  84 GFCEGGDLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTN---IIKVGDLGIARVLENHC 160
Cdd:cd14084   91 ELMEGGELFDRVVSNKR--LKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEeecLIKITDFGLSKILGETS 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 161 DMaSTLIGTPYYMSPELFSN---KPYNYKSDVWALGCCVYEMATLKHAFNA--KDMnSLVYRIIEGKL---PPMPRDYSP 232
Cdd:cd14084  169 LM-KTLCGTPTYLAPEVLRSfgtEGYTRAVDCWSLGVILFICLSGYPPFSEeyTQM-SLKEQILSGKYtfiPKAWKNVSE 246
                        250       260
                 ....*....|....*....|....*....
gi 148839316 233 ELAELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd14084  247 EAKDLVKKMLVVDPSRRPSIEEALEHPWL 275
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
12-261 2.87e-43

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: 157.85  E-value: 2.87e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHR--RDGKQYVIKKLNLRNASS-----RERRAAEQEaqLLSQLKHPNIVTYKESWEGGDGLLYIVMG 84
Cdd:cd13994    1 IGKGATSVVRIVTKKnpRSGVLYAVKEYRRRDDESkrkdyVKRLTSEYI--ISSKLHHPNIVKVLDLCQDLHGKWCLVME 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGGDLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCD--- 161
Cdd:cd13994   79 YCPGGDLFTLIEKADS--LSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAEVFGMPAEkes 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 162 -MASTLIGTPYYMSPELFSNKPYN-YKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPRDYSP------- 232
Cdd:cd13994  157 pMSAGLCGSEPYMAPEVFTSGSYDgRAVDVWSCGIVLFALFTGRFPWRSAKKSDSAYKAYEKSGDFTNGPYEPienllps 236
                        250       260
                 ....*....|....*....|....*....
gi 148839316 233 ELAELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd13994  237 ECRRLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
6-261 9.32e-43

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: 156.01  E-value: 9.32e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKL-NLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLyIVMG 84
Cdd:cd14073    3 YELLETLGKGTYGKVKLAIERATGREVAIKSIkKDKIEDEQDMVRIRREIEIMSSLNHPHIIRIYEVFENKDKIV-IVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGGDLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHcDMAS 164
Cdd:cd14073   82 YASGGELYDYISERRR--LPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSNLYSKD-KLLQ 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 TLIGTPYYMSPELFSNKPYN-YKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKL--PPMPRDYSpelaELIRTM 241
Cdd:cd14073  159 TFCGSPLYASPEIVNGTPYQgPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISSGDYrePTQPSDAS----GLIRWM 234
                        250       260
                 ....*....|....*....|
gi 148839316 242 LSKRPEERPSVRSILRQPYI 261
Cdd:cd14073  235 LTVNPKRRATIEDIANHWWV 254
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
6-261 1.29e-42

Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 155.47  E-value: 1.29e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNassRERRAAEQEAQLLSQLK----HPNIVTYKESWE-GGDGLLY 80
Cdd:cd05118    1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDF---RHPKAALREIKLLKHLNdvegHPNIVKLLDVFEhRGGNHLC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  81 IVMGFCeGGDLYRKLKEQkGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLT-RTNIIKVGDLGIARVLenH 159
Cdd:cd05118   78 LVFELM-GMNLYELIKDY-PRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINlELGQLKLADFGLARSF--T 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 160 CDMASTLIGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEgKLPPmprdysPELAELI 238
Cdd:cd05118  154 SPPYTPYVATRWYRAPEvLLGAKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIVR-LLGT------PEALDLL 226
                        250       260
                 ....*....|....*....|...
gi 148839316 239 RTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd05118  227 SKMLKYDPAKRITASQALAHPYF 249
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
14-255 5.63e-42

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: 154.68  E-value: 5.63e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  14 KGSYGEVTLVKHRRDGKQY---VIKKLNLRNASSRERRAAEQEAqlLSQLKHPNIVTYKESWEGGDGLlYIVMGFCEGGD 90
Cdd:cd05579    3 RGAYGRVYLAKKKSTGDLYaikVIKKRDMIRKNQVDSVLAERNI--LSQAQNPFVVKLYYSFQGKKNL-YLVMEYLPGGD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  91 LYRKLkEQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARV--LENHCDMAS---- 164
Cdd:cd05579   80 LYSLL-ENVGAL-DEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKVglVRRQIKLSIqkks 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 ---------TLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPmPRD--YSPE 233
Cdd:cd05579  158 ngapekedrRIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNILNGKIEW-PEDpeVSDE 236
                        250       260
                 ....*....|....*....|..
gi 148839316 234 LAELIRTMLSKRPEERPSVRSI 255
Cdd:cd05579  237 AKDLISKLLTPDPEKRLGAKGI 258
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
6-260 1.23e-41

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: 153.40  E-value: 1.23e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRER--RAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVM 83
Cdd:cd14098    2 YQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRKVAGNDKnlQLFQREINILKSLEHPGIVRLIDWYED-DQHIYLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  84 GFCEGGDLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTN--IIKVGDLGIARVLENHcD 161
Cdd:cd14098   81 EYVEGGDLMDFIMAWGA--IPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDpvIVKISDFGLAKVIHTG-T 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 162 MASTLIGTPYYMSPELFSNKP------YNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMP---RDYSP 232
Cdd:cd14098  158 FLVTFCGTMAYLAPEILMSKEqnlqggYSNLVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIRKGRYTQPPlvdFNISE 237
                        250       260
                 ....*....|....*....|....*...
gi 148839316 233 ELAELIRTMLSKRPEERPSVRSILRQPY 260
Cdd:cd14098  238 EAIDFILRLLDVDPEKRMTAAQALDHPW 265
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
10-268 1.45e-41

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: 153.52  E-value: 1.45e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASsRERRAA----EQEAqlLSQLKHPNIV----TYKESWEggdglLYI 81
Cdd:cd05581    7 KPLGEGSYSTVVLAKEKETGKEYAIKVLDKRHII-KEKKVKyvtiEKEV--LSRLAHPGIVklyyTFQDESK-----LYF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  82 VMGFCEGGDLYRKLKeQKGQLlpENQVVEWFV-QIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVL---- 156
Cdd:cd05581   79 VLEYAPNGDLLEYIR-KYGSL--DEKCTRFYTaEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGTAKVLgpds 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 157 ----------ENHCDM---ASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKl 223
Cdd:cd05581  156 spestkgdadSQIAYNqarAASFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIVKLE- 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 148839316 224 PPMPRDYSPELAELIRTMLSKRPEERPSVRSILRQPYIKRQiSFF 268
Cdd:cd05581  235 YEFPENFPPDAKDLIQKLLVLDPSKRLGVNENGGYDELKAH-PFF 278
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
11-261 1.75e-41

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: 152.98  E-value: 1.75e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  11 VVGKGSYGEVTLVKHRRdGKQYVIKKLNL----RNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGFC 86
Cdd:cd06631    8 VLGKGAYGTVYCGLTST-GQLIAVKQVELdtsdKEKAEKEYEKLQEEVDLLKTLKHVNIVGYLGTCLE-DNVVSIFMEFV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  87 EGGDLYRKLKeQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVL------ENHC 160
Cdd:cd06631   86 PGGSIASILA-RFGAL-EEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGCAKRLcinlssGSQS 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 161 DMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFnaKDMNSL--VYRIIEGK--LPPMPRDYSPELAE 236
Cdd:cd06631  164 QLLKSMRGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPW--ADMNPMaaIFAIGSGRkpVPRLPDKFSPEARD 241
                        250       260
                 ....*....|....*....|....*
gi 148839316 237 LIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd06631  242 FVHACLTRDQDERPSAEQLLKHPFI 266
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
12-249 2.43e-41

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: 152.38  E-value: 2.43e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASsrERRAAE---QEAQLLSQLKHPNIV----TYKESWEggdglLYIVMG 84
Cdd:cd05572    1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIV--QTRQQEhifSEKEILEECNSPFIVklyrTFKDKKY-----LYMLME 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGGDLYRKLKEqKGqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHcDMAS 164
Cdd:cd05572   74 YCLGGELWTILRD-RG-LFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKKLGSG-RKTW 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 TLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSL-VYRII---EGKLpPMPRDYSPELAELIRT 240
Cdd:cd05572  151 TFCGTPEYVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFGGDDEDPMkIYNIIlkgIDKI-EFPKYIDKNAKNLIKQ 229

                 ....*....
gi 148839316 241 MLSKRPEER 249
Cdd:cd05572  230 LLRRNPEER 238
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
13-260 2.56e-41

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: 152.06  E-value: 2.56e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  13 GKGSYGEVTLVKHRRDGKQYV----IKKLNLrNASSRERRAAEQEaqLLSQLKHPNIVTYKE-SWEggDGLLYIVMGFCE 87
Cdd:cd14121    4 GSGTYATVYKAYRKSGAREVVavkcVSKSSL-NKASTENLLTEIE--LLKKLKHPHIVELKDfQWD--EEHIYLIMEYCS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  88 GGDLYRKLKEQKgqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTR--TNIIKVGDLGIARVLENHcDMAST 165
Cdd:cd14121   79 GGDLSRFIRSRR--TLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSryNPVLKLADFGFAQHLKPN-DEAHS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRI-----IEgkLPPMPRdYSPELAELIRT 240
Cdd:cd14121  156 LRGSPLYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFASRSFEELEEKIrsskpIE--IPTRPE-LSADCRDLLLR 232
                        250       260
                 ....*....|....*....|
gi 148839316 241 MLSKRPEERPSVRSILRQPY 260
Cdd:cd14121  233 LLQRDPDRRISFEEFFAHPF 252
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
13-264 8.37e-41

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: 151.43  E-value: 8.37e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  13 GKGSYGEVTLVKHRRDGKQYVIKKLNLRnaSSRERRAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGFCEGGDLy 92
Cdd:cd06611   14 GDGAFGKVYKAQHKETGLFAAAKIIQIE--SEEELEDFMVEIDILSECKHPNIVGLYEAYFY-ENKLWILIEFCDGGAL- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  93 RKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTLIGTPYY 172
Cdd:cd06611   90 DSIMLELERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAKNKSTLQKRDTFIGTPYW 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 173 MSPEL-----FSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPM--PRDYSPELAELIRTMLSKR 245
Cdd:cd06611  170 MAPEVvacetFKDNPYDYKADIWSLGITLIELAQMEPPHHELNPMRVLLKILKSEPPTLdqPSKWSSSFNDFLKSCLVKD 249
                        250
                 ....*....|....*....
gi 148839316 246 PEERPSVRSILRQPYIKRQ 264
Cdd:cd06611  250 PDDRPTAAELLKHPFVSDQ 268
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
12-260 3.33e-40

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: 149.06  E-value: 3.33e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYV-IKKLNLRNASsRERRAAEQEAQLLSQLKHPNIVT---YKESWEGgdglLYIVMGFCE 87
Cdd:cd14120    1 IGHGAFAVVFKGRHRKKPDLPVaIKCITKKNLS-KSQNLLGKEIKILKELSHENVVAlldCQETSSS----VYLVMEYCN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  88 GGDLYRKLkEQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTR--------TNI-IKVGDLGIARVLEN 158
Cdd:cd14120   76 GGDLADYL-QAKGTL-SEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHnsgrkpspNDIrLKIADFGFARFLQD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 159 HcDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSL--VYRIIEGKLPPMPRDYSPELAE 236
Cdd:cd14120  154 G-MMAATLCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQAQTPQELkaFYEKNANLRPNIPSGTSPALKD 232
                        250       260
                 ....*....|....*....|....
gi 148839316 237 LIRTMLSKRPEERPSVRSILRQPY 260
Cdd:cd14120  233 LLLGLLKRNPKDRIDFEDFFSHPF 256
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
9-258 5.04e-40

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: 149.02  E-value: 5.04e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRerRAAEQEAQLLSQL-KHPNIVTY---KESWEGGDGLLYIVMG 84
Cdd:cd13985    5 TKQLGEGGFSYVYLAHDVNTGRRYALKRMYFNDEEQL--RVAIKEIEIMKRLcGHPNIVQYydsAILSSEGRKEVLLLME 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCeGGDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKH--ILHRDLKTQNVFLTRTNIIKVGDLG----IARVLEN 158
Cdd:cd13985   83 YC-PGSLVDILEKSPPSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFGsattEHYPLER 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 159 HCD--MASTLIG---TPYYMSPE---LFSNKPYNYKSDVWALGCCVYEMATLKHAFNAkdmnSLVYRIIEGK--LPPMPR 228
Cdd:cd13985  162 AEEvnIIEEEIQkntTPMYRAPEmidLYSKKPIGEKADIWALGCLLYKLCFFKLPFDE----SSKLAIVAGKysIPEQPR 237
                        250       260       270
                 ....*....|....*....|....*....|
gi 148839316 229 dYSPELAELIRTMLSKRPEERPSVRSILRQ 258
Cdd:cd13985  238 -YSPELHDLIRHMLTPDPAERPDIFQVINI 266
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
12-257 7.69e-40

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: 147.87  E-value: 7.69e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGFCEGGDL 91
Cdd:cd14075   10 LGSGNFSQVKLGIHQLTKEKVAIKILDKTKLDQKTQRLLSREISSMEKLHHPNIIRLYEVVET-LSKLHLVMEYASGGEL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  92 YRKLKEQkGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHcDMASTLIGTPY 171
Cdd:cd14075   89 YTKISTE-GKL-SESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFSTHAKRG-ETLNTFCGSPP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 172 YMSPELFSNKPY-NYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGK--LPPMprdYSPELAELIRTMLSKRPEE 248
Cdd:cd14075  166 YAAPELFKDEHYiGIYVDIWALGVLLYFMVTGVMPFRAETVAKLKKCILEGTytIPSY---VSEPCQELIRGILQPVPSD 242

                 ....*....
gi 148839316 249 RPSVRSILR 257
Cdd:cd14075  243 RYSIDEIKN 251
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
8-261 1.38e-39

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: 147.37  E-value: 1.38e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   8 YLR---VVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLYI-VM 83
Cdd:cd13983    2 YLKfneVLGRGSFKTVYRAFDTEEGIEVAWNEIKLRKLPKAERQRFKQEIEILKSLKHPNIIKFYDSWESKSKKEVIfIT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  84 GFCEGGDL--YRKlkeqKGQLLPENQVVEWFVQIAMALQYLH--EKHILHRDLKTQNVFLT-RTNIIKVGDLGIARVLEN 158
Cdd:cd13983   82 ELMTSGTLkqYLK----RFKRLKLKVIKSWCRQILEGLNYLHtrDPPIIHRDLKCDNIFINgNTGEVKIGDLGLATLLRQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 159 HcdMASTLIGTPYYMSPELFSNKpYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPP--MPRDYSPELAE 236
Cdd:cd13983  158 S--FAKSVIGTPEFMAPEMYEEH-YDEKVDIYAFGMCLLEMATGEYPYSECTNAAQIYKKVTSGIKPesLSKVKDPELKD 234
                        250       260
                 ....*....|....*....|....*
gi 148839316 237 LIRTMLSKrPEERPSVRSILRQPYI 261
Cdd:cd13983  235 FIEKCLKP-PDERPSARELLEHPFF 258
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
10-261 1.73e-39

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: 147.12  E-value: 1.73e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLNL---RNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGFC 86
Cdd:cd06625    6 KLLGQGAFGQVYLCYDADTGRELAVKQVEIdpiNTEASKEVKALECEIQLLKNLQHERIVQYYGCLQD-EKSLSIFMEYM 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  87 EGGDLYRKLKeQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMA--S 164
Cdd:cd06625   85 PGGSVKDEIK-AYGAL-TENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASKRLQTICSSTgmK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 TLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRII-EGKLPPMPRDYSPELAELIRTMLS 243
Cdd:cd06625  163 SVTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPWAEFEPMAAIFKIAtQPTNPQLPPHVSEDARDFLSLIFV 242
                        250
                 ....*....|....*...
gi 148839316 244 KRPEERPSVRSILRQPYI 261
Cdd:cd06625  243 RNKKQRPSAEELLSHSFV 260
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
6-260 2.12e-39

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: 146.70  E-value: 2.12e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKL-NLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLlYIVMG 84
Cdd:cd14188    3 YCRGKVLGKGGFAKCYEMTDLTTNKVYAAKIIpHSRVSKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENI-YILLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGGDLYRKLKEQKgqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMAS 164
Cdd:cd14188   82 YCSRRSMAHILKARK--VLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLEPLEHRRR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 TLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSlVYRIIEGKLPPMPRDYSPELAELIRTMLSK 244
Cdd:cd14188  160 TICGTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKE-TYRCIREARYSLPSSLLAPAKHLIASMLSK 238
                        250
                 ....*....|....*.
gi 148839316 245 RPEERPSVRSILRQPY 260
Cdd:cd14188  239 NPEDRPSLDEIIRHDF 254
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
12-262 2.37e-39

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: 146.82  E-value: 2.37e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRErrAAEQEAQLLSQLKHPNIVTYKESWEGGDGLlYIVMGFCEGGDL 91
Cdd:cd06648   15 IGEGSTGIVCIATDKSTGRQVAVKKMDLRKQQRRE--LLFNEVVIMRDYQHPNIVEMYSSYLVGDEL-WVVMEFLEGGAL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  92 YRKLKEQKgqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTLIGTPY 171
Cdd:cd06648   92 TDIVTHTR---MNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQVSKEVPRRKSLVGTPY 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 172 YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLvyRIIEGKLPPMPRDY---SPELAELIRTMLSKRPE 247
Cdd:cd06648  169 WMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPyFNEPPLQAM--KRIRDNEPPKLKNLhkvSPRLRSFLDRMLVRDPA 246
                        250
                 ....*....|....*
gi 148839316 248 ERPSVRSILRQPYIK 262
Cdd:cd06648  247 QRATAAELLNHPFLA 261
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
12-266 4.32e-39

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: 147.10  E-value: 4.32e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEaqLLSQLKHPNIVTYKESWEGgDGLLYIVMGFCEGG-- 89
Cdd:cd06644   20 LGDGAFGKVYKAKNKETGALAAAKVIETKSEEELEDYMVEIE--ILATCNHPYIVKLLGAFYW-DGKLWIMIEFCPGGav 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  90 -----DLYRKLKEqkgqllPENQVVewFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMAS 164
Cdd:cd06644   97 daimlELDRGLTE------PQIQVI--CRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSAKNVKTLQRRD 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 TLIGTPYYMSPEL-----FSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPM--PRDYSPELAEL 237
Cdd:cd06644  169 SFIGTPYWMAPEVvmcetMKDTPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSEPPTLsqPSKWSMEFRDF 248
                        250       260
                 ....*....|....*....|....*....
gi 148839316 238 IRTMLSKRPEERPSVRSILRQPYIKRQIS 266
Cdd:cd06644  249 LKTALDKHPETRPSAAQLLEHPFVSSVTS 277
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
9-245 7.77e-39

Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. The PKA subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 146.01  E-value: 7.77e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRN-ASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLlYIVMGFCE 87
Cdd:cd14209    6 IKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKvVKLKQVEHTLNEKRILQAINFPFLVKLEYSFKDNSNL-YMVMEYVP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  88 GGDLYRKLkeQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHcdmASTLI 167
Cdd:cd14209   85 GGEMFSHL--RRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRVKGR---TWTLC 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 168 GTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLpPMPRDYSPELAELIRTML----S 243
Cdd:cd14209  160 GTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKV-RFPSHFSSDLKDLLRNLLqvdlT 238

                 ..
gi 148839316 244 KR 245
Cdd:cd14209  239 KR 240
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
6-260 8.62e-39

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: 145.75  E-value: 8.62e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRE----RraaeqEAQLLSQLK-HPNIVTYKESW-EGGDglL 79
Cdd:cd07830    1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKMKKKFYSWEEcmnlR-----EVKSLRKLNeHPNIVKLKEVFrENDE--L 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  80 YIVMGFCEGgDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENh 159
Cdd:cd07830   74 YFVFEYMEG-NLYQLMKDRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLAREIRS- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 160 CDMASTLIGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAF---NAKDMnslVYRII------------EG-- 221
Cdd:cd07830  152 RPPYTDYVSTRWYRAPEiLLRSTSYSSPVDIWALGCIMAELYTLRPLFpgsSEIDQ---LYKICsvlgtptkqdwpEGyk 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 148839316 222 -------KLPPMPR--------DYSPELAELIRTMLSKRPEERPSVRSILRQPY 260
Cdd:cd07830  229 lasklgfRFPQFAPtslhqlipNASPEAIDLIKDMLRWDPKKRPTASQALQHPY 282
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
6-261 1.53e-38

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: 145.14  E-value: 1.53e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYV---IKKLNLRNASSrerraAEQEAQLLSQLKHPNIVTYKESWEGGDGLlYIV 82
Cdd:cd14166    5 FIFMEVLGSGAFSEVYLVKQRSTGKLYAlkcIKKSPLSRDSS-----LENEIAVLKRIKHENIVTLEDIYESTTHY-YLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  83 MGFCEGGDLYRKLKEQKgqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNV-FLT--RTNIIKVGDLGIARVLENh 159
Cdd:cd14166   79 MQLVSGGELFDRILERG--VYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLlYLTpdENSKIMITDFGLSKMEQN- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 160 cDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKL---PPMPRDYSPELAE 236
Cdd:cd14166  156 -GIMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGYYefeSPFWDDISESAKD 234
                        250       260
                 ....*....|....*....|....*
gi 148839316 237 LIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd14166  235 FIRHLLEKNPSKRYTCEKALSHPWI 259
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
2-261 1.64e-38

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: 145.15  E-value: 1.64e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   2 PLAAYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLrnaSSRERRAAEQEAQLLSQLKH-PNIVTY-----KESWEGG 75
Cdd:cd06636   14 PAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDV---TEDEEEEIKLEINMLKKYSHhRNIATYygafiKKSPPGH 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  76 DGLLYIVMGFCEGGDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARV 155
Cdd:cd06636   91 DDQLWLVMEFCGAGSVTDLVKNTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQ 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 156 LENHCDMASTLIGTPYYMSPELFS-----NKPYNYKSDVWALGCCVYEMAtlKHAFNAKDMNSLVYRIIEGKLPP---MP 227
Cdd:cd06636  171 LDRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMA--EGAPPLCDMHPMRALFLIPRNPPpklKS 248
                        250       260       270
                 ....*....|....*....|....*....|....
gi 148839316 228 RDYSPELAELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd06636  249 KKWSKKFIDFIEGCLVKNYLSRPSTEQLLKHPFI 282
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
10-287 1.96e-38

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: 145.82  E-value: 1.96e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLN----LRN----ASSRERRAaeqeaqLLSQLKHPNIVTYKESWEGGDGLlYI 81
Cdd:cd05570    1 KVLGKGSFGKVMLAERKKTDELYAIKVLKkeviIEDddveCTMTEKRV------LALANRHPFLTGLHACFQTEDRL-YF 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  82 VMGFCEGGDLYRKLkeQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARvlEN--H 159
Cdd:cd05570   74 VMEYVNGGDLMFHI--QRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCK--EGiwG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 160 CDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLvYRIIEGKLPPMPRDYSPELAELIR 239
Cdd:cd05570  150 GNTTSTFCGTPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDEL-FEAILNDEVLYPRWLSREAVSILK 228
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148839316 240 TMLSKRPEERPSVRsilrqPYIKRQI---SFF-------LEATKIK-------TSKNNIKNGDSQ 287
Cdd:cd05570  229 GLLTKDPARRLGCG-----PKGEADIkahPFFrnidwdkLEKKEVEppfkpkvKSPRDTSNFDPE 288
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
6-260 5.85e-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: 142.54  E-value: 5.85e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNlRNASSRERrAAEQ---EAQLLSQLKHPNIVTYKESWeGGDGLLYIV 82
Cdd:cd14663    2 YELGRTLGEGTFAKVKFARNTKTGESVAIKIID-KEQVAREG-MVEQikrEIAIMKLLRHPNIVELHEVM-ATKTKIFFV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  83 MGFCEGGDLYRKLKeqKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIArVLENHCD- 161
Cdd:cd14663   79 MELVTGGELFSKIA--KNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLS-ALSEQFRq 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 162 --MASTLIGTPYYMSPELFSNKPYN-YKSDVWALGCCVYEMATLKHAFNAKDMNSLvYRIIEGKLPPMPRDYSPELAELI 238
Cdd:cd14663  156 dgLLHTTCGTPNYVAPEVLARRGYDgAKADIWSCGVILFVLLAGYLPFDDENLMAL-YRKIMKGEFEYPRWFSPGAKSLI 234
                        250       260
                 ....*....|....*....|..
gi 148839316 239 RTMLSKRPEERPSVRSILRQPY 260
Cdd:cd14663  235 KRILDPNPSTRITVEQIMASPW 256
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
11-261 8.24e-38

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


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 142.46  E-value: 8.24e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  11 VVGKGSYGEVTLVKHR-RDGKQYVIKKLNLRNASsRERRAAEQEAQLLSQLKHPNIVTYKESWEGGdGLLYIVMGFCEGG 89
Cdd:cd14202    9 LIGHGAFAVVFKGRHKeKHDLEVAVKCINKKNLA-KSQTLLGKEIKILKELKHENIVALYDFQEIA-NSVYLVMEYCNGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  90 DLYRKLKEQKgqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRT--------NI-IKVGDLGIARVLENHC 160
Cdd:cd14202   87 DLADYLHTMR--TLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSggrksnpnNIrIKIADFGFARYLQNNM 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 161 dMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSL--VYRIIEGKLPPMPRDYSPELAELI 238
Cdd:cd14202  165 -MAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQDLrlFYEKNKSLSPNIPRETSSHLRQLL 243
                        250       260
                 ....*....|....*....|...
gi 148839316 239 RTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd14202  244 LGLLQRNQKDRMDFDEFFHHPFL 266
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
3-262 8.33e-38

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 152.97  E-value: 8.33e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316    3 LAAYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESW-EGGDGLLYI 81
Cdd:PTZ00266   12 LNEYEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISYRGLKEREKSQLVIEVNVMRELKHKNIVRYIDRFlNKANQKLYI 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   82 VMGFCEGGDLYRKLKEQKGQL--LPENQVVEWFVQIAMALQYLHE-------KHILHRDLKTQNVFLT-----------R 141
Cdd:PTZ00266   92 LMEFCDAGDLSRNIQKCYKMFgkIEEHAIVDITRQLLHALAYCHNlkdgpngERVLHRDLKPQNIFLStgirhigkitaQ 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  142 TN------IIKVGDLGIARVLENHcDMASTLIGTPYYMSPELF--SNKPYNYKSDVWALGCCVYEMATLKHAFN-AKDMN 212
Cdd:PTZ00266  172 ANnlngrpIAKIGDFGLSKNIGIE-SMAHSCVGTPYYWSPELLlhETKSYDDKSDMWALGCIIYELCSGKTPFHkANNFS 250
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 148839316  213 SLVYRIIEGklPPMP-RDYSPELAELIRTMLSKRPEERPSVRSILRQPYIK 262
Cdd:PTZ00266  251 QLISELKRG--PDLPiKGKSKELNILIKNLLNLSAKERPSALQCLGYQIIK 299
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
13-260 1.01e-37

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: 141.63  E-value: 1.01e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  13 GKGSYGEV-------TLVkhRRDGKqyVIKKLNLR---NASSRERRaaeqEAQLLSQLKHPNIVTYKESWEGGD-GLLYI 81
Cdd:cd14119    2 GEGSYGKVkevldteTLC--RRAVK--ILKKRKLRripNGEANVKR----EIQILRRLNHRNVIKLVDVLYNEEkQKLYM 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  82 VMGFCEGGdLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLE--NH 159
Cdd:cd14119   74 VMEYCVGG-LQEMLDSAPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAEALDlfAE 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 160 CDMASTLIGTPYYMSPELFSNKPY--NYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLpPMPRDYSPELAEL 237
Cdd:cd14119  153 DDTCTTSQGSPAFQPPEIANGQDSfsGFKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKGEY-TIPDDVDPDLQDL 231
                        250       260
                 ....*....|....*....|...
gi 148839316 238 IRTMLSKRPEERPSVRSILRQPY 260
Cdd:cd14119  232 LRGMLEKDPEKRFTIEQIRQHPW 254
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
8-265 2.34e-37

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: 141.79  E-value: 2.34e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   8 YLRVVGKGSYGEVTLVKHRrDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESW-EGGDGLLYIVMGFC 86
Cdd:cd06621    5 ELSSLGEGAGGSVTKCRLR-NTKTIFALKTITTDPNPDVQKQILRELEINKSCASPYIVKYYGAFlDEQDSSIGIAMEYC 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  87 EGGDL---YRKLKEQKGQL--LPENQVVEwfvQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENhcD 161
Cdd:cd06621   84 EGGSLdsiYKKVKKKGGRIgeKVLGKIAE---SVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVSGELVN--S 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 162 MASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNS-----LVYRIIEGKLPPMPRD------Y 230
Cdd:cd06621  159 LAGTFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFPPEGEPPlgpieLLSYIVNMPNPELKDEpengikW 238
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 148839316 231 SPELAELIRTMLSKRPEERPSVRSILRQPYIKRQI 265
Cdd:cd06621  239 SESFKDFIEKCLEKDGTRRPGPWQMLAHPWIKAQE 273
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
9-253 3.06e-37

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: 142.79  E-value: 3.06e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLN---LRNASSRERRAAEQEAqLLSQLKHPNIVTYKESWEGGDGLlYIVMGF 85
Cdd:cd05604    1 LKVIGKGSFGKVLLAKRKRDGKYYAVKVLQkkvILNRKEQKHIMAERNV-LLKNVKHPFLVGLHYSFQTTDKL-YFVLDF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGGDLYRKLkeQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMAST 165
Cdd:cd05604   79 VNGGELFFHL--QRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKEGISNSDTTTT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPrDYSPELAELIRTMLSKR 245
Cdd:cd05604  157 FCGTPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENILHKPLVLRP-GISLTAWSILEELLEKD 235

                 ....*...
gi 148839316 246 PEERPSVR 253
Cdd:cd05604  236 RQLRLGAK 243
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
11-262 5.13e-37

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: 140.14  E-value: 5.13e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  11 VVGKGSYGEVTLVKHRRDGK-QYVIKKLNLRNASsRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLlYIVMGFCEGG 89
Cdd:cd14201   13 LVGHGAFAVVFKGRHRKKTDwEVAIKSINKKNLS-KSQILLGKEIKILKELQHENIVALYDVQEMPNSV-FLVMEYCNGG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  90 DLYRKLkEQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLT-----RTNI----IKVGDLGIARVLENHC 160
Cdd:cd14201   91 DLADYL-QAKGTL-SEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSyasrkKSSVsgirIKIADFGFARYLQSNM 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 161 dMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSL--VYRIIEGKLPPMPRDYSPELAELI 238
Cdd:cd14201  169 -MAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQDLrmFYEKNKNLQPSIPRETSPYLADLL 247
                        250       260
                 ....*....|....*....|....
gi 148839316 239 RTMLSKRPEERPSVRSILRQPYIK 262
Cdd:cd14201  248 LGLLQRNQKDRMDFEAFFSHPFLE 271
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
10-258 6.52e-37

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: 140.34  E-value: 6.52e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLnLRNASSReRRAAEQEAQLLSQLK-HPNIVTY--------KESWEGGDGLLy 80
Cdd:cd14036    6 RVIAEGGFAFVYEAQDVGTGKEYALKRL-LSNEEEK-NKAIIQEINFMKKLSgHPNIVQFcsaasigkEESDQGQAEYL- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  81 IVMGFCEGG--DLYRKLkEQKGQLLPEnQVVEWFVQIAMALQYLHEKH--ILHRDLKTQNVFLTRTNIIKVGDLGIARVL 156
Cdd:cd14036   83 LLTELCKGQlvDFVKKV-EAPGPFSPD-TVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQIKLCDFGSATTE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 157 ENHCD---------MASTLIG---TPYYMSPE---LFSNKPYNYKSDVWALGCCVYEMATLKHAFNakdmNSLVYRIIEG 221
Cdd:cd14036  161 AHYPDyswsaqkrsLVEDEITrntTPMYRTPEmidLYSNYPIGEKQDIWALGCILYLLCFRKHPFE----DGAKLRIINA 236
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 148839316 222 K--LPPMPRDYSpELAELIRTMLSKRPEERPSVRSILRQ 258
Cdd:cd14036  237 KytIPPNDTQYT-VFHDLIRSTLKVNPEERLSITEIVEQ 274
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
8-242 2.98e-36

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: 138.72  E-value: 2.98e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   8 YLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNA-SSRERRAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGFC 86
Cdd:cd05612    5 RIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEViRLKQEQHVHNEKRVLKEVSHPFIIRLFWTEHD-QRFLYMLMEYV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  87 EGGDLYRKLKeQKGQLlpENQVVEWFV-QIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLEnhcDMAST 165
Cdd:cd05612   84 PGGELFSYLR-NSGRF--SNSTGLFYAsEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKKLR---DRTWT 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148839316 166 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLpPMPRDYSPELAELIRTML 242
Cdd:cd05612  158 LCGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGKL-EFPRHLDLYAKDLIKKLL 233
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
6-261 4.50e-36

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


Pssm-ID: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 136.88  E-value: 4.50e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGF 85
Cdd:cd14072    2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPSSLQKLFREVRIMKILNHPNIVKLFEVIET-EKTLYLVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGGDLYRKLKEQkGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMaST 165
Cdd:cd14072   81 ASGGEVFDYLVAH-GRM-KEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFTPGNKL-DT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 LIGTPYYMSPELFSNKPYN-YKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLpPMPRDYSPELAELIRTMLSK 244
Cdd:cd14072  158 FCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKY-RIPFYMSTDCENLLKKFLVL 236
                        250
                 ....*....|....*..
gi 148839316 245 RPEERPSVRSILRQPYI 261
Cdd:cd14072  237 NPSKRGTLEQIMKDRWM 253
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
10-260 5.27e-36

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: 137.04  E-value: 5.27e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRER-RAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGFCEG 88
Cdd:cd14162    6 KTLGHGSYAVVKKAYSTKHKCKVAIKIVSKKKAPEDYLqKFLPREIEVIKGLKHPNLICFYEAIET-TSRVYIIMELAEN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  89 GDLYRKLKEQKgqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIAR----VLENHCDMAS 164
Cdd:cd14162   85 GDLLDYIRKNG--ALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFARgvmkTKDGKPKLSE 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 TLIGTPYYMSPELFSNKPYN-YKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPRDYSPELAELIRTMLS 243
Cdd:cd14162  163 TYCGSYAYASPEILRGIPYDpFLSDIWSMGVVLYTMVYGRLPFDDSNLKVLLKQVQRRVVFPKNPTVSEECKDLILRMLS 242
                        250
                 ....*....|....*..
gi 148839316 244 KRPeERPSVRSILRQPY 260
Cdd:cd14162  243 PVK-KRITIEEIKRDPW 258
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
6-314 5.41e-36

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: 139.73  E-value: 5.41e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLN----LRNASSRERRAaeqEAQLLSQLKHPNIVTYKESWEGGDGLlYI 81
Cdd:cd05573    3 FEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRksdmLKREQIAHVRA---ERDILADADSPWIVRLHYAFQDEDHL-YL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  82 VMGFCEGGDLYRKLKEQkgQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIA-------- 153
Cdd:cd05573   79 VMEYMPGGDLMNLLIKY--DVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCtkmnksgd 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 154 -------RVLENHCD--------------MASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMN 212
Cdd:cd05573  157 resylndSVNTLFQDnvlarrrphkqrrvRAYSAVGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPPFYSDSLV 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 213 SLVYRIIEGK----LPPMPrDYSPELAELIRTMLsKRPEER-PSVRSILRQPYIKrqisffleatkiKTSKNNIKNgdsQ 287
Cdd:cd05573  237 ETYSKIMNWKeslvFPDDP-DVSPEAIDLIRRLL-CDPEDRlGSAEEIKAHPFFK------------GIDWENLRE---S 299
                        330       340
                 ....*....|....*....|....*...
gi 148839316 288 SKPFATVVSGEAE-SNHEVIHPQPLSSE 314
Cdd:cd05573  300 PPPFVPELSSPTDtSNFDDFEDDLLLSE 327
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
12-257 5.95e-36

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: 136.80  E-value: 5.95e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRrdGKQYVIKKLNlrnaSSRERRAAEQEAQLLSQLKHPNIV------TYKESWeggdgllYIVMGF 85
Cdd:cd14058    1 VGRGSFGVVCKARWR--NQIVAVKIIE----SESEKKAFEVEVRQLSRVDHPNIIklygacSNQKPV-------CLVMEY 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGGDLYRKLKEQKGQllPE---NQVVEWFVQIAMALQYLH---EKHILHRDLKTQNVFLTRT-NIIKVGDLGIArvlen 158
Cdd:cd14058   68 AEGGSLYNVLHGKEPK--PIytaAHAMSWALQCAKGVAYLHsmkPKALIHRDLKPPNLLLTNGgTVLKICDFGTA----- 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 159 hCDMASTLI---GTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFnaKDMNSLVYRII----EGKLPPMPRDYS 231
Cdd:cd14058  141 -CDISTHMTnnkGSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPF--DHIGGPAFRIMwavhNGERPPLIKNCP 217
                        250       260
                 ....*....|....*....|....*.
gi 148839316 232 PELAELIRTMLSKRPEERPSVRSILR 257
Cdd:cd14058  218 KPIESLMTRCWSKDPEKRPSMKEIVK 243
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
10-309 7.92e-36

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: 138.22  E-value: 7.92e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLNL-----RNASSR---ERRAaeqeaqLLSQLKHPNIVTYKESWEGGDGLlYI 81
Cdd:cd05575    1 KVIGKGSFGKVLLARHKAEGKLYAVKVLQKkailkRNEVKHimaERNV------LLKNVKHPFLVGLHYSFQTKDKL-YF 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  82 VMGFCEGGDLYRKLkeQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCD 161
Cdd:cd05575   74 VLDYVNGGELFFHL--QRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKEGIEPSD 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 162 MASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLpPMPRDYSPELAELIRTM 241
Cdd:cd05575  152 TTSTFCGTPEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILHKPL-RLRTNVSPSARDLLEGL 230
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148839316 242 LSKRPEERPSVRSILRQpyIKRQiSFF-------LEATKIKTsknnikngdsqskPFATVVSGEAESNHevIHPQ 309
Cdd:cd05575  231 LQKDRTKRLGSGNDFLE--IKNH-SFFrpinwddLEAKKIPP-------------PFNPNVSGPLDLRN--IDPE 287
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
10-261 1.17e-35

Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase (also called MAK-V); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HUNK/MAK-V was identified from a mammary tumor in an MMTV-neu transgenic mouse. It is required for the metastasis of c-myc-induced mammary tumors, but is not necessary for c-myc-induced primary tumor formation or normal development. It is required for HER2/neu-induced tumor formation and maintenance of the cells' tumorigenic phenotype. It is over-expressed in aggressive subsets of ovary, colon, and breast carcinomas. HUNK interacts with synaptopodin, and may also play a role in synaptic plasticity. The HUNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 136.10  E-value: 1.17e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNA--SSRERRAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGFCE 87
Cdd:cd14070    8 RKLGEGSFAKVREGLHAVTGEKVAIKVIDKKKAkkDSYVTKNLRREGRIQQMIRHPNITQLLDILET-ENSYYLVMELCP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  88 GGDLYRKLKEQKgqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARV--LENHCDMAST 165
Cdd:cd14070   87 GGNLMHRIYDKK--RLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNCagILGYSDPFST 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMN--SLVYRIIEGKLPPMPRDYSPELAELIRTMLS 243
Cdd:cd14070  165 QCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPFTVEPFSlrALHQKMVDKEMNPLPTDLSPGAISFLRSLLE 244
                        250
                 ....*....|....*...
gi 148839316 244 KRPEERPSVRSILRQPYI 261
Cdd:cd14070  245 PDPLKRPNIKQALANRWL 262
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
10-260 1.22e-35

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: 135.92  E-value: 1.22e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLlYIVMGFCEGG 89
Cdd:cd14069    7 QTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPGDCPENIKKEVCIQKMLSHKNVVRFYGHRREGEFQ-YLFLEYASGG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  90 DLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIA---------RVLENHC 160
Cdd:cd14069   86 ELFDKIEPDVG--MPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLAtvfrykgkeRLLNKMC 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 161 dmastliGTPYYMSPELFSNKPYN-YKSDVWALGCCVYEMATLKHAFNAKDMNSLVY-RIIEGKLP---PMPRDYSPELA 235
Cdd:cd14069  164 -------GTLPYVAPELLAKKKYRaEPVDVWSCGIVLFAMLAGELPWDQPSDSCQEYsDWKENKKTyltPWKKIDTAALS 236
                        250       260
                 ....*....|....*....|....*
gi 148839316 236 eLIRTMLSKRPEERPSVRSILRQPY 260
Cdd:cd14069  237 -LLRKILTENPNKRITIEDIKKHPW 260
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
6-261 1.37e-35

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: 135.76  E-value: 1.37e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSR-ERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLYIVMG 84
Cdd:cd14164    2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIKIVDRRRASPDfVQKFLPRELSILRRVNHPNIVQMFECIEVANGRLYIVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGgDLYRKLKEQKgqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTN-IIKVGDLGIARVLENHCDMA 163
Cdd:cd14164   82 AAAT-DLLQKIQEVH--HIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDrKIKIADFGFARFVEDYPELS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 164 STLIGTPYYMSPELFSNKPYNYKS-DVWALGCCVYEMATLKHAFNaKDMNSLVYRIIEGKLPPMPRDYSPELAELIRTML 242
Cdd:cd14164  159 TTFCGSRAYTPPEVILGTPYDPKKyDVWSLGVVLYVMVTGTMPFD-ETNVRRLRLQQRGVLYPSGVALEEPCRALIRTLL 237
                        250
                 ....*....|....*....
gi 148839316 243 SKRPEERPSVRSILRQPYI 261
Cdd:cd14164  238 QFNPSTRPSIQQVAGNSWL 256
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
9-263 1.48e-35

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: 135.66  E-value: 1.48e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRER-RAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGFCE 87
Cdd:cd06607    6 LREIGHGSFGAVYYARNKRTSEVVAIKKMSYSGKQSTEKwQDIIKEVKFLRQLRHPNTIEYKGCYLR-EHTAWLVMEYCL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  88 G--GDLYRKLKeqkgQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVlenhCDMAST 165
Cdd:cd06607   85 GsaSDIVEVHK----KPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFGSASL----VCPANS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 LIGTPYYMSPEL---FSNKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLvYRIIEGKLPPM-PRDYSPELAELIRT 240
Cdd:cd06607  157 FVGTPYWMAPEVilaMDEGQYDGKVDVWSLGITCIELAERKPPlFNMNAMSAL-YHIAQNDSPTLsSGEWSDDFRNFVDS 235
                        250       260
                 ....*....|....*....|...
gi 148839316 241 MLSKRPEERPSVRSILRQPYIKR 263
Cdd:cd06607  236 CLQKIPQDRPSAEDLLKHPFVTR 258
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
10-260 1.54e-35

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: 135.53  E-value: 1.54e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERrAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGFCEGG 89
Cdd:cd14095    6 RVIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGKEH-MIENEVAILRRVKHPNIVQLIEEYDT-DTELYLVMELVKGG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  90 DLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTR----TNIIKVGDLGIARVLENhcdMAST 165
Cdd:cd14095   84 DLFDAITSSTK--FTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEhedgSKSLKLADFGLATEVKE---PLFT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNS--LVYRIIEGK---LPPMPRDYSPELAELIRT 240
Cdd:cd14095  159 VCGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRSPDRDQeeLFDLILAGEfefLSPYWDNISDSAKDLISR 238
                        250       260
                 ....*....|....*....|
gi 148839316 241 MLSKRPEERPSVRSILRQPY 260
Cdd:cd14095  239 MLVVDPEKRYSAGQVLDHPW 258
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
6-255 1.77e-35

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. NUAK2 is implicated in regulating actin stress fiber assembly through its association with myosin phosphatase Rho-interacting protein (MRIP), which leads to an increase in myosin regulatory light chain (MLC) phosphorylation. It is also associated with tumor growth, migration, and oncogenicity of melanoma cells. The NUAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 135.47  E-value: 1.77e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRdGKQYVIKKLNlrnassRERRAAEQ-------EAQLLSQLKHPNIVTYKESWEGGDGL 78
Cdd:cd14161    5 YEFLETLGKGTYGRVKKARDSS-GRLVAIKSIR------KDRIKDEQdllhirrEIEIMSSLNHPHIISVYEVFENSSKI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  79 LyIVMGFCEGGDLYRKLKEQkgQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLeN 158
Cdd:cd14161   78 V-IVMEYASRGDLYDYISER--QRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSNLY-N 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 159 HCDMASTLIGTPYYMSPELFSNKPY-NYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEG--KLPPMPRDyspeLA 235
Cdd:cd14161  154 QDKFLQTYCGSPLYASPEIVNGRPYiGPEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISSGayREPTKPSD----AC 229
                        250       260
                 ....*....|....*....|
gi 148839316 236 ELIRTMLSKRPEERPSVRSI 255
Cdd:cd14161  230 GLIRWLLMVNPERRATLEDV 249
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
9-266 2.66e-35

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: 135.64  E-value: 2.66e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKqYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLYIVMGFCEG 88
Cdd:cd06620   10 LKDLGAGNGGSVSKVLHIPTGT-IMAKKVIHIDAKSSVRKQILRELQILHECHSPYIVSFYGAFLNENNNIIICMEYMDC 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  89 GDLYRKLKEqKGQLlPENQVVEWFVQIAMALQYLHEKH-ILHRDLKTQNVFLTRTNIIKVGDLGIARVLENhcDMASTLI 167
Cdd:cd06620   89 GSLDKILKK-KGPF-PEEVLGKIAVAVLEGLTYLYNVHrIIHRDIKPSNILVNSKGQIKLCDFGVSGELIN--SIADTFV 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 168 GTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNS-----------LVYRIIEGKLPPMPRD--YSPEL 234
Cdd:cd06620  165 GTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFAGSNDDDdgyngpmgildLLQRIVNEPPPRLPKDriFPKDL 244
                        250       260       270
                 ....*....|....*....|....*....|..
gi 148839316 235 AELIRTMLSKRPEERPSVRSILRQPYIKRQIS 266
Cdd:cd06620  245 RDFVDRCLLKDPRERPSPQLLLDHDPFIQAVR 276
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
13-260 2.74e-35

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: 134.32  E-value: 2.74e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  13 GKGSYGEVTLVKHRRDGKQYVIKKLNLRnasSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLyIVMGFCEGGDLY 92
Cdd:cd14006    2 GRGRFGVVKRCIEKATGREFAAKFIPKR---DKKKEAVLREISILNQLQHPRIIQLHEAYESPTELV-LILELCSGGELL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  93 RKLKEQkgQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLT--RTNIIKVGDLGIARVLeNHCDMASTLIGTP 170
Cdd:cd14006   78 DRLAER--GSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLAdrPSPQIKIIDFGLARKL-NPGEELKEIFGTP 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 171 YYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKL---PPMPRDYSPELAELIRTMLSKRPE 247
Cdd:cd14006  155 EFVAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVdfsEEYFSSVSQEAKDFIRKLLVKEPR 234
                        250
                 ....*....|...
gi 148839316 248 ERPSVRSILRQPY 260
Cdd:cd14006  235 KRPTAQEALQHPW 247
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
5-260 2.97e-35

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: 134.67  E-value: 2.97e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   5 AYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKL-NLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLlYIVM 83
Cdd:cd14189    2 SYCKGRLLGKGGFARCYEMTDLATNKTYAVKVIpHSRVAKPHQREKIVNEIELHRDLHHKHVVKFSHHFEDAENI-YIFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  84 GFCEGGDLYRKLKEQKGQLLPEnqvVEWFV-QIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDM 162
Cdd:cd14189   81 ELCSRKSLAHIWKARHTLLEPE---VRYYLkQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAARLEPPEQR 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 163 ASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSlVYRIIEGKLPPMPRDYSPELAELIRTML 242
Cdd:cd14189  158 KKTICGTPNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETLDLKE-TYRCIKQVKYTLPASLSLPARHLLAGIL 236
                        250
                 ....*....|....*...
gi 148839316 243 SKRPEERPSVRSILRQPY 260
Cdd:cd14189  237 KRNPGDRLTLDQILEHEF 254
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
10-249 7.02e-35

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: 135.61  E-value: 7.02e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHR--RD-GKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGFC 86
Cdd:cd05582    1 KVLGQGSFGKVFLVRKItgPDaGTLYAMKVLKKATLKVRDRVRTKMERDILADVNHPFIVKLHYAFQT-EGKLYLILDFL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  87 EGGDLYRKLkeQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTL 166
Cdd:cd05582   80 RGGDLFTRL--SKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKESIDHEKKAYSF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 167 IGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLpPMPRDYSPELAELIRTMLSKRP 246
Cdd:cd05582  158 CGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAKL-GMPQFLSPEAQSLLRALFKRNP 236

                 ...
gi 148839316 247 EER 249
Cdd:cd05582  237 ANR 239
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
9-261 1.01e-34

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: 133.06  E-value: 1.01e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLN---LRNASSRERraAEQEAQLLSQLKHPNIVTYKESWEGGDgLLYIVMGF 85
Cdd:cd14186    6 LNLLGKGSFACVYRARSLHTGLEVAIKMIDkkaMQKAGMVQR--VRNEVEIHCQLKHPSILELYNYFEDSN-YVYLVLEM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGGDLYRKLKEQKgQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMAST 165
Cdd:cd14186   83 CHNGEMSRYLKNRK-KPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKMPHEKHFT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLpPMPRDYSPELAELIRTMLSKR 245
Cdd:cd14186  162 MCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLADY-EMPAFLSREAQDLIHQLLRKN 240
                        250
                 ....*....|....*.
gi 148839316 246 PEERPSVRSILRQPYI 261
Cdd:cd14186  241 PADRLSLSSVLDHPFM 256
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
12-261 1.08e-34

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: 133.66  E-value: 1.08e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNL-----RNASSRER---RAAEQEAQLLSQLKHPNIVTYKeSWEGGDGLLYIVM 83
Cdd:cd06629    9 IGKGTYGRVYLAMNATTGEMLAVKQVELpktssDRADSRQKtvvDALKSEIDTLKDLDHPNIVQYL-GFEETEDYFSIFL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  84 GFCEGG---DLYRKLkeqkGQLlpENQVVEWFV-QIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLEN- 158
Cdd:cd06629   88 EYVPGGsigSCLRKY----GKF--EEDLVRFFTrQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISKKSDDi 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 159 -HCDMASTLIGTPYYMSPELFSN--KPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIieGKL---PPMPRD--Y 230
Cdd:cd06629  162 yGNNGATSMQGSVFWMAPEVIHSqgQGYSAKVDIWSLGCVVLEMLAGRRPWSDDEAIAAMFKL--GNKrsaPPVPEDvnL 239
                        250       260       270
                 ....*....|....*....|....*....|.
gi 148839316 231 SPELAELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd06629  240 SPEALDFLNACFAIDPRDRPTAAELLSHPFL 270
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
5-261 1.09e-34

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: 133.25  E-value: 1.09e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   5 AYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNL--RNASSRERRaaeQEAQLLSQLKHPNIVTYKESWEGGDgLLYIV 82
Cdd:cd06610    2 DYELIEVIGSGATAVVYAAYCLPKKEKVAIKRIDLekCQTSMDELR---KEIQAMSQCNHPNVVSYYTSFVVGD-ELWLV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  83 MGFCEGGDLYRKLKEQ-KGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCD 161
Cdd:cd06610   78 MPLLSGGSLLDIMKSSyPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVSASLATGGD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 162 MAS----TLIGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAF-NAKDMNSLVyRIIEGKLPPMPRD-----Y 230
Cdd:cd06610  158 RTRkvrkTFVGTPCWMAPEvMEQVRGYDFKADIWSFGITAIELATGAAPYsKYPPMKVLM-LTLQNDPPSLETGadykkY 236
                        250       260       270
                 ....*....|....*....|....*....|.
gi 148839316 231 SPELAELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd06610  237 SKSFRKMISLCLQKDPSKRPTAEELLKHKFF 267
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
9-255 1.32e-34

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: 133.46  E-value: 1.32e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLNL-RNASSRERraAEQEAQLLSQLKHPNIVTYKESWEG----------GDG 77
Cdd:cd14048   11 IQCLGRGGFGVVFEAKNKVDDCNYAVKRIRLpNNELAREK--VLREVRALAKLDHPGIVRYFNAWLErppegwqekmDEV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  78 LLYIVMGFCEGGDLYRKLKEQKGQLLPENQV-VEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIA--- 153
Cdd:cd14048   89 YLYIQMQLCRKENLKDWMNRRCTMESRELFVcLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVGDFGLVtam 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 154 ---------RVLENHCDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEmatLKHAFNAKDMNSLVYRIIE-GKL 223
Cdd:cd14048  169 dqgepeqtvLTPMPAYAKHTGQVGTRLYMSPEQIHGNQYSEKVDIFALGLILFE---LIYSFSTQMERIRTLTDVRkLKF 245
                        250       260       270
                 ....*....|....*....|....*....|..
gi 148839316 224 PPMPRDYSPELAELIRTMLSKRPEERPSVRSI 255
Cdd:cd14048  246 PALFTNKYPEERDMVQQMLSPSPSERPEAHEV 277
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
12-256 1.40e-34

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: 132.23  E-value: 1.40e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRrdGKQYVIKKLnlrnassreRRAAEQEAQLLSQLKHPNIVTYKesweggdGLLY------IVMGF 85
Cdd:cd14059    1 LGSGAQGAVFLGKFR--GEEVAVKKV---------RDEKETDIKHLRKLNHPNIIKFK-------GVCTqapcycILMEY 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGGDLYRKLKEqkGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVL-ENHCDMas 164
Cdd:cd14059   63 CPYGQLYEVLRA--GREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKELsEKSTKM-- 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 TLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLP-PMPRDYSPELAELIRTMLS 243
Cdd:cd14059  139 SFAGTVAWMAPEVIRNEPCSEKVDIWSFGVVLWELLTGEIPYKDVDSSAIIWGVGSNSLQlPVPSTCPDGFKLLMKQCWN 218
                        250
                 ....*....|...
gi 148839316 244 KRPEERPSVRSIL 256
Cdd:cd14059  219 SKPRNRPSFRQIL 231
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
6-261 1.63e-34

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: 132.84  E-value: 1.63e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERrAAEQEAQLLSQLKHPNIVTYKESWEGGdGLLYIVMGF 85
Cdd:cd14167    5 YDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGKET-SIENEIAVLHKIKHPNIVALDDIYESG-GHLYLIMQL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGGDLYRKLKEqKGqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVF---LTRTNIIKVGDLGIARVlENHCDM 162
Cdd:cd14167   83 VSGGELFDRIVE-KG-FYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGLSKI-EGSGSV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 163 ASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKL---PPMPRDYSPELAELIR 239
Cdd:cd14167  160 MSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEYefdSPYWDDISDSAKDFIQ 239
                        250       260
                 ....*....|....*....|..
gi 148839316 240 TMLSKRPEERPSVRSILRQPYI 261
Cdd:cd14167  240 HLMEKDPEKRFTCEQALQHPWI 261
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
2-264 1.83e-34

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: 133.69  E-value: 1.83e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   2 PLAAYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLrnaSSRERRAAEQEAQLLSQLKH-PNIVTY-----KESWEGG 75
Cdd:cd06637    4 PAGIFELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDV---TGDEEEEIKQEINMLKKYSHhRNIATYygafiKKNPPGM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  76 DGLLYIVMGFCEGGDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARV 155
Cdd:cd06637   81 DDQLWLVMEFCGAGSVTDLIKNTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 156 LENHCDMASTLIGTPYYMSPELFS-----NKPYNYKSDVWALGCCVYEMAtlKHAFNAKDMNSL--VYRIIEGKLPPM-P 227
Cdd:cd06637  161 LDRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDFKSDLWSLGITAIEMA--EGAPPLCDMHPMraLFLIPRNPAPRLkS 238
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 148839316 228 RDYSPELAELIRTMLSKRPEERPSVRSILRQPYIKRQ 264
Cdd:cd06637  239 KKWSKKFQSFIESCLVKNHSQRPSTEQLMKHPFIRDQ 275
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
10-260 2.19e-34

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


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 133.17  E-value: 2.19e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGK---GSYGEVTLVKHRRDGKQYVIKKLNlRNASSRERRAAEQEAQLLSQLK-HPNIVTYKES-WEGGDGLLYIVMG 84
Cdd:cd07831    2 KILGKigeGTFSEVLKAQSRKTGKYYAIKCMK-KHFKSLEQVNNLREIQALRRLSpHPNILRLIEVlFDRKTGRLALVFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGgDLYRKLKEQKgQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVfLTRTNIIKVGDLGIARVLenHCDMAS 164
Cdd:cd07831   81 LMDM-NLYELIKGRK-RPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENI-LIKDDILKLADFGSCRGI--YSKPPY 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 T-LIGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAF---NAKDMNSLVYRII--------EGKLPPMPRDY- 230
Cdd:cd07831  156 TeYISTRWYRAPEcLLTDGYYGPKMDIWAVGCVFFEILSLFPLFpgtNELDQIAKIHDVLgtpdaevlKKFRKSRHMNYn 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 148839316 231 ----------------SPELAELIRTMLSKRPEERPSVRSILRQPY 260
Cdd:cd07831  236 fpskkgtglrkllpnaSAEGLDLLKKLLAYDPDERITAKQALRHPY 281
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
12-257 2.21e-34

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: 132.78  E-value: 2.21e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVkHRRDGKQYVIKKLNLRNASSRERRAaEQEAQLLSQLKHPNIVT-YKESWEGGDGLLyiVMGFCEGGD 90
Cdd:cd14066    1 IGSGGFGTVYKG-VLENGTVVAVKRLNEMNCAASKKEF-LTELEMLGRLRHPNLVRlLGYCLESDEKLL--VYEYMPNGS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  91 LYRKLKEQKGQllpenQVVEW------FVQIAMALQYLHE---KHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCD 161
Cdd:cd14066   77 LEDRLHCHKGS-----PPLPWpqrlkiAKGIARGLEYLHEecpPPIIHGDIKSSNILLDEDFEPKLTDFGLARLIPPSES 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 162 MAST--LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVY---------------RIIEGKLP 224
Cdd:cd14066  152 VSKTsaVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDENRENASRKdlvewveskgkeeleDILDKRLV 231
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 148839316 225 PMPRDYSPELAELIRTML---SKRPEERPSVRSILR 257
Cdd:cd14066  232 DDDGVEEEEVEALLRLALlctRSDPSLRPSMKEVVQ 267
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
6-253 2.40e-34

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: 132.47  E-value: 2.40e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKL-----NLRNASSRERRAAEQEAQLLSQL-KHPNIVTYKESWEGGDgLL 79
Cdd:cd13993    2 YQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLyksgpNSKDGNDFQKLPQLREIDLHRRVsRHPNIITLHDVFETEV-AI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  80 YIVMGFCEGGDLYRKLKEQKgqLLPENQVVEW--FVQIAMALQYLHEKHILHRDLKTQNVFLT-RTNIIKVGDLGIARVL 156
Cdd:cd13993   81 YIVLEYCPNGDLFEAITENR--IYVGKTELIKnvFLQLIDAVKHCHSLGIYHRDIKPENILLSqDEGTVKLCDFGLATTE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 157 ENHCDMAstlIGTPYYMSPELFSNKPYNYKS------DVWALGCC-------------VYEMATLKHAFNAKDMNslVYR 217
Cdd:cd13993  159 KISMDFG---VGSEFYMAPECFDEVGRSLKGypcaagDIWSLGIIllnltfgrnpwkiASESDPIFYDYYLNSPN--LFD 233
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 148839316 218 IIegklPPMprdySPELAELIRTMLSKRPEERPSVR 253
Cdd:cd13993  234 VI----LPM----SDDFYNLLRQIFTVNPNNRILLP 261
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
6-260 3.00e-34

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: 132.34  E-value: 3.00e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKhRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKH-PNIVTYKEsWE--GGDGLLYIV 82
Cdd:cd14131    3 YEILKQLGKGGSSKVYKVL-NPKKKIYALKRVDLEGADEQTLQSYKNEIELLKKLKGsDRIIQLYD-YEvtDEDDYLYMV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  83 MGFCEGgDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNvFLTRTNIIKVGDLGIARVLENHCD- 161
Cdd:cd14131   81 MECGEI-DLATILKKKRPKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPAN-FLLVKGRLKLIDFGIAKAIQNDTTs 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 162 -MASTLIGTPYYMSPELF---SNKPYN-------YKSDVWALGCCVYEMATLKHAF-NAKDMNSLVYRII----EGKLPP 225
Cdd:cd14131  159 iVRDSQVGTLNYMSPEAIkdtSASGEGkpkskigRPSDVWSLGCILYQMVYGKTPFqHITNPIAKLQAIIdpnhEIEFPD 238
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 148839316 226 MPrdySPELAELIRTMLSKRPEERPSVRSILRQPY 260
Cdd:cd14131  239 IP---NPDLIDVMKRCLQRDPKKRPSIPELLNHPF 270
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
6-261 3.07e-34

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: 131.83  E-value: 3.07e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSR-ERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLYIVMG 84
Cdd:cd14165    3 YILGINLGEGSYAKVKSAYSERLKCNVAIKIIDKKKAPDDfVEKFLPRELEILARLNHKSIIKTYEIFETSDGKVYIVME 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGGDLYRKLKEQkGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCD--- 161
Cdd:cd14165   83 LGVQGDLLEFIKLR-GAL-PEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCLRDENgri 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 162 -MASTLIGTPYYMSPELFSNKPYNYK-SDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPR-DYSPELAELI 238
Cdd:cd14165  161 vLSKTFCGSAAYAAPEVLQGIPYDPRiYDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQKEHRVRFPRSkNLTSECKDLI 240
                        250       260
                 ....*....|....*....|...
gi 148839316 239 RTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd14165  241 YRLLQPDVSQRLCIDEVLSHPWL 263
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
6-261 3.47e-34

Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PASK (or PASKIN) is a nutrient and energy sensor and thus, plays an important role in maintaining cellular energy homeostasis. It coordinates the utilization of glucose in response to metabolic demand. It contains an N-terminal PAS domain which directly interacts and inhibits a C-terminal catalytic kinase domain. The PAS domain serves as a sensory module for different environmental signals such as light, redox state, and various metabolites. Binding of ligands to the PAS domain causes structural changes which leads to kinase activation and the phosphorylation of substrates to trigger the appropriate cellular response. The PASK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270906 [Multi-domain]  Cd Length: 256  Bit Score: 131.74  E-value: 3.47e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGK----QYVIKKLNLRNASSRERRAAE--QEAQLLSQLK---HPNIVTYKESWEGgD 76
Cdd:cd14004    2 YTILKEMGEGAYGQVNLAIYKSKGKevviKFIFKERILVDTWVRDRKLGTvpLEIHILDTLNkrsHPNIVKLLDFFED-D 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  77 GLLYIVM-GFCEGGDLYRKLKEQKGQLLPENQVVewFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARV 155
Cdd:cd14004   81 EFYYLVMeKHGSGMDLFDFIERKPNMDEKEAKYI--FRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFGSAAY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 156 LENhcDMASTLIGTPYYMSPELFSNKPYNYKS-DVWALGCCVYEMATLKHAFnakdmnSLVYRIIEGKLPPmPRDYSPEL 234
Cdd:cd14004  159 IKS--GPFDTFVGTIDYAAPEVLRGNPYGGKEqDIWALGVLLYTLVFKENPF------YNIEEILEADLRI-PYAVSEDL 229
                        250       260
                 ....*....|....*....|....*..
gi 148839316 235 AELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd14004  230 IDLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
10-261 3.90e-34

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: 131.89  E-value: 3.90e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASS----RERR---AAEQEAQLLSQLKHPNIVTYKESWEGGDgLLYIV 82
Cdd:cd06628    6 ALIGSGSFGSVYLGMNASSGELMAVKQVELPSVSAenkdRKKSmldALQREIALLRELQHENIVQYLGSSSDAN-HLNIF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  83 MGFCEGGDLyRKLKEQKGQLlpENQVVEWFV-QIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLE-NHC 160
Cdd:cd06628   85 LEYVPGGSV-ATLLNNYGAF--EESLVRNFVrQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKKLEaNSL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 161 DMAS-----TLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPRDYSPELA 235
Cdd:cd06628  162 STKNngarpSLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFPDCTQMQAIFKIGENASPTIPSNISSEAR 241
                        250       260
                 ....*....|....*....|....*.
gi 148839316 236 ELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd06628  242 DFLEKTFEIDHNKRPTADELLKHPFL 267
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
9-259 4.89e-34

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: 130.89  E-value: 4.89e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLK-HPNIVTYKESWEGGdGLLYIVMGFCe 87
Cdd:cd14050    6 LSKLGEGSFGEVFKVRSREDGKLYAVKRSRSRFRGEKDRKRKLEEVERHEKLGeHPNCVRFIKAWEEK-GILYIQTELC- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  88 GGDLYRKLKEQkgQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIarVLE-NHCDMASTL 166
Cdd:cd14050   84 DTSLQQYCEET--HSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGL--VVElDKEDIHDAQ 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 167 IGTPYYMSPELFsNKPYNYKSDVWALGCCVYEMATlkhafnakDMN-----SLVYRIIEGKLP-PMPRDYSPELAELIRT 240
Cdd:cd14050  160 EGDPRYMAPELL-QGSFTKAADIFSLGITILELAC--------NLElpsggDGWHQLRQGYLPeEFTAGLSPELRSIIKL 230
                        250
                 ....*....|....*....
gi 148839316 241 MLSKRPEERPSVRSILRQP 259
Cdd:cd14050  231 MMDPDPERRPTAEDLLALP 249
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
53-250 7.12e-34

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 137.62  E-value: 7.12e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  53 EAQLLSQLKHPNIVTYKESWEGGdGLLYIVMGFCEGGDLyRKLKEQKGQLLPEnQVVEWFVQIAMALQYLHEKHILHRDL 132
Cdd:NF033483  57 EAQSAASLSHPNIVSVYDVGEDG-GIPYIVMEYVDGRTL-KDYIREHGPLSPE-EAVEIMIQILSALEHAHRNGIVHRDI 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 133 KTQNVFLTRTNIIKVGDLGIARVL-ENHCDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMAT---------- 201
Cdd:NF033483 134 KPQNILITKDGRVKVTDFGIARALsSTTMTQTNSVLGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTgrppfdgdsp 213
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 148839316 202 ----LKHaFNakdmnslvyriiegKLPPMPRDY----SPELAELIRTMLSKRPEERP 250
Cdd:NF033483 214 vsvaYKH-VQ--------------EDPPPPSELnpgiPQSLDAVVLKATAKDPDDRY 255
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
10-249 7.63e-34

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


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 132.82  E-value: 7.63e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAE-QEAQLLSQLKHPNIVTYKESWEGGDGLLYiVMGFCEG 88
Cdd:cd05595    1 KLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTvTESRVLQNTRHPFLTALKYAFQTHDRLCF-VMEYANG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  89 GDLYRKLKEQKgqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARvlENHCDMAS--TL 166
Cdd:cd05595   80 GELFFHLSRER--VFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCK--EGITDGATmkTF 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 167 IGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLpPMPRDYSPELAELIRTMLSKRP 246
Cdd:cd05595  156 CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEI-RFPRTLSPEAKSLLAGLLKKDP 234

                 ...
gi 148839316 247 EER 249
Cdd:cd05595  235 KQR 237
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
11-259 8.50e-34

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: 131.01  E-value: 8.50e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  11 VVGKGSYGEVTLVKHRRDGKQYVIKKLNL-RNASSRERRAAE---QEAQLLSQLKHPNIV-TYKESWEGGDglLYIVMGF 85
Cdd:cd06630    7 LLGTGAFSSCYQARDVKTGTLMAVKQVSFcRNSSSEQEEVVEairEEIRMMARLNHPNIVrMLGATQHKSH--FNIFVEW 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGGDLyRKLKEQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRT-NIIKVGDLGIARVLENHCDMAS 164
Cdd:cd06630   85 MAGGSV-ASLLSKYGAF-SENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTgQRLRIADFGAAARLASKGTGAG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 ----TLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMN---SLVYRIIEG-KLPPMPRDYSPELAE 236
Cdd:cd06630  163 efqgQLLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEKISnhlALIFKIASAtTPPPIPEHLSPGLRD 242
                        250       260
                 ....*....|....*....|...
gi 148839316 237 LIRTMLSKRPEERPSVRSILRQP 259
Cdd:cd06630  243 VTLRCLELQPEDRPPARELLKHP 265
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
6-260 1.19e-33

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: 131.15  E-value: 1.19e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNassrER----RAAEQEAQLLSQLKHPNIVTYKE-----SWEGGD 76
Cdd:cd07840    1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRMEN----EKegfpITAIREIKLLQKLDHPNVVRLKEivtskGSAKYK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  77 GLLYIVMGFCEGgDLyRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVL 156
Cdd:cd07840   77 GSIYMVFEYMDH-DL-TGLLDNPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLARPY 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 157 ENHCDMAST--LIgTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIE--G---------- 221
Cdd:cd07840  155 TKENNADYTnrVI-TLWYRPPElLLGATRYGPEVDMWSVGCILAELFTGKPIFQGKTELEQLEKIFElcGspteenwpgv 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 148839316 222 -KLP----PMP--------RDY-----SPELAELIRTMLSKRPEERPSVRSILRQPY 260
Cdd:cd07840  234 sDLPwfenLKPkkpykrrlREVfknviDPSALDLLDKLLTLDPKKRISADQALQHEY 290
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
6-261 1.31e-33

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: 130.26  E-value: 1.31e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLN-----LRNASSRERRAAE--------QEAQLLSQLKHPNIVTYKE-- 70
Cdd:cd14077    3 WEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIPrasnaGLKKEREKRLEKEisrdirtiREAALSSLLNHPHICRLRDfl 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  71 --SWEggdglLYIVMGFCEGGDLYR------KLKEQKGQllpenqvvEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRT 142
Cdd:cd14077   83 rtPNH-----YYMLFEYVDGGQLLDyiishgKLKEKQAR--------KFARQIASALDYLHRNSIVHRDLKIENILISKS 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 143 NIIKVGDLGIARVLENHcDMASTLIGTPYYMSPELFSNKPY-NYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEG 221
Cdd:cd14077  150 GNIKIIDFGLSNLYDPR-RLLRTFCGSLYFAAPELLQAQPYtGPEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKIKKG 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 148839316 222 KLpPMPRDYSPELAELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd14077  229 KV-EYPSYLSSECKSLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
12-261 1.74e-33

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: 130.16  E-value: 1.74e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLK-HPNIVTYKESWEGGDGLLyIVMGFCEGGD 90
Cdd:cd14106   16 LGRGKFAVVRKCIHKETGKEYAAKFLRKRRRGQDCRNEILHEIAVLELCKdCPRVVNLHEVYETRSELI-LILELAAGGE 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  91 LYRKLKEQkgQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNI---IKVGDLGIARVLENHCDMAStLI 167
Cdd:cd14106   95 LQTLLDEE--ECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFPlgdIKLCDFGISRVIGEGEEIRE-IL 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 168 GTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLppmprDYSPEL--------AELIR 239
Cdd:cd14106  172 GTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQCNL-----DFPEELfkdvsplaIDFIK 246
                        250       260
                 ....*....|....*....|..
gi 148839316 240 TMLSKRPEERPSVRSILRQPYI 261
Cdd:cd14106  247 RLLVKDPEKRLTAKECLEHPWL 268
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
12-259 2.77e-33

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: 129.85  E-value: 2.77e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRD-GKQYVIKKL--NLRNASSRERRAaeQEAQLLSQLK---HPNIVTYKESWEGGdGLLYIVMGF 85
Cdd:cd14052    8 IGSGEFSQVYKVSERVPtGKVYAVKKLkpNYAGAKDRLRRL--EEVSILRELTldgHDNIVQLIDSWEYH-GHLYIQTEL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGGDLYRKLKEQkGQL--LPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLEnhCDMA 163
Cdd:cd14052   85 CENGSLDVFLSEL-GLLgrLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMATVWP--LIRG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 164 STLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMAT------------------LKHAFNAKDMN----SLVYRIIEG 221
Cdd:cd14052  162 IEREGDREYIAPEILSEHMYDKPADIFSLGLILLEAAAnvvlpdngdawqklrsgdLSDAPRLSSTDlhsaSSPSSNPPP 241
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 148839316 222 KLPPMPRDySPELAELIRTMLSKRPEERPSVRSILRQP 259
Cdd:cd14052  242 DPPNMPIL-SGSLDRVVRWMLSPEPDRRPTADDVLATP 278
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
13-201 4.20e-33

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: 129.49  E-value: 4.20e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  13 GKGSYGEVTLVKHRRDGKQYVIKKLNLR-NASSRERRAAEQEAQLLSQLKHPNIVTYKESWEG-----GDGLLYIVMGFC 86
Cdd:cd13989    2 GSGGFGYVTLWKHQDTGEYVAIKKCRQElSPSDKNRERWCLEVQIMKKLNHPNVVSARDVPPEleklsPNDLPLLAMEYC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  87 EGGDLYRKLKEQKGQL-LPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTN---IIKVGDLGIARVLENHcDM 162
Cdd:cd13989   82 SGGDLRKVLNQPENCCgLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGgrvIYKLIDLGYAKELDQG-SL 160
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 148839316 163 ASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMAT 201
Cdd:cd13989  161 CTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECIT 199
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
5-260 4.40e-33

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: 129.36  E-value: 4.40e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   5 AYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEgGDGLLYIVMG 84
Cdd:cd07833    2 KYEVLGVVGEGAYGVVLKCRNKATGEIVAIKKFKESEDDEDVKKTALREVKVLRQLRHENIVNLKEAFR-RKGRLYLVFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEgGDLYRKLKEQKGQLLPEnQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLenHCDMAS 164
Cdd:cd07833   81 YVE-RTLLELLEASPGGLPPD-AVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARAL--TARPAS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 TL---IGTPYYMSPELF-SNKPYNYKSDVWALGCCVYEMATLKHAFNAK-DMNSLvYRI--IEGKLPP------------ 225
Cdd:cd07833  157 PLtdyVATRWYRAPELLvGDTNYGKPVDVWAIGCIMAELLDGEPLFPGDsDIDQL-YLIqkCLGPLPPshqelfssnprf 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 148839316 226 ----MPRDYSPE-LAELIRTMLSKR------------PEERPSVRSILRQPY 260
Cdd:cd07833  236 agvaFPEPSQPEsLERRYPGKVSSPaldflkaclrmdPKERLTCDELLQHPY 287
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
9-249 5.49e-33

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: 130.22  E-value: 5.49e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVK--HRRDGKQY----VIKKLNL-RNASSRERRAAEQeaQLLSQLKHPNIVTYKESWEGGdGLLYI 81
Cdd:cd05584    1 LKVLGKGGYGKVFQVRktTGSDKGKIfamkVLKKASIvRNQKDTAHTKAER--NILEAVKHPFIVDLHYAFQTG-GKLYL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  82 VMGFCEGGDLYRKLkEQKGqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIA--RVLENH 159
Cdd:cd05584   78 ILEYLSGGELFMHL-EREG-IFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLCkeSIHDGT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 160 cdMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPrdY-SPELAELI 238
Cdd:cd05584  156 --VTHTFCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGKLNLPP--YlTNEARDLL 231
                        250
                 ....*....|.
gi 148839316 239 RTMLSKRPEER 249
Cdd:cd05584  232 KKLLKRNVSSR 242
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
12-256 6.99e-33

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: 128.78  E-value: 6.99e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESW-EGGDGLLYIVMGFCEGG- 89
Cdd:cd14049   14 LGKGGYGKVYKVRNKLDGQYYAIKKILIKKVTKRDCMKVLREVKVLAGLQHPNIVGYHTAWmEHVQLMLYIQMQLCELSl 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  90 -----DLYRKLKEQKGQLLPENQV-VEW----FVQIAMALQYLHEKHILHRDLKTQNVFLTRTNI-IKVGDLGIA--RVL 156
Cdd:cd14049   94 wdwivERNKRPCEEEFKSAPYTPVdVDVttkiLQQLLEGVTYIHSMGIVHRDLKPRNIFLHGSDIhVRIGDFGLAcpDIL 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 157 ENHCDMASTL----------IGTPYYMSPELFSNKPYNYKSDVWALGCCVYEmatLKHAFNAkDMN--SLVYRIIEGKLP 224
Cdd:cd14049  174 QDGNDSTTMSrlnglthtsgVGTCLYAAPEQLEGSHYDFKSDMYSIGVILLE---LFQPFGT-EMEraEVLTQLRNGQIP 249
                        250       260       270
                 ....*....|....*....|....*....|..
gi 148839316 225 PMPRDYSPELAELIRTMLSKRPEERPSVRSIL 256
Cdd:cd14049  250 KSLCKRWPVQAKYIKLLTSTEPSERPSASQLL 281
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
12-262 7.37e-33

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: 129.00  E-value: 7.37e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRErrAAEQEAQLLSQLKHPNIVTYKESWEGGDGLlYIVMGFCEGGDL 91
Cdd:cd06658   30 IGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQRRE--LLFNEVVIMRDYHHENVVDMYNSYLVGDEL-WVVMEFLEGGAL 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  92 YRKLKEQKgqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTLIGTPY 171
Cdd:cd06658  107 TDIVTHTR---MNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQVSKEVPKRKSLVGTPY 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 172 YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLvyRIIEGKLPPMPRD---YSPELAELIRTMLSKRPE 247
Cdd:cd06658  184 WMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPyFNEPPLQAM--RRIRDNLPPRVKDshkVSSVLRGFLDLMLVREPS 261
                        250
                 ....*....|....*
gi 148839316 248 ERPSVRSILRQPYIK 262
Cdd:cd06658  262 QRATAQELLQHPFLK 276
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
10-249 7.64e-33

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: 128.60  E-value: 7.64e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRA-AEQEAQLLSQLKHPNIVTYKESWEGGDGLLyIVMGFCEG 88
Cdd:cd05630    6 RVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAmALNEKQILEKVNSRFVVSLAYAYETKDALC-LVLTLMNG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  89 GDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARvlenHCDMASTL-- 166
Cdd:cd05630   85 GDLKFHIYHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAV----HVPEGQTIkg 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 167 -IGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNA---KDMNSLVYRIIEGKLPPMPRDYSPELAELIRTML 242
Cdd:cd05630  161 rVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQrkkKIKREEVERLVKEVPEEYSEKFSPQARSLCSMLL 240

                 ....*..
gi 148839316 243 SKRPEER 249
Cdd:cd05630  241 CKDPAER 247
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
2-286 8.51e-33

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: 129.39  E-value: 8.51e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   2 PLAAYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRER-RAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLY 80
Cdd:cd06633   19 PEEIFVDLHEIGHGSFGAVYFATNSHTNEVVAIKKMSYSGKQTNEKwQDIIKEVKFLQQLKHPNTIEYKGCYLK-DHTAW 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  81 IVMGFCEGGDlyRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENhc 160
Cdd:cd06633   98 LVMEYCLGSA--SDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIASP-- 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 161 dmASTLIGTPYYMSPEL---FSNKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLvYRIIEGKLPPM-PRDYSPELA 235
Cdd:cd06633  174 --ANSFVGTPYWMAPEVilaMDEGQYDGKVDIWSLGITCIELAERKPPlFNMNAMSAL-YHIAQNDSPTLqSNEWTDSFR 250
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 148839316 236 ELIRTMLSKRPEERPSVRSILRQPYIKRQISFFLEATKIKTSKNNIKNGDS 286
Cdd:cd06633  251 GFVDYCLQKIPQERPSSAELLRHDFVRRERPPRVLIDLIQRTKDAVRELDN 301
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
11-258 9.58e-33

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: 127.51  E-value: 9.58e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  11 VVGKGSYGEVtlvkHRR--DGKQYVIK--KLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKeswegGDGL----LYIV 82
Cdd:cd14061    1 VIGVGGFGKV----YRGiwRGEEVAVKaaRQDPDEDISVTLENVRQEARLFWMLRHPNIIALR-----GVCLqppnLCLV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  83 MGFCEGGDLYRKLKeqkGQLLPENQVVEWFVQIAMALQYLHEKH---ILHRDLKTQNVFLTRT--------NIIKVGDLG 151
Cdd:cd14061   72 MEYARGGALNRVLA---GRKIPPHVLVDWAIQIARGMNYLHNEApvpIIHRDLKSSNILILEAienedlenKTLKITDFG 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 152 IARVLENHCDMASTliGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLP-PMPRDY 230
Cdd:cd14061  149 LAREWHKTTRMSAA--GTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPYKGIDGLAVAYGVAVNKLTlPIPSTC 226
                        250       260
                 ....*....|....*....|....*...
gi 148839316 231 SPELAELIRTMLSKRPEERPSVRSILRQ 258
Cdd:cd14061  227 PEPFAQLMKDCWQPDPHDRPSFADILKQ 254
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
12-249 1.08e-32

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: 128.03  E-value: 1.08e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRA-AEQEAQLLSQLKHPNIVTYKESWEGGDGLLyIVMGFCEGGD 90
Cdd:cd05577    1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKGETmALNEKIILEKVSSPFIVSLAYAFETKDKLC-LVLTLMNGGD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  91 LYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIArvlenhCDMAS-----T 165
Cdd:cd05577   80 LKYHIYNVGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLA------VEFKGgkkikG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 LIGTPYYMSPELFSNK-PYNYKSDVWALGCCVYEMATLKHAFNA----KDMNSLVYRIIEGKLpPMPRDYSPELAELIRT 240
Cdd:cd05577  154 RVGTHGYMAPEVLQKEvAYDFSVDWFALGCMLYEMIAGRSPFRQrkekVDKEELKRRTLEMAV-EYPDSFSPEARSLCEG 232

                 ....*....
gi 148839316 241 MLSKRPEER 249
Cdd:cd05577  233 LLQKDPERR 241
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
6-261 1.19e-32

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: 127.66  E-value: 1.19e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDgLLYIVMGF 85
Cdd:cd14097    3 YTFGRKLGQGSFGVVIEATHKETQTKWAIKKINREKAGSSAVKLLEREVDILKHVNHAHIIHLEEVFETPK-RMYLVMEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGGDLyRKLKEQKGQLlPENQVvEWFVQ-IAMALQYLHEKHILHRDLKTQNVFLTRTNI-------IKVGDLGIARVLE 157
Cdd:cd14097   82 CEDGEL-KELLLRKGFF-SENET-RHIIQsLASAVAYLHKNDIVHRDLKLENILVKSSIIdnndklnIKVTDFGLSVQKY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 158 N-HCDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLP---PMPRDYSPE 233
Cdd:cd14097  159 GlGEDMLQETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDLTftqSVWQSVSDA 238
                        250       260
                 ....*....|....*....|....*...
gi 148839316 234 LAELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd14097  239 AKNVLQQLLKVDPAHRMTASELLDNPWI 266
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
10-261 1.20e-32

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: 127.45  E-value: 1.20e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLNL---RNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDG-LLYIVMGF 85
Cdd:cd06653    8 KLLGRGAFGEVYLCYDADTGRELAVKQVPFdpdSQETSKEVNALECEIQLLKNLRHDRIVQYYGCLRDPEEkKLSIFVEY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGGDLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCdMAST 165
Cdd:cd06653   88 MPGGSVKDQLKAYGA--LTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRIQTIC-MSGT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 LI----GTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRI-IEGKLPPMPRDYSPELAELIRT 240
Cdd:cd06653  165 GIksvtGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPWAEYEAMAAIFKIaTQPTKPQLPDGVSDACRDFLRQ 244
                        250       260
                 ....*....|....*....|.
gi 148839316 241 MLSKRpEERPSVRSILRQPYI 261
Cdd:cd06653  245 IFVEE-KRRPTAEFLLRHPFV 264
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
6-262 2.03e-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: 128.04  E-value: 2.03e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAE---QEAQLLSQLKHPNIVTYKESWEGgDGLLYIV 82
Cdd:cd14094    5 YELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFTSSPGLSTEdlkREASICHMLKHPHIVELLETYSS-DGMLYMV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  83 MGFCEGGDLYRKL--KEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNI---IKVGDLGIARVLE 157
Cdd:cd14094   84 FEFMDGADLCFEIvkRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 158 NHCDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNsLVYRIIEGKL---PPMPRDYSPEL 234
Cdd:cd14094  164 ESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKER-LFEGIIKGKYkmnPRQWSHISESA 242
                        250       260
                 ....*....|....*....|....*...
gi 148839316 235 AELIRTMLSKRPEERPSVRSILRQPYIK 262
Cdd:cd14094  243 KDLVRRMLMLDPAERITVYEALNHPWIK 270
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
10-261 2.59e-32

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: 126.70  E-value: 2.59e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNAS---SRERRAAEQEAQLLSQLKHPNIVTY----KESWEGgdgLLYIV 82
Cdd:cd06652    8 KLLGQGAFGRVYLCYDADTGRELAVKQVQFDPESpetSKEVNALECEIQLLKNLLHERIVQYygclRDPQER---TLSIF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  83 MGFCEGGDLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDM 162
Cdd:cd06652   85 MEYMPGGSIKDQLKSYGA--LTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGASKRLQTICLS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 163 AS---TLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRI----IEGKLPPMPRDYSPELa 235
Cdd:cd06652  163 GTgmkSVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPWAEFEAMAAIFKIatqpTNPQLPAHVSDHCRDF- 241
                        250       260
                 ....*....|....*....|....*.
gi 148839316 236 eLIRTMLSKRpeERPSVRSILRQPYI 261
Cdd:cd06652  242 -LKRIFVEAK--LRPSADELLRHTFV 264
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
12-263 2.63e-32

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: 127.15  E-value: 2.63e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEgGDGLLYIVMGFCEGGDL 91
Cdd:cd14086    9 LGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSIS-EEGFHYLVFDLVTGGEL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  92 YRKLKEQKgqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFL---TRTNIIKVGDLGIARVLENHCDMASTLIG 168
Cdd:cd14086   88 FEDIVARE--FYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLaskSKGAAVKLADFGLAIEVQGDQQAWFGFAG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 169 TPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKL---PPMPRDYSPELAELIRTMLSKR 245
Cdd:cd14086  166 TPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYdypSPEWDTVTPEAKDLINQMLTVN 245
                        250
                 ....*....|....*...
gi 148839316 246 PEERPSVRSILRQPYIKR 263
Cdd:cd14086  246 PAKRITAAEALKHPWICQ 263
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
11-261 2.82e-32

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: 126.37  E-value: 2.82e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  11 VVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNasSRERRAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGFCEGGD 90
Cdd:cd06624   15 VLGKGTFGVVYAARDLSTQVRIAIKEIPERD--SREVQPLHEEIALHSRLSHKNIVQYLGSVSE-DGFFKIFMEQVPGGS 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  91 LYRKLKEQKGQLLPENQVVEWFV-QIAMALQYLHEKHILHRDLKTQNVFL-TRTNIIKVGDLGIARVLENHCDMASTLIG 168
Cdd:cd06624   92 LSALLRSKWGPLKDNENTIGYYTkQILEGLKYLHDNKIVHRDIKGDNVLVnTYSGVVKISDFGTSKRLAGINPCTETFTG 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 169 TPYYMSPELFSNKPYNY--KSDVWALGCCVYEMATLKHAF-NAKDMNSLVYRIIEGKL-PPMPRDYSPELAELIRTMLSK 244
Cdd:cd06624  172 TLQYMAPEVIDKGQRGYgpPADIWSLGCTIIEMATGKPPFiELGEPQAAMFKVGMFKIhPEIPESLSEEAKSFILRCFEP 251
                        250
                 ....*....|....*..
gi 148839316 245 RPEERPSVRSILRQPYI 261
Cdd:cd06624  252 DPDKRATASDLLQDPFL 268
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
12-261 2.91e-32

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: 127.07  E-value: 2.91e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRnaSSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLlYIVMGFCEGG-- 89
Cdd:cd06643   13 LGDGAFGKVYKAQNKETGILAAAKVIDTK--SEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNL-WILIEFCAGGav 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  90 -----DLYRKLKEqkgqllPENQVVewFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMAS 164
Cdd:cd06643   90 davmlELERPLTE------PQIRVV--CKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTRTLQRRD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 TLIGTPYYMSPELF-----SNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPM--PRDYSPELAEL 237
Cdd:cd06643  162 SFIGTPYWMAPEVVmcetsKDRPYDYKADVWSLGVTLIEMAQIEPPHHELNPMRVLLKIAKSEPPTLaqPSRWSPEFKDF 241
                        250       260
                 ....*....|....*....|....
gi 148839316 238 IRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd06643  242 LRKCLEKNVDARWTTSQLLQHPFV 265
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
36-260 3.02e-32

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: 126.27  E-value: 3.02e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  36 KLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEG---GDGLLYIVMGFCEGGDL---YRKLKEQKGQLLPenqvv 109
Cdd:cd14033   33 ELQTRKLSKGERQRFSEEVEMLKGLQHPNIVRFYDSWKStvrGHKCIILVTELMTSGTLktyLKRFREMKLKLLQ----- 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 110 EWFVQIAMALQYLHEKH--ILHRDLKTQNVFLT-RTNIIKVGDLGIARVleNHCDMASTLIGTPYYMSPELFSNKpYNYK 186
Cdd:cd14033  108 RWSRQILKGLHFLHSRCppILHRDLKCDNIFITgPTGSVKIGDLGLATL--KRASFAKSVIGTPEFMAPEMYEEK-YDEA 184
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148839316 187 SDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPP--MPRDYSPELAELIRTMLSKRPEERPSVRSILRQPY 260
Cdd:cd14033  185 VDVYAFGMCILEMATSEYPYSECQNAAQIYRKVTSGIKPdsFYKVKVPELKEIIEGCIRTDKDERFTIQDLLEHRF 260
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
10-260 3.15e-32

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: 126.20  E-value: 3.15e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYG---EVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQllSQLKHPNIVTYKESWEGGDgLLYIVMGFC 86
Cdd:cd14187   13 RFLGKGGFAkcyEITDADTKEVFAGKIVPKSLLLKPHQKEKMSMEIAIH--RSLAHQHVVGFHGFFEDND-FVYVVLELC 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  87 EGGDLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTL 166
Cdd:cd14187   90 RRRSLLELHKRRKA--LTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKVEYDGERKKTL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 167 IGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLpPMPRDYSPELAELIRTMLSKRP 246
Cdd:cd14187  168 CGTPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEY-SIPKHINPVAASLIQKMLQTDP 246
                        250
                 ....*....|....
gi 148839316 247 EERPSVRSILRQPY 260
Cdd:cd14187  247 TARPTINELLNDEF 260
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
10-261 4.20e-32

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: 125.58  E-value: 4.20e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDgLLYIVMGFCEGG 89
Cdd:cd14071    6 RTIGKGNFAVVKLARHRITKTEVAIKIIDKSQLDEENLKKIYREVQIMKMLNHPHIIKLYQVMETKD-MLYLVTEYASNG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  90 DLYRKLKeQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHcDMASTLIGT 169
Cdd:cd14071   85 EIFDYLA-QHGRM-SEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSNFFKPG-ELLKTWCGS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 170 PYYMSPELFSNKPYN-YKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLpPMPRDYSPELAELIRTMLSKRPEE 248
Cdd:cd14071  162 PPYAAPEVFEGKEYEgPQLDIWSLGVVLYVLVCGALPFDGSTLQTLRDRVLSGRF-RIPFFMSTDCEHLIRRMLVLDPSK 240
                        250
                 ....*....|...
gi 148839316 249 RPSVRSILRQPYI 261
Cdd:cd14071  241 RLTIEQIKKHKWM 253
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
10-260 4.20e-32

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: 125.83  E-value: 4.20e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERrAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGFCEGG 89
Cdd:cd14185    6 RTIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGKED-MIESEILIIKSLSHPNIVKLFEVYET-EKEIYLILEYVRGG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  90 DLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTR----TNIIKVGDLGIARVLENHCdmaST 165
Cdd:cd14185   84 DLFDAIIESVK--FTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHnpdkSTTLKLADFGLAKYVTGPI---FT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNS-LVYRIIEGK----LPPMPRDYSPELAELIRT 240
Cdd:cd14185  159 VCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRSPERDQeELFQIIQLGhyefLPPYWDNISEAAKDLISR 238
                        250       260
                 ....*....|....*....|
gi 148839316 241 MLSKRPEERPSVRSILRQPY 260
Cdd:cd14185  239 LLVVDPEKRYTAKQVLQHPW 258
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
12-198 5.23e-32

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: 126.19  E-value: 5.23e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLR-NASSRERRAaeQEAQLLSQLKHPNIVTYKESWEGGDGLL----YIVMGFC 86
Cdd:cd14039    1 LGTGGFGNVCLYQNQETGEKIAIKSCRLElSVKNKDRWC--HEIQIMKKLNHPNVVKACDVPEEMNFLVndvpLLAMEYC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  87 EGGDLyRKL--KEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTN---IIKVGDLGIARVLENHcD 161
Cdd:cd14039   79 SGGDL-RKLlnKPENCCGLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINgkiVHKIIDLGYAKDLDQG-S 156
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 148839316 162 MASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYE 198
Cdd:cd14039  157 LCTSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFE 193
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
2-262 5.35e-32

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: 125.42  E-value: 5.35e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   2 PLAAYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRErrAAEQEAQLLSQLKHPNIVTYKESWEGGDGLlYI 81
Cdd:cd06647    5 PKKKYTRFEKIGQGASGTVYTAIDVATGQEVAIKQMNLQQQPKKE--LIINEILVMRENKNPNIVNYLDSYLVGDEL-WV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  82 VMGFCEGGDLYRKLKEQkgqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCD 161
Cdd:cd06647   82 VMEYLAGGSLTDVVTET---CMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 162 MASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLP--PMPRDYSPELAELIR 239
Cdd:cd06647  159 KRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPelQNPEKLSAIFRDFLN 238
                        250       260
                 ....*....|....*....|...
gi 148839316 240 TMLSKRPEERPSVRSILRQPYIK 262
Cdd:cd06647  239 RCLEMDVEKRGSAKELLQHPFLK 261
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
6-260 5.78e-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: 126.46  E-value: 5.78e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKK-LNLRNASSRErraaeqeAQLLSQLKHPNIVT-----YKESWEGGDGLL 79
Cdd:cd14137    6 YTIEKVIGSGSFGVVYQAKLLETGEVVAIKKvLQDKRYKNRE-------LQIMRRLKHPNIVKlkyffYSSGEKKDEVYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  80 YIVMGFCEGgDLYRKLKE--QKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFL-TRTNIIKVGDLGIARVL 156
Cdd:cd14137   79 NLVMEYMPE-TLYRVIRHysKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVdPETGVLKLCDFGSAKRL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 157 ENHcDMASTLIGTPYYMSPEL-FSNKPYNYKSDVWALGCCVYEMATLKHAFNA----------------------KDMNS 213
Cdd:cd14137  158 VPG-EPNVSYICSRYYRAPELiFGATDYTTAIDIWSAGCVLAELLLGQPLFPGessvdqlveiikvlgtptreqiKAMNP 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 148839316 214 LVYRIIEGKLPPMPRDY------SPELAELIRTMLSKRPEERPSVRSILRQPY 260
Cdd:cd14137  237 NYTEFKFPQIKPHPWEKvfpkrtPPDAIDLLSKILVYNPSKRLTALEALAHPF 289
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
8-258 6.12e-32

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: 127.44  E-value: 6.12e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   8 YLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRN--ASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLlYIVMGF 85
Cdd:cd05602   11 FLKVIGKGSFGKVLLARHKSDEKFYAVKVLQKKAilKKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQTTDKL-YFVLDY 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGGDLYRKLKEQKGQLLPENQVveWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMAST 165
Cdd:cd05602   90 INGGELFYHLQRERCFLEPRARF--YAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIEPNGTTST 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMatlkhafnakdmnslVYriiegKLPPMprdYSPELAELIRTMLSKR 245
Cdd:cd05602  168 FCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEM---------------LY-----GLPPF---YSRNTAEMYDNILNKP 224
                        250
                 ....*....|...
gi 148839316 246 PEERPSVRSILRQ 258
Cdd:cd05602  225 LQLKPNITNSARH 237
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
12-261 7.47e-32

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: 126.25  E-value: 7.47e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRErrAAEQEAQLLSQLKHPNIVTYKESWEGGDGLlYIVMGFCEGGDL 91
Cdd:cd06659   29 IGEGSTGVVCIAREKHSGRQVAVKMMDLRKQQRRE--LLFNEVVIMRDYQHPNVVEMYKSYLVGEEL-WVLMEYLQGGAL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  92 YRKLKEQKgqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTLIGTPY 171
Cdd:cd06659  106 TDIVSQTR---LNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFCAQISKDVPKRKSLVGTPY 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 172 YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKlPPMPRDY---SPELAELIRTMLSKRPEE 248
Cdd:cd06659  183 WMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRDSP-PPKLKNShkaSPVLRDFLERMLVRDPQE 261
                        250
                 ....*....|...
gi 148839316 249 RPSVRSILRQPYI 261
Cdd:cd06659  262 RATAQELLDHPFL 274
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
12-249 8.84e-32

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 126.86  E-value: 8.84e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRNA-SSRERRAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGFCEGGD 90
Cdd:PTZ00263  26 LGTGSFGRVRIAKHKGTGEYYAIKCLKKREIlKMKQVQHVAQEKSILMELSHPFIVNMMCSFQD-ENRVYFLLEFVVGGE 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  91 LYRKLKeqKGQLLPeNQVVEWF-VQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLEnhcDMASTLIGT 169
Cdd:PTZ00263 105 LFTHLR--KAGRFP-NDVAKFYhAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVP---DRTFTLCGT 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 170 PYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLpPMPRDYSPELAELIRTMLSKRPEER 249
Cdd:PTZ00263 179 PEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRL-KFPNWFDGRARDLVKGLLQTDHTKR 257
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
6-275 1.20e-31

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: 125.44  E-value: 1.20e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLnlrnasSRERRAAEQEAQ-LLSQLKHPNIVTYKESWEGGdGLLYIVMG 84
Cdd:cd14091    2 YEIKEEIGKGSYSVCKRCIHKATGKEYAVKII------DKSKRDPSEEIEiLLRYGQHPNIITLRDVYDDG-NSVYLVTE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGGDLYRKLKEQKgqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNV-FLTRT---NIIKVGDLGIARVL--EN 158
Cdd:cd14091   75 LLRGGELLDRILRQK--FFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNIlYADESgdpESLRICDFGFAKQLraEN 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 159 hcdmasTLIGTPYY----MSPELFSNKPYNYKSDVWALGCCVYEMAT--LKHAFNAKDM-NSLVYRIIEGKLP---PMPR 228
Cdd:cd14091  153 ------GLLMTPCYtanfVAPEVLKKQGYDAACDIWSLGVLLYTMLAgyTPFASGPNDTpEVILARIGSGKIDlsgGNWD 226
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 148839316 229 DYSPELAELIRTMLSKRPEERPSVRSILRQPYIK-------RQISFFLEATKIK 275
Cdd:cd14091  227 HVSDSAKDLVRKMLHVDPSQRPTAAQVLQHPWIRnrdslpqRQLTDPQDAALVK 280
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
13-262 1.32e-31

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: 124.84  E-value: 1.32e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  13 GKGSYGEVTLVKHRRDGKQYVIKKLNLrNASSRERRaaeqeaQLLSQLK-------HPNIVT-YKESWEGGDglLYIVMG 84
Cdd:cd06617   10 GRGAYGVVDKMRHVPTGTIMAVKRIRA-TVNSQEQK------RLLMDLDismrsvdCPYTVTfYGALFREGD--VWICME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGG--DLYRKLKeQKGQLLPENQVVEWFVQIAMALQYLHEK-HILHRDLKTQNVFLTRTNIIKVGDLGIARVLENhcD 161
Cdd:cd06617   81 VMDTSldKFYKKVY-DKGLTIPEDILGKIAVSIVKALEYLHSKlSVIHRDVKPSNVLINRNGQVKLCDFGISGYLVD--S 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 162 MASTL-IGTPYYMSPELF----SNKPYNYKSDVWALGCCVYEMATLKHAF-NAKDMNSLVYRIIEGKLPPMPRD-YSPEL 234
Cdd:cd06617  158 VAKTIdAGCKPYMAPERInpelNQKGYDVKSDVWSLGITMIELATGRFPYdSWKTPFQQLKQVVEEPSPQLPAEkFSPEF 237
                        250       260
                 ....*....|....*....|....*...
gi 148839316 235 AELIRTMLSKRPEERPSVRSILRQPYIK 262
Cdd:cd06617  238 QDFVNKCLKKNYKERPNYPELLQHPFFE 265
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
6-258 1.89e-31

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: 124.33  E-value: 1.89e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRErrAAEQEAQLLSQLKHPNIVTYKESW----EGGDGLLYI 81
Cdd:cd13986    2 YRIQRLLGEGGFSFVYLVEDLSTGRLYALKKILCHSKEDVK--EAMREIENYRLFNHPNILRLLDSQivkeAGGKKEVYL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  82 VMGFCEGG---DLYRKLKEqKGQLLPENQVVEWFVQIAMALQYLHE---KHILHRDLKTQNVFLTRTNIIKVGDLG---I 152
Cdd:cd13986   80 LLPYYKRGslqDEIERRLV-KGTFFPEDRILHIFLGICRGLKAMHEpelVPYAHRDIKPGNVLLSEDDEPILMDLGsmnP 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 153 ARVLENHCDMASTLI------GTPYYMSPELFSNKPY---NYKSDVWALGCCVYEMATLKHAFnakDM-----NSLVYRI 218
Cdd:cd13986  159 ARIEIEGRREALALQdwaaehCTMPYRAPELFDVKSHctiDEKTDIWSLGCTLYALMYGESPF---ERifqkgDSLALAV 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 148839316 219 IEGKL-PPMPRDYSPELAELIRTMLSKRPEERPSVRSILRQ 258
Cdd:cd13986  236 LSGNYsFPDNSRYSEELHQLVKSMLVVNPAERPSIDDLLSR 276
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
2-270 2.69e-31

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: 124.01  E-value: 2.69e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   2 PLAAYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSrERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLlYI 81
Cdd:cd06642    2 PEELFTKLERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEEAED-EIEDIQQEITVLSQCDSPYITRYYGSYLKGTKL-WI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  82 VMGFCEGGDLYRKLKEQKgqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCD 161
Cdd:cd06642   80 IMEYLGGGSALDLLKPGP---LEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 162 MASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPRDYSPELAELIRTM 241
Cdd:cd06642  157 KRNTFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDLHPMRVLFLIPKNSPPTLEGQHSKPFKEFVEAC 236
                        250       260       270
                 ....*....|....*....|....*....|..
gi 148839316 242 LSKRPEERPSVRSILRQPYIKR---QISFFLE 270
Cdd:cd06642  237 LNKDPRFRPTAKELLKHKFITRytkKTSFLTE 268
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
9-263 3.13e-31

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: 123.64  E-value: 3.13e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSrERRAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGFCEG 88
Cdd:cd06641    9 LEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAED-EIEDIQQEITVLSQCDSPYVTKYYGSYLK-DTKLWIIMEYLGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  89 GDLYRKLKEQKgqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTLIG 168
Cdd:cd06641   87 GSALDLLEPGP---LDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIKRN*FVG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 169 TPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPRDYSPELAELIRTMLSKRPEE 248
Cdd:cd06641  164 TPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIPKNNPPTLEGNYSKPLKEFVEACLNKEPSF 243
                        250
                 ....*....|....*
gi 148839316 249 RPSVRSILRQPYIKR 263
Cdd:cd06641  244 RPTAKELLKHKFILR 258
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
36-272 3.30e-31

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: 123.68  E-value: 3.30e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  36 KLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEG---GDGLLYIVMGFCEGGDLYRKLKEQKgqLLPENQVVEWF 112
Cdd:cd14031   42 ELQDRKLTKAEQQRFKEEAEMLKGLQHPNIVRFYDSWESvlkGKKCIVLVTELMTSGTLKTYLKRFK--VMKPKVLRSWC 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 113 VQIAMALQYLHEKH--ILHRDLKTQNVFLT-RTNIIKVGDLGIARVLENhcDMASTLIGTPYYMSPELFSNKpYNYKSDV 189
Cdd:cd14031  120 RQILKGLQFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLATLMRT--SFAKSVIGTPEFMAPEMYEEH-YDESVDV 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 190 WALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMP--RDYSPELAELIRTMLSKRPEERPSVRSILRQpyikrqiSF 267
Cdd:cd14031  197 YAFGMCMLEMATSEYPYSECQNAAQIYRKVTSGIKPASfnKVTDPEVKEIIEGCIRQNKSERLSIKDLLNH-------AF 269

                 ....*
gi 148839316 268 FLEAT 272
Cdd:cd14031  270 FAEDT 274
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
10-260 3.37e-31

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called Doublecortin-like and CAM kinase-like 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL2 (or DCAMKL2) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL2 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL2 has been shown to interact with tubulin, JIP1/2, JNK, neurabin 2, and actin. It is associated with the terminal segments of axons and dendrites, and may function as a phosphorylation-dependent switch to control microtubule dynamics in neuronal growth cones. The DCKL2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 123.22  E-value: 3.37e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERrAAEQEAQLLSQLKHPNIVTYKESWEGGdGLLYIVMGFCEGG 89
Cdd:cd14184    7 KVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKEH-LIENEVSILRRVKHPNIIMLIEEMDTP-AELYLVMELVKGG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  90 DLY------RKLKEQKGQLLPENqvvewfvqIAMALQYLHEKHILHRDLKTQNVFLTR----TNIIKVGDLGIARVLENH 159
Cdd:cd14184   85 DLFdaitssTKYTERDASAMVYN--------LASALKYLHGLCIVHRDIKPENLLVCEypdgTKSLKLGDFGLATVVEGP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 160 CdmaSTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKD--MNSLVYRIIEGKLP-PMP--RDYSPEL 234
Cdd:cd14184  157 L---YTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSENnlQEDLFDQILLGKLEfPSPywDNITDSA 233
                        250       260
                 ....*....|....*....|....*.
gi 148839316 235 AELIRTMLSKRPEERPSVRSILRQPY 260
Cdd:cd14184  234 KELISHMLQVNVEARYTAEQILSHPW 259
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
2-262 3.44e-31

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: 123.95  E-value: 3.44e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   2 PLAAYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRErraAEQEAQLLSQL-KHPNIVTYKESWEGGD---- 76
Cdd:cd06639   20 PSDTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKILDPISDVDEE---IEAEYNILRSLpNHPNVVKFYGMFYKADqyvg 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  77 GLLYIVMGFCEGGDLYRKLKE--QKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIAR 154
Cdd:cd06639   97 GQLWLVLELCNGGSVTELVKGllKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSA 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 155 VLENHCDMASTLIGTPYYMSPELFS-----NKPYNYKSDVWALGCCVYEMATLKHAFNakDMNSL--VYRIIEGKLPPM- 226
Cdd:cd06639  177 QLTSARLRRNTSVGTPFWMAPEVIAceqqyDYSYDARCDVWSLGITAIELADGDPPLF--DMHPVkaLFKIPRNPPPTLl 254
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 148839316 227 -PRDYSPELAELIRTMLSKRPEERPSVRSILRQPYIK 262
Cdd:cd06639  255 nPEKWCRGFSHFISQCLIKDFEKRPSVTHLLEHPFIK 291
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
10-275 5.16e-31

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: 123.23  E-value: 5.16e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRA-AEQEAQLLSQLKHPNIVTYKESWEGGDGLLyIVMGFCEG 88
Cdd:cd05605    6 RVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAmALNEKQILEKVNSRFVVSLAYAYETKDALC-LVLTIMNG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  89 GDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHcDMASTLIG 168
Cdd:cd05605   85 GDLKFHIYNMGNPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVEIPEG-ETIRGRVG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 169 TPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNA---KDMNSLVYRIIEGKLPPMPRDYSPELAELIRTMLSKR 245
Cdd:cd05605  164 TVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRArkeKVKREEVDRRVKEDQEEYSEKFSEEAKSICSQLLQKD 243
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 148839316 246 PEER-----PSVRSILRQPYIKrQISF-FLEATKIK 275
Cdd:cd05605  244 PKTRlgcrgEGAEDVKSHPFFK-SINFkRLEAGLLE 278
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
9-262 5.33e-31

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: 122.59  E-value: 5.33e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRER--RAAEQEAQLLSQLKHPNIVTYKESWEGGDgLLYIVMGFC 86
Cdd:cd05611    1 LKPISKGAFGSVYLAKKRSTGDYFAIKVLKKSDMIAKNQvtNVKAERAIMMIQGESPYVAKLYYSFQSKD-YLYLVMEYL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  87 EGGDLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARV-LENHcdMAST 165
Cdd:cd05611   80 NGGDCASLIKTLGG--LPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSRNgLEKR--HNKK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKL--PPMPRDY-SPELAELIRTML 242
Cdd:cd05611  156 FVGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRRInwPEEVKEFcSPEAVDLINRLL 235
                        250       260
                 ....*....|....*....|...
gi 148839316 243 SKRPEER---PSVRSILRQPYIK 262
Cdd:cd05611  236 CMDPAKRlgaNGYQEIKSHPFFK 258
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
12-251 5.75e-31

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: 122.56  E-value: 5.75e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIV----TYKESWEGGdgllyIVMGFCE 87
Cdd:cd13978    1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIEERKALLKEAEKMERARHSYVLpllgVCVERRSLG-----LVMEYME 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  88 GGDLyRKLKEQKGQLLPENQVVEWFVQIAMALQYLH--EKHILHRDLKTQNVFLTRTNIIKVGDLGIARV-----LENHC 160
Cdd:cd13978   76 NGSL-KSLLEREIQDVPWSLRFRIIHEIALGMNFLHnmDPPLLHHDLKPENILLDNHFHVKISDFGLSKLgmksiSANRR 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 161 DMASTLIGTPYYMSPELFS--NKPYNYKSDVWALGCCVYEMATLKHAF-NAKDMNSLVYRIIEGK---LPPMPRDYSPE- 233
Cdd:cd13978  155 RGTENLGGTPIYMAPEAFDdfNKKPTSKSDVYSFAIVIWAVLTRKEPFeNAINPLLIMQIVSKGDrpsLDDIGRLKQIEn 234
                        250       260
                 ....*....|....*....|.
gi 148839316 234 LAELIRTML---SKRPEERPS 251
Cdd:cd13978  235 VQELISLMIrcwDGNPDARPT 255
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
10-260 7.36e-31

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK3 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. In addition, MEKK3 is involved in interleukin-1 receptor and Toll-like receptor 4 signaling. It is also a specific regulator of the proinflammatory cytokines IL-6 and GM-CSF in some immune cells. MEKK3 also regulates calcineurin, which plays a critical role in T cell activation, apoptosis, skeletal myocyte differentiation, and cardiac hypertrophy. The MEKK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 122.50  E-value: 7.36e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNAS---SRERRAAEQEAQLLSQLKHPNIVTYKESW-EGGDGLLYIVMGF 85
Cdd:cd06651   13 KLLGQGAFGRVYLCYDVDTGRELAAKQVQFDPESpetSKEVSALECEIQLLKNLQHERIVQYYGCLrDRAEKTLTIFMEY 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGGDLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCdMAST 165
Cdd:cd06651   93 MPGGSVKDQLKAYGA--LTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTIC-MSGT 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 ----LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRI-IEGKLPPMPRDYSPELAELIRT 240
Cdd:cd06651  170 girsVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIaTQPTNPQLPSHISEHARDFLGC 249
                        250       260
                 ....*....|....*....|
gi 148839316 241 MLSKrPEERPSVRSILRQPY 260
Cdd:cd06651  250 IFVE-ARHRPSAEELLRHPF 268
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
8-249 8.34e-31

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: 124.42  E-value: 8.34e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   8 YLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAE-QEAQLLSQLKHPNIVTYKESWEGGDGLLYiVMGFC 86
Cdd:cd05593   19 YLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTlTESRVLKNTRHPFLTSLKYSFQTKDRLCF-VMEYV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  87 EGGDLYRKLKEQKgqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARvlENHCDMAS-- 164
Cdd:cd05593   98 NGGELFFHLSRER--VFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCK--EGITDAATmk 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 TLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLvYRIIEGKLPPMPRDYSPELAELIRTMLSK 244
Cdd:cd05593  174 TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKL-FELILMEDIKFPRTLSADAKSLLSGLLIK 252

                 ....*
gi 148839316 245 RPEER 249
Cdd:cd05593  253 DPNKR 257
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
2-262 9.11e-31

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: 122.91  E-value: 9.11e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   2 PLAAYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRErrAAEQEAQLLSQLKHPNIVTYKESWEGGDGLlYI 81
Cdd:cd06655   17 PKKKYTRYEKIGQGASGTVFTAIDVATGQEVAIKQINLQKQPKKE--LIINEILVMKELKNPNIVNFLDSFLVGDEL-FV 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  82 VMGFCEGGDLYRKLKEQkgqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCD 161
Cdd:cd06655   94 VMEYLAGGSLTDVVTET---CMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQITPEQS 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 162 MASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPM--PRDYSPELAELIR 239
Cdd:cd06655  171 KRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELqnPEKLSPIFRDFLN 250
                        250       260
                 ....*....|....*....|...
gi 148839316 240 TMLSKRPEERPSVRSILRQPYIK 262
Cdd:cd06655  251 RCLEMDVEKRGSAKELLQHPFLK 273
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
10-249 9.30e-31

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: 123.54  E-value: 9.30e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRA---AEQEAqLLSQLKHPNIVTYKESWEGGDGLlYIVMGFC 86
Cdd:cd05603    1 KVIGKGSFGKVLLAKRKCDGKFYAVKVLQKKTILKKKEQNhimAERNV-LLKNLKHPFLVGLHYSFQTSEKL-YFVLDYV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  87 EGGDLYRKLKEQKGQLLPENQVveWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTL 166
Cdd:cd05603   79 NGGELFFHLQRERCFLEPRARF--YAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEGMEPEETTSTF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 167 IGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLpPMPRDYSPELAELIRTMLSKRP 246
Cdd:cd05603  157 CGTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILHKPL-HLPGGKTVAACDLLQGLLHKDQ 235

                 ...
gi 148839316 247 EER 249
Cdd:cd05603  236 RRR 238
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
4-261 1.10e-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: 121.49  E-value: 1.10e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   4 AAYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRnasSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLlYIVM 83
Cdd:cd14087    1 AKYDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIETK---CRGREVCESELNVLRRVRHTNIIQLIEVFETKERV-YMVM 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  84 GFCEGGDLYRKLKeQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNI---IKVGDLGIA--RVLEN 158
Cdd:cd14087   77 ELATGGELFDRII-AKGSF-TERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPdskIMITDFGLAstRKKGP 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 159 HCDMASTlIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMP---RDYSPELA 235
Cdd:cd14087  155 NCLMKTT-CGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSYSGepwPSVSNLAK 233
                        250       260
                 ....*....|....*....|....*.
gi 148839316 236 ELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd14087  234 DFIDRLLTVNPGERLSATQALKHPWI 259
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
10-261 1.21e-30

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: 121.64  E-value: 1.21e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLNlRNASSRE--RRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLYIVMGFCE 87
Cdd:cd14163    6 KTIGEGTYSKVKEAFSKKHQRKVAIKIID-KSGGPEEfiQRFLPRELQIVERLDHKNIIHVYEMLESADGKIYLVMELAE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  88 GGDLYRKLKEqkGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNiIKVGDLGIARVL-ENHCDMASTL 166
Cdd:cd14163   85 DGDVFDCVLH--GGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGFT-LKLTDFGFAKQLpKGGRELSQTF 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 167 IGTPYYMSPELFSNKPYNY-KSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPRDYSPELAELIRTMLSKR 245
Cdd:cd14163  162 CGSTAYAAPEVLQGVPHDSrKGDIWSMGVVLYVMLCAQLPFDDTDIPKMLCQQQKGVSLPGHLGVSRTCQDLLKRLLEPD 241
                        250
                 ....*....|....*.
gi 148839316 246 PEERPSVRSILRQPYI 261
Cdd:cd14163  242 MVLRPSIEEVSWHPWL 257
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
9-268 1.24e-30

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: 122.32  E-value: 1.24e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRE-RRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLyIVMGFCE 87
Cdd:cd05607    7 FRVLGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKSgEKMALLEKEILEKVNSPFIVSLAYAFETKTHLC-LVMSLMN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  88 GGDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTlI 167
Cdd:cd05607   86 GGDLKYHIYNVGERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEVKEGKPITQR-A 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 168 GTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAF-NAK---DMNSLVYRIIEGKLPPMPRDYSPELAELIRTMLS 243
Cdd:cd05607  165 GTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFrDHKekvSKEELKRRTLEDEVKFEHQNFTEEAKDICRLFLA 244
                        250       260
                 ....*....|....*....|....*
gi 148839316 244 KRPEERPSVRSILRQPyikRQISFF 268
Cdd:cd05607  245 KKPENRLGSRTNDDDP---RKHEFF 266
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
12-261 1.55e-30

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: 121.70  E-value: 1.55e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLN----LRNASSRERRAAE-----------------QEAQLLSQLKHPNIVTYKE 70
Cdd:cd14118    2 IGKGSYGIVKLAYNEEDNTLYAMKILSkkklLKQAGFFRRPPPRrkpgalgkpldpldrvyREIAILKKLDHPNVVKLVE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  71 SWEG-GDGLLYIVMGFCEGGDLyrkLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGD 149
Cdd:cd14118   82 VLDDpNEDNLYMVFELVDKGAV---MEVPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIAD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 150 LGIARVLENHCDMASTLIGTPYYMSPELFSNKPYNYKS---DVWALGCCVYEMATLKHAFNAKDMNSLVYRII--EGKLP 224
Cdd:cd14118  159 FGVSNEFEGDDALLSSTAGTPAFMAPEALSESRKKFSGkalDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIKtdPVVFP 238
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 148839316 225 PMPrDYSPELAELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd14118  239 DDP-VVSEQLKDLILRMLDKNPSERITLPEIKEHPWV 274
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
12-263 1.57e-30

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: 122.05  E-value: 1.57e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRErrAAEQEAQLLSQLKHPNIVTYKESWEGGDGLlYIVMGFCEGGDL 91
Cdd:cd06657   28 IGEGSTGIVCIATVKSSGKLVAVKKMDLRKQQRRE--LLFNEVVIMRDYQHENVVEMYNSYLVGDEL-WVVMEFLEGGAL 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  92 YRKLKEQKgqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTLIGTPY 171
Cdd:cd06657  105 TDIVTHTR---MNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPY 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 172 YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLvyRIIEGKLPPMPRD---YSPELAELIRTMLSKRPE 247
Cdd:cd06657  182 WMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPyFNEPPLKAM--KMIRDNLPPKLKNlhkVSPSLKGFLDRLLVRDPA 259
                        250
                 ....*....|....*.
gi 148839316 248 ERPSVRSILRQPYIKR 263
Cdd:cd06657  260 QRATAAELLKHPFLAK 275
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
10-258 1.59e-30

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: 121.62  E-value: 1.59e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASsrERRAAEQEAQLLSQLK-HPNIVTYKES---------WEggdglL 79
Cdd:cd14037    9 KYLAEGGFAHVYLVKTSNGGNRAALKRVYVNDEH--DLNVCKREIEIMKRLSgHKNIVGYIDSsanrsgngvYE-----V 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  80 YIVMGFCEGGDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKH--ILHRDLKTQNVFLTRTNIIKVGDLGIA---- 153
Cdd:cd14037   82 LLLMEYCKGGGVIDLMNQRLQTGLTESEILKIFCDVCEAVAAMHYLKppLIHRDLKVENVLISDSGNYKLCDFGSAttki 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 154 RVLENHCDMAS--------TligTPYYMSPE---LFSNKPYNYKSDVWALGCCVYEMATLKHAFNakdmNSLVYRIIEGK 222
Cdd:cd14037  162 LPPQTKQGVTYveedikkyT---TLQYRAPEmidLYRGKPITEKSDIWALGCLLYKLCFYTTPFE----ESGQLAILNGN 234
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 148839316 223 --LPPMPRdYSPELAELIRTMLSKRPEERPSVRSILRQ 258
Cdd:cd14037  235 ftFPDNSR-YSKRLHKLIRYMLEEDPEKRPNIYQVSYE 271
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
10-249 1.80e-30

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: 122.85  E-value: 1.80e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAE-QEAQLLSQLKHPNIVTYKESWEGGDgLLYIVMGFCEG 88
Cdd:cd05571    1 KVLGKGTFGKVILCREKATGELYAIKILKKEVIIAKDEVAHTlTENRVLQNTRHPFLTSLKYSFQTND-RLCFVMEYVNG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  89 GDLYRKLKEQKgqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTLIG 168
Cdd:cd05571   80 GELFFHLSRER--VFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCKEEISYGATTKTFCG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 169 TPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLpPMPRDYSPELAELIRTMLSKRPEE 248
Cdd:cd05571  158 TPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEV-RFPSTLSPEAKSLLAGLLKKDPKK 236

                 .
gi 148839316 249 R 249
Cdd:cd05571  237 R 237
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
9-249 2.52e-30

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: 121.53  E-value: 2.52e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRE-RRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLyIVMGFCE 87
Cdd:cd05608    6 FRVLGKGGFGEVSACQMRATGKLYACKKLNKKRLKKRKgYEGAMVEKRILAKVHSRFIVSLAYAFQTKTDLC-LVMTIMN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  88 GGDL----YRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMA 163
Cdd:cd05608   85 GGDLryhiYNVDEENPG--FQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVELKDGQTKT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 164 STLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAK----DMNSLVYRIIEGKLpPMPRDYSPELAELIR 239
Cdd:cd05608  163 KGYAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFRARgekvENKELKQRILNDSV-TYSEKFSPASKSICE 241
                        250
                 ....*....|
gi 148839316 240 TMLSKRPEER 249
Cdd:cd05608  242 ALLAKDPEKR 251
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
6-262 2.86e-30

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: 122.25  E-value: 2.86e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLN------------LRnassrerraaeqEAQLLSQLKHPNIV------T 67
Cdd:cd07834    2 YELLKPIGSGAYGVVCSAYDKRTGRKVAIKKISnvfddlidakriLR------------EIKILRHLKHENIIglldilR 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  68 YKESWEGGDglLYIVMGFCEGgDLYRKLKeQKGQLLPENqvVEWFV-QIAMALQYLHEKHILHRDLKTQNVFLTRTNIIK 146
Cdd:cd07834   70 PPSPEEFND--VYIVTELMET-DLHKVIK-SPQPLTDDH--IQYFLyQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLK 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 147 VGDLGIARVLENHcDMASTLIG---TPYYMSPEL-FSNKPYNYKSDVWALGCCVYEMATLKHAFNAKD---MNSLVYRII 219
Cdd:cd07834  144 ICDFGLARGVDPD-EDKGFLTEyvvTRWYRAPELlLSSKKYTKAIDIWSVGCIFAELLTRKPLFPGRDyidQLNLIVEVL 222
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148839316 220 eGK--------------------LPPMPR--------DYSPELAELIRTMLSKRPEERPSVRSILRQPYIK 262
Cdd:cd07834  223 -GTpseedlkfissekarnylksLPKKPKkplsevfpGASPEAIDLLEKMLVFNPKKRITADEALAHPYLA 292
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
12-260 2.97e-30

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: 121.23  E-value: 2.97e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLK---HPNIVTYKESWEGGDG----LLYIVMG 84
Cdd:cd07838    7 IGEGAYGTVYKARDLQDGRFVALKKVRVPLSEEGIPLSTIREIALLKQLEsfeHPNVVRLLDVCHGPRTdrelKLTLVFE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGgDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHcdMAS 164
Cdd:cd07838   87 HVDQ-DLATYLDKCPKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFGLARIYSFE--MAL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 TLI-GTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAF---NAKDMNSLVYRIIeGK------------------ 222
Cdd:cd07838  164 TSVvVTLWYRAPEVLLQSSYATPVDMWSVGCIFAELFNRRPLFrgsSEADQLGKIFDVI-GLpseeewprnsalprssfp 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 148839316 223 --LPPMPRDYSPEL----AELIRTMLSKRPEERPSVRSILRQPY 260
Cdd:cd07838  243 syTPRPFKSFVPEIdeegLDLLKKMLTFNPHKRISAFEALQHPY 286
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
8-271 3.28e-30

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: 120.87  E-value: 3.28e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   8 YLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRA-AEQEAQLLSQLKHPNIVTYKESWEGGDGLLyIVMGFC 86
Cdd:cd05631    4 HYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAmALNEKRILEKVNSRFVVSLAYAYETKDALC-LVLTIM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  87 EGGDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIA-RVLENhcDMAST 165
Cdd:cd05631   83 NGGDLKFHIYNMGNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAvQIPEG--ETVRG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNaKDMNSLVYRIIEGKLPPMPRDYSPELAE----LIRTM 241
Cdd:cd05631  161 RVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFR-KRKERVKREEVDRRVKEDQEEYSEKFSEdaksICRML 239
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 148839316 242 LSKRPEERPSVR----SILRQPYIKRQISF-FLEA 271
Cdd:cd05631  240 LTKNPKERLGCRgngaAGVKQHPIFKNINFkRLEA 274
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
11-260 3.64e-30

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: 3.64e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  11 VVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERrAAEQEAQLLSQLKHPNIVTYKESWEGGdGLLYIVMGFCEGGD 90
Cdd:cd14083   10 VLGTGAFSEVVLAEDKATGKLVAIKCIDKKALKGKED-SLENEIAVLRKIKHPNIVQLLDIYESK-SHLYLVMELVTGGE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  91 LYRKLKEqKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRT---NIIKVGDLGIARVLENhcDMASTLI 167
Cdd:cd14083   88 LFDRIVE-KGSY-TEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYYSPdedSKIMISDFGLSKMEDS--GVMSTAC 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 168 GTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKL---PPMPRDYSPELAELIRTMLSK 244
Cdd:cd14083  164 GTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILKAEYefdSPYWDDISDSAKDFIRHLMEK 243
                        250
                 ....*....|....*.
gi 148839316 245 RPEERPSVRSILRQPY 260
Cdd:cd14083  244 DPNKRYTCEQALEHPW 259
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
12-256 4.25e-30

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: 119.81  E-value: 4.25e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGevTLVKHRRDGkQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTY-----KESweggdglLYIVMGFC 86
Cdd:cd14062    1 IGSGSFG--TVYKGRWHG-DVAVKKLNVTDPTPSQLQAFKNEVAVLRKTRHVNILLFmgymtKPQ-------LAIVTQWC 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  87 EGGDLYRKLK--EQKGQLLpenQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARV--LENHCDM 162
Cdd:cd14062   71 EGSSLYKHLHvlETKFEML---QLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLATVktRWSGSQQ 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 163 ASTLIGTPYYMSPELFSNK---PYNYKSDVWALGCCVYEMATLK---HAFNAKDMnsLVYRIIEGKLPP----MPRDYSP 232
Cdd:cd14062  148 FEQPTGSILWMAPEVIRMQdenPYSFQSDVYAFGIVLYELLTGQlpySHINNRDQ--ILFMVGRGYLRPdlskVRSDTPK 225
                        250       260
                 ....*....|....*....|....
gi 148839316 233 ELAELIRTMLSKRPEERPSVRSIL 256
Cdd:cd14062  226 ALRRLMEDCIKFQRDERPLFPQIL 249
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
8-249 4.30e-30

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: 122.45  E-value: 4.30e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   8 YLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAE-QEAQLLSQLKHPNIVTYKESWEGGDGLLYiVMGFC 86
Cdd:cd05594   29 YLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTlTENRVLQNSRHPFLTALKYSFQTHDRLCF-VMEYA 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  87 EGGDLYRKLKEQKgqLLPENQVVEWFVQIAMALQYLH-EKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMAST 165
Cdd:cd05594  108 NGGELFFHLSRER--VFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKT 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLpPMPRDYSPELAELIRTMLSKR 245
Cdd:cd05594  186 FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEI-RFPRTLSPEAKSLLSGLLKKD 264

                 ....
gi 148839316 246 PEER 249
Cdd:cd05594  265 PKQR 268
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
3-249 5.04e-30

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: 122.03  E-value: 5.04e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   3 LAAYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNA-SSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLYI 81
Cdd:cd05615    9 LTDFNFLMVLGKGSFGKVMLAERKGSDELYAIKILKKDVViQDDDVECTMVEKRVLALQDKPPFLTQLHSCFQTVDRLYF 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  82 VMGFCEGGDLYRKLkEQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARvlENHCD 161
Cdd:cd05615   89 VMEYVNGGDLMYHI-QQVGKF-KEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCK--EHMVE 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 162 MAST--LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLpPMPRDYSPELAELIR 239
Cdd:cd05615  165 GVTTrtFCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNV-SYPKSLSKEAVSICK 243
                        250
                 ....*....|
gi 148839316 240 TMLSKRPEER 249
Cdd:cd05615  244 GLMTKHPAKR 253
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
9-261 6.27e-30

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: 120.12  E-value: 6.27e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRErraAEQEAQLLSQLK-HPNIVT-----YKESWEGGDGLlYIV 82
Cdd:cd06638   23 IETIGKGTYGKVFKVLNKKNGSKAAVKILDPIHDIDEE---IEAEYNILKALSdHPNVVKfygmyYKKDVKNGDQL-WLV 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  83 MGFCEGGDLYRKLKE--QKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHC 160
Cdd:cd06638   99 LELCNGGSVTDLVKGflKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTR 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 161 DMASTLIGTPYYMSPELFS-----NKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPM--PRDYSPE 233
Cdd:cd06638  179 LRRNTSVGTPFWMAPEVIAceqqlDSTYDARCDVWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPTLhqPELWSNE 258
                        250       260
                 ....*....|....*....|....*...
gi 148839316 234 LAELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd06638  259 FNDFIRKCLTKDYEKRPTVSDLLQHVFI 286
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
6-262 1.02e-29

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: 121.25  E-value: 1.02e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIV------TYKESWEGGDGLl 79
Cdd:cd07851   17 YQNLSPVGSGAYGQVCSAFDTKTGRKVAIKKLSRPFQSAIHAKRTYRELRLLKHMKHENVIglldvfTPASSLEDFQDV- 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  80 YIVMGFCeGGDLYRKLKEQKgqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARvlenH 159
Cdd:cd07851   96 YLVTHLM-GADLNNIVKCQK---LSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLAR----H 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 160 CDMAST-LIGTPYYMSPELFSNK-PYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIE----------------- 220
Cdd:cd07851  168 TDDEMTgYVATRWYRAPEIMLNWmHYNQTVDIWSVGCIMAELLTGKTLFPGSDHIDQLKRIMNlvgtpdeellkkisses 247
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 148839316 221 -----GKLPPMPRD--------YSPELAELIRTMLSKRPEERPSVRSILRQPYIK 262
Cdd:cd07851  248 arnyiQSLPQMPKKdfkevfsgANPLAIDLLEKMLVLDPDKRITAAEALAHPYLA 302
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
6-260 1.04e-29

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: 119.74  E-value: 1.04e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLK-HPNIVTYKESWEGGDGLlYIVMG 84
Cdd:cd07832    2 YKILGRIGEGAHGIVFKAKDRETGETVALKKVALRKLEGGIPNQALREIKALQACQgHPYVVKLRDVFPHGTGF-VLVFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCeGGDLYRKLKEQKgQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMA- 163
Cdd:cd07832   81 YM-LSSLSEVLRDEE-RPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLARLFSEEDPRLy 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 164 STLIGTPYYMSPELFSNKP-YNYKSDVWALGCCVYEMATLKHAFNAK-DMNSL--VYRII----------------EGKL 223
Cdd:cd07832  159 SHQVATRWYRAPELLYGSRkYDEGVDLWAVGCIFAELLNGSPLFPGEnDIEQLaiVLRTLgtpnektwpeltslpdYNKI 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 148839316 224 --PPMPR--------DYSPELAELIRTMLSKRPEERPSVRSILRQPY 260
Cdd:cd07832  239 tfPESKGirleeifpDCSPEAIDLLKGLLVYNPKKRLSAEEALRHPY 285
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
12-261 1.04e-29

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: 119.26  E-value: 1.04e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRnassreRRAAEQEAQLLSQL-------KHPNIVTYKESWEGgDGLLYIVMG 84
Cdd:cd14198   16 LGRGKFAVVRQCISKSTGQEYAAKFLKKR------RRGQDCRAEILHEIavlelakSNPRVVNLHEVYET-TSEIILILE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGGDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNI---IKVGDLGIARVLENHCD 161
Cdd:cd14198   89 YAAGGEIFNLCVPDLAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYPlgdIKIVDFGMSRKIGHACE 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 162 MaSTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLppmprDYSPE-------L 234
Cdd:cd14198  169 L-REIMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNISQVNV-----DYSEEtfssvsqL 242
                        250       260
                 ....*....|....*....|....*...
gi 148839316 235 A-ELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd14198  243 AtDFIQKLLVKNPEKRPTAEICLSHSWL 270
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
2-261 1.35e-29

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: 119.00  E-value: 1.35e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   2 PLAAYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSrERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLlYI 81
Cdd:cd06640    2 PEELFTKLERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEEAED-EIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKL-WI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  82 VMGFCEGGDLYRKLKEQKgqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCD 161
Cdd:cd06640   80 IMEYLGGGSALDLLRAGP---FDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 162 MASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMAtlKHAFNAKDMNSL--VYRIIEGKLPPMPRDYSPELAELIR 239
Cdd:cd06640  157 KRNTFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELA--KGEPPNSDMHPMrvLFLIPKNNPPTLVGDFSKPFKEFID 234
                        250       260
                 ....*....|....*....|..
gi 148839316 240 TMLSKRPEERPSVRSILRQPYI 261
Cdd:cd06640  235 ACLNKDPSFRPTAKELLKHKFI 256
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
11-258 1.53e-29

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: 118.60  E-value: 1.53e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  11 VVGKGSYGEVTLVKHRrdGKQYVIKKLnlRNASSRERRAA----EQEAQLLSQLKHPNIVTYKeswegGDGL----LYIV 82
Cdd:cd14146    1 IIGVGGFGKVYRATWK--GQEVAVKAA--RQDPDEDIKATaesvRQEAKLFSMLRHPNIIKLE-----GVCLeepnLCLV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  83 MGFCEGGDLYRKL-------KEQKGQLLPENQVVEWFVQIAMALQYLHEKH---ILHRDLKTQNVFLTR--------TNI 144
Cdd:cd14146   72 MEFARGGTLNRALaaanaapGPRRARRIPPHILVNWAVQIARGMLYLHEEAvvpILHRDLKSSNILLLEkiehddicNKT 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 145 IKVGDLGIARvlENHCDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLP 224
Cdd:cd14146  152 LKITDFGLAR--EWHRTTKMSAAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYRGIDGLAVAYGVAVNKLT 229
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 148839316 225 -PMPRDYSPELAELIRTMLSKRPEERPSVRSILRQ 258
Cdd:cd14146  230 lPIPSTCPEPFAKLMKECWEQDPHIRPSFALILEQ 264
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
5-260 1.65e-29

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: 118.96  E-value: 1.65e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   5 AYCYLRVVGKGSYGEV----TLVKHRrdgkqYVIKKLNLRNASSRE------RRAAEQEAQLLSQLKHPNIVTYKESWEG 74
Cdd:cd13990    1 RYLLLNLLGKGGFSEVykafDLVEQR-----YVACKIHQLNKDWSEekkqnyIKHALREYEIHKSLDHPRIVKLYDVFEI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  75 GDGLLYIVMGFCEGGDLYRKLKEQKgqLLPENQVVEWFVQIAMALQYLHEKH--ILHRDLKTQNVFLTRTNI---IKVGD 149
Cdd:cd13990   76 DTDSFCTVLEYCDGNDLDFYLKQHK--SIPEREARSIIMQVVSALKYLNEIKppIIHYDLKPGNILLHSGNVsgeIKITD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 150 LGIARVLENHCDMASTLI------GTPYYMSPELFSNKP----YNYKSDVWALGCCVYEMATLKHAFnAKDMNS---LVY 216
Cdd:cd13990  154 FGLSKIMDDESYNSDGMEltsqgaGTYWYLPPECFVVGKtppkISSKVDVWSVGVIFYQMLYGRKPF-GHNQSQeaiLEE 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 148839316 217 RII----EGKLPPMPRdYSPELAELIRTMLSKRPEERPSVRSILRQPY 260
Cdd:cd13990  233 NTIlkatEVEFPSKPV-VSSEAKDFIRRCLTYRKEDRPDVLQLANDPY 279
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
6-249 1.79e-29

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: 120.10  E-value: 1.79e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNA-SSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLYIVMG 84
Cdd:cd05616    2 FNFLMVLGKGSFGKVMLAERKGTDELYAVKILKKDVViQDDDVECTMVEKRVLALSGKPPFLTQLHSCFQTMDRLYFVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGGDLYRKLkEQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARvlENHCD--M 162
Cdd:cd05616   82 YVNGGDLMYHI-QQVGRF-KEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCK--ENIWDgvT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 163 ASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLpPMPRDYSPELAELIRTML 242
Cdd:cd05616  158 TKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNV-AYPKSMSKEAVAICKGLM 236

                 ....*..
gi 148839316 243 SKRPEER 249
Cdd:cd05616  237 TKHPGKR 243
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
13-260 2.04e-29

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: 117.75  E-value: 2.04e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  13 GKGSYGEVTLVKHRRDGKQYVIKKLN---LRNASSRERraAEQEAQLLSQLKHPNIVTYKESWEGGDGLlYIVMGFCEGG 89
Cdd:cd14079   11 GVGSFGKVKLAEHELTGHKVAVKILNrqkIKSLDMEEK--IRREIQILKLFRHPHIIRLYEVIETPTDI-FMVMEYVSGG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  90 DLYRKLKeQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHcDMASTLIGT 169
Cdd:cd14079   88 ELFDYIV-QKGRL-SEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLSNIMRDG-EFLKTSCGS 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 170 PYYMSPELFSNKPY-NYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLpPMPRDYSPELAELIRTMLSKRPEE 248
Cdd:cd14079  165 PNYAAPEVISGKLYaGPEVDVWSCGVILYALLCGSLPFDDEHIPNLFKKIKSGIY-TIPSHLSPGARDLIKRMLVVDPLK 243
                        250
                 ....*....|..
gi 148839316 249 RPSVRSILRQPY 260
Cdd:cd14079  244 RITIPEIRQHPW 255
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
12-261 2.49e-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: 117.48  E-value: 2.49e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIK---KLNLRNASSRERRaaeqEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGFCEG 88
Cdd:cd14078   11 IGSGGFAKVKLATHILTGEKVAIKimdKKALGDDLPRVKT----EIEALKNLSHQHICRLYHVIET-DNKIFMVLEYCPG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  89 GDLYRKLKEQkgQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMA-STLI 167
Cdd:cd14078   86 GELFDYIVAK--DRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCAKPKGGMDHHlETCC 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 168 GTPYYMSPELFSNKPY-NYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLpPMPRDYSPELAELIRTMLSKRP 246
Cdd:cd14078  164 GSPAYAAPELIQGKPYiGSEADVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSGKY-EEPEWLSPSSKLLLDQMLQVDP 242
                        250
                 ....*....|....*
gi 148839316 247 EERPSVRSILRQPYI 261
Cdd:cd14078  243 KKRITVKELLNHPWV 257
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
13-256 3.12e-29

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: 116.98  E-value: 3.12e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  13 GKGSYGEVTLVKHRRDGKQYVIKKLNlrnassrerrAAEQEAQLLSQLKHPNIVT-YKESWEG-GDGllyIVMGFCEGGD 90
Cdd:cd14060    2 GGGSFGSVYRAIWVSQDKEVAVKKLL----------KIEKEAEILSVLSHRNIIQfYGAILEApNYG---IVTEYASYGS 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  91 LYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEK---HILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMasTLI 167
Cdd:cd14060   69 LFDYLNSNESEEMDMDQIMTWATDIAKGMHYLHMEapvKVIHRDLKSRNVVIAADGVLKICDFGASRFHSHTTHM--SLV 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 168 GTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIE-GKLPPMPRDYSPELAELIRTMLSKRP 246
Cdd:cd14060  147 GTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPFKGLEGLQVAWLVVEkNERPTIPSSCPRSFAELMRRCWEADV 226
                        250
                 ....*....|
gi 148839316 247 EERPSVRSIL 256
Cdd:cd14060  227 KERPSFKQII 236
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
9-263 3.61e-29

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 119.93  E-value: 3.61e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLnLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGdGLLYIVMGFCEG 88
Cdd:PLN00034  79 VNRIGSGAGGTVYKVIHRPTGRLYALKVI-YGNHEDTVRRQICREIEILRDVNHPNVVKCHDMFDHN-GEIQVLLEFMDG 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  89 GDLyrklkeQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTLIG 168
Cdd:PLN00034 157 GSL------EGTHIADEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRILAQTMDPCNSSVG 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 169 TPYYMSPE-----LFSNKPYNYKSDVWALGCCVYEMATLKHAF---NAKDMNSLVYRIIEGKLPPMPRDYSPELAELIRT 240
Cdd:PLN00034 231 TIAYMSPErintdLNHGAYDGYAGDIWSLGVSILEFYLGRFPFgvgRQGDWASLMCAICMSQPPEAPATASREFRHFISC 310
                        250       260
                 ....*....|....*....|...
gi 148839316 241 MLSKRPEERPSVRSILRQPYIKR 263
Cdd:PLN00034 311 CLQREPAKRWSAMQLLQHPFILR 333
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
12-260 3.91e-29

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: 117.86  E-value: 3.91e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLlYIVMGFCEGGDL 91
Cdd:cd07847    9 IGEGSYGVVFKCRNRETGQIVAIKKFVESEDDPVIKKIALREIRMLKQLKHPNLVNLIEVFRRKRKL-HLVFEYCDHTVL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  92 YRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTLIGTPY 171
Cdd:cd07847   88 NELEKNPRG--VPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARILTGPGDDYTDYVATRW 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 172 YMSPELF-SNKPYNYKSDVWALGCCVYEMATLKHAFNAK-DMNSLvYRIIE--GKLPP----------------MP---- 227
Cdd:cd07847  166 YRAPELLvGDTQYGPPVDVWAIGCVFAELLTGQPLWPGKsDVDQL-YLIRKtlGDLIPrhqqifstnqffkglsIPepet 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 148839316 228 --------RDYSPELAELIRTMLSKRPEERPSVRSILRQPY 260
Cdd:cd07847  245 repleskfPNISSPALSFLKGCLQMDPTERLSCEELLEHPY 285
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
10-249 4.00e-29

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: 118.64  E-value: 4.00e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLN----LRN----ASSRERRAaeqeaqLLSQLKHPNIVTYKESWEgGDGLLYI 81
Cdd:cd05592    1 KVLGKGSFGKVMLAELKGTNQYFAIKALKkdvvLEDddveCTMIERRV------LALASQHPFLTHLFCTFQ-TESHLFF 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  82 VMGFCEGGDLYRKLkEQKGQlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARvlENHCD 161
Cdd:cd05592   74 VMEYLNGGDLMFHI-QQSGR-FDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCK--ENIYG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 162 --MASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKlPPMPRDYSPELAELIR 239
Cdd:cd05592  150 enKASTFCGTPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICNDT-PHYPRWLTKEAASCLS 228
                        250
                 ....*....|
gi 148839316 240 TMLSKRPEER 249
Cdd:cd05592  229 LLLERNPEKR 238
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
36-272 4.97e-29

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: 117.10  E-value: 4.97e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  36 KLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEG---GDGLLYIVMGFCEGGDLYRKLKEQKgqLLPENQVVEWF 112
Cdd:cd14032   33 ELQDRKLTKVERQRFKEEAEMLKGLQHPNIVRFYDFWEScakGKRCIVLVTELMTSGTLKTYLKRFK--VMKPKVLRSWC 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 113 VQIAMALQYLHEKH--ILHRDLKTQNVFLT-RTNIIKVGDLGIARVleNHCDMASTLIGTPYYMSPELFSNKpYNYKSDV 189
Cdd:cd14032  111 RQILKGLLFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLATL--KRASFAKSVIGTPEFMAPEMYEEH-YDESVDV 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 190 WALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPP--MPRDYSPELAELIRTMLSKRPEERPSVRSILRQpyikrqiSF 267
Cdd:cd14032  188 YAFGMCMLEMATSEYPYSECQNAAQIYRKVTCGIKPasFEKVTDPEIKEIIGECICKNKEERYEIKDLLSH-------AF 260

                 ....*
gi 148839316 268 FLEAT 272
Cdd:cd14032  261 FAEDT 265
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
2-286 5.82e-29

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: 118.20  E-value: 5.82e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   2 PLAAYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRER-RAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLY 80
Cdd:cd06634   13 PEKLFSDLREIGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNEKwQDIIKEVKFLQKLRHPNTIEYRGCYLR-EHTAW 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  81 IVMGFCEGGDlyRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENhc 160
Cdd:cd06634   92 LVMEYCLGSA--SDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGSASIMAP-- 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 161 dmASTLIGTPYYMSPEL---FSNKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLvYRIIEGKLPPMPRD-YSPELA 235
Cdd:cd06634  168 --ANSFVGTPYWMAPEVilaMDEGQYDGKVDVWSLGITCIELAERKPPlFNMNAMSAL-YHIAQNESPALQSGhWSEYFR 244
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 148839316 236 ELIRTMLSKRPEERPSVRSILRQPYIKRQISFFLEATKIKTSKNNIKNGDS 286
Cdd:cd06634  245 NFVDSCLQKIPQDRPTSDVLLKHRFLLRERPPTVIMDLIQRTKDAVRELDN 295
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
9-249 5.86e-29

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: 118.26  E-value: 5.86e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLN---LRNASSRERRAAEQEAQLLSQlKHPNIVTYKESWEGGDgLLYIVMGF 85
Cdd:cd05587    1 LMVLGKGSFGKVMLAERKGTDELYAIKILKkdvIIQDDDVECTMVEKRVLALSG-KPPFLTQLHSCFQTMD-RLYFVMEY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGGDL-YRKLKEQKgqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMAS 164
Cdd:cd05587   79 VNGGDLmYHIQQVGK---FKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKEGIFGGKTTR 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 TLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKlPPMPRDYSPELAELIRTMLSK 244
Cdd:cd05587  156 TFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHN-VSYPKSLSKEAVSICKGLLTK 234

                 ....*
gi 148839316 245 RPEER 249
Cdd:cd05587  235 HPAKR 239
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
2-283 6.30e-29

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: 117.52  E-value: 6.30e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   2 PLAAYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRErrAAEQEAQLLSQLKHPNIVTYKESWEGGDGLlYI 81
Cdd:cd06656   17 PKKKYTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKE--LIINEILVMRENKNPNIVNYLDSYLVGDEL-WV 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  82 VMGFCEGGDLYRKLKEQkgqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCD 161
Cdd:cd06656   94 VMEYLAGGSLTDVVTET---CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQS 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 162 MASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPM--PRDYSPELAELIR 239
Cdd:cd06656  171 KRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELqnPERLSAVFRDFLN 250
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 148839316 240 TMLSKRPEERPSVRSILRQPYIKRQISFFLEATKIKTSKNNIKN 283
Cdd:cd06656  251 RCLEMDVDRRGSAKELLQHPFLKLAKPLSSLTPLIIAAKEAIKN 294
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
7-251 6.59e-29

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: 116.71  E-value: 6.59e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   7 CYLRVVGKGSYGEVTLVKHRrdGKQYVIKKLNLRNASSRERRAAEQEAQLLSqLKHPNIVTY--KESWEGGDGLLYIVMG 84
Cdd:cd13979    6 RLQEPLGSGGFGSVYKATYK--GETVAVKIVRRRRKNRASRQSFWAELNAAR-LRHENIVRVlaAETGTDFASLGLIIME 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGGDLYRKLKEQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDM-- 162
Cdd:cd13979   83 YCGNGTLQQLIYEGSEPL-PLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSVKLGEGNEVgt 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 163 -ASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFnAKDMNSLVYRIIEGKL-PPMPRDYSPELAE---- 236
Cdd:cd13979  162 pRSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPY-AGLRQHVLYAVVAKDLrPDLSGLEDSEFGQrlrs 240
                        250
                 ....*....|....*
gi 148839316 237 LIRTMLSKRPEERPS 251
Cdd:cd13979  241 LISRCWSAQPAERPN 255
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
11-258 6.83e-29

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: 116.68  E-value: 6.83e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  11 VVGKGSYG----------EVTLVKHRRDGKQYVIKKL-NLRnassrerraaeQEAQLLSQLKHPNIVTYKeswegGDGL- 78
Cdd:cd14145   13 IIGIGGFGkvyraiwigdEVAVKAARHDPDEDISQTIeNVR-----------QEAKLFAMLKHPNIIALR-----GVCLk 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  79 ---LYIVMGFCEGGDLYRKLKeqkGQLLPENQVVEWFVQIAMALQYLHEKHI---LHRDLKTQNVFLTR--------TNI 144
Cdd:cd14145   77 epnLCLVMEFARGGPLNRVLS---GKRIPPDILVNWAVQIARGMNYLHCEAIvpvIHRDLKSSNILILEkvengdlsNKI 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 145 IKVGDLGIARvlENHCDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLP 224
Cdd:cd14145  154 LKITDFGLAR--EWHRTTKMSAAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPFRGIDGLAVAYGVAMNKLS 231
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 148839316 225 -PMPRDYSPELAELIRTMLSKRPEERPSVRSILRQ 258
Cdd:cd14145  232 lPIPSTCPEPFARLMEDCWNPDPHSRPPFTNILDQ 266
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
10-261 7.01e-29

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: 116.21  E-value: 7.01e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIK---KLNLRNASSRERRAAEQEAQllSQLKHPNIVTYKESWEGGdGLLYIVMGFC 86
Cdd:cd14116   11 RPLGKGKFGNVYLAREKQSKFILALKvlfKAQLEKAGVEHQLRREVEIQ--SHLRHPNILRLYGYFHDA-TRVYLILEYA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  87 EGGDLYRKLkeQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIArvLENHCDMASTL 166
Cdd:cd14116   88 PLGTVYREL--QKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWS--VHAPSSRRTTL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 167 IGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRI--IEGKLPPMprdYSPELAELIRTMLSK 244
Cdd:cd14116  164 CGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRIsrVEFTFPDF---VTEGARDLISRLLKH 240
                        250
                 ....*....|....*..
gi 148839316 245 RPEERPSVRSILRQPYI 261
Cdd:cd14116  241 NPSQRPMLREVLEHPWI 257
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
11-249 7.14e-29

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: 118.06  E-value: 7.14e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  11 VVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSR-ERRAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGFCEGG 89
Cdd:cd05585    1 VIGKGSFGKVMQVRKKDTSRIYALKTIRKAHIVSRsEVTHTLAERTVLAQVDCPFIVPLKFSFQS-PEKLYLVLAFINGG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  90 DLYRKLkeQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTLIGT 169
Cdd:cd05585   80 ELFHHL--QREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKLNMKDDDKTNTFCGT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 170 PYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLpPMPRDYSPELAELIRTMLSKRPEER 249
Cdd:cd05585  158 PEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPL-RFPDGFDRDAKDLLIGLLNRDPTKR 236
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
6-261 8.44e-29

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: 116.43  E-value: 8.44e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTL-----VKHRRDGKQYVIKkLNLRNASSRERRAA--EQEAQLLSQLKHPNIVTYkESWEGGDGL 78
Cdd:cd14076    3 YILGRTLGEGEFGKVKLgwplpKANHRSGVQVAIK-LIRRDTQQENCQTSkiMREINILKGLTHPNIVRL-LDVLKTKKY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  79 LYIVMGFCEGGDLY------RKLKEQKGQLLpenqvvewFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGI 152
Cdd:cd14076   81 IGIVLEFVSGGELFdyilarRRLKDSVACRL--------FAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 153 ARVL-ENHCDMASTLIGTPYYMSPELF-SNKPYN-YKSDVWALGCCVYEMATLKHAF-------NAKDMNSLvYRIIEGK 222
Cdd:cd14076  153 ANTFdHFNGDLMSTSCGSPCYAAPELVvSDSMYAgRKADIWSCGVILYAMLAGYLPFdddphnpNGDNVPRL-YRYICNT 231
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 148839316 223 LPPMPRDYSPELAELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd14076  232 PLIFPEYVTPKARDLLRRILVPNPRKRIRLSAIMRHAWL 270
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
12-264 8.52e-29

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: 117.07  E-value: 8.52e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEG---GDGLLYIVMGFCEG 88
Cdd:cd14030   33 IGRGSFKTVYKGLDTETTVEVAWCELQDRKLSKSERQRFKEEAGMLKGLQHPNIVRFYDSWEStvkGKKCIVLVTELMTS 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  89 GDLYRKLKEQKgqLLPENQVVEWFVQIAMALQYLHEKH--ILHRDLKTQNVFLT-RTNIIKVGDLGIARVleNHCDMAST 165
Cdd:cd14030  113 GTLKTYLKRFK--VMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLATL--KRASFAKS 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 LIGTPYYMSPELFSNKpYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPRDYS--PELAELIRTMLS 243
Cdd:cd14030  189 VIGTPEFMAPEMYEEK-YDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRRVTSGVKPASFDKVaiPEVKEIIEGCIR 267
                        250       260
                 ....*....|....*....|.
gi 148839316 244 KRPEERPSVRSILRQPYIKRQ 264
Cdd:cd14030  268 QNKDERYAIKDLLNHAFFQEE 288
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
8-261 8.80e-29

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: 117.46  E-value: 8.80e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   8 YLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERrAAEQEAQLLSQLKHPNIVTYKESWEGGDGLlYIVMGFCE 87
Cdd:cd14168   14 FKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKGKES-SIENEIAVLRKIKHENIVALEDIYESPNHL-YLVMQLVS 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  88 GGDLYRKLKEqKGqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFL---TRTNIIKVGDLGIARvLENHCDMAS 164
Cdd:cd14168   92 GGELFDRIVE-KG-FYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYfsqDEESKIMISDFGLSK-MEGKGDVMS 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 TLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKL---PPMPRDYSPELAELIRTM 241
Cdd:cd14168  169 TACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKADYefdSPYWDDISDSAKDFIRNL 248
                        250       260
                 ....*....|....*....|
gi 148839316 242 LSKRPEERPSVRSILRQPYI 261
Cdd:cd14168  249 MEKDPNKRYTCEQALRHPWI 268
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
3-249 1.10e-28

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: 118.60  E-value: 1.10e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   3 LAAYCYLRVVGKGSYGEVTLVKHRRDGKQYVIK--KLNLRNaSSRERRAAEQEAQLLSQLK-HPNIVTYKESWEGgDGLL 79
Cdd:cd05618   19 LQDFDLLRVIGRGSYAKVLLVRLKKTERIYAMKvvKKELVN-DDEDIDWVQTEKHVFEQASnHPFLVGLHSCFQT-ESRL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  80 YIVMGFCEGGDLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENH 159
Cdd:cd05618   97 FFVIEYVNGGDLMFHMQRQRK--LPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRP 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 160 CDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNA--------KDMNSLVYRIIEGKLPPMPRDYS 231
Cdd:cd05618  175 GDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDIvgssdnpdQNTEDYLFQVILEKQIRIPRSLS 254
                        250
                 ....*....|....*...
gi 148839316 232 PELAELIRTMLSKRPEER 249
Cdd:cd05618  255 VKAASVLKSFLNKDPKER 272
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
2-261 1.14e-28

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: 115.90  E-value: 1.14e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   2 PLAAYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASsrERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLlYI 81
Cdd:cd06646    7 PQHDYELIQRVGSGTYGDVYKARNLHTGELAAVKIIKLEPGD--DFSLIQQEIFMVKECKHCNIVAYFGSYLSREKL-WI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  82 VMGFCEGGDLyRKLKEQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCD 161
Cdd:cd06646   84 CMEYCGGGSL-QDIYHVTGPL-SELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAAKITATIA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 162 MASTLIGTPYYMSPELFS---NKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLVYRIIEGKLPPMPRD---YSPEL 234
Cdd:cd06646  162 KRKSFIGTPYWMAPEVAAvekNGGYNQLCDIWAVGITAIELAELQPPmFDLHPMRALFLMSKSNFQPPKLKDktkWSSTF 241
                        250       260
                 ....*....|....*....|....*..
gi 148839316 235 AELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd06646  242 HNFVKISLTKNPKKRPTAERLLTHLFV 268
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
2-209 1.18e-28

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: 117.08  E-value: 1.18e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   2 PLAAYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGgDGL--L 79
Cdd:cd07845    5 SVTEFEKLNRIGEGTYGIVYRARDTTSGEIVALKKVRMDNERDGIPISSLREITLLLNLRHPNIVELKEVVVG-KHLdsI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  80 YIVMGFCEGgDLYRKLKEQKgQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENH 159
Cdd:cd07845   84 FLVMEYCEQ-DLASLLDNMP-TPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLARTYGLP 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 148839316 160 C-DMASTLIgTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAFNAK 209
Cdd:cd07845  162 AkPMTPKVV-TLWYRAPElLLGCTTYTTAIDMWAVGCILAELLAHKPLLPGK 212
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
10-260 1.19e-28

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPK-activated protein kinases MK2, MK3, MK5 (also called PRAK for p38-regulated/activated protein kinase), and related proteins. These proteins contain a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. In addition, MK2 and MK3 contain an N-terminal proline-rich region that can bind to SH3 domains. MK2 and MK3 are bonafide substrates for the MAPK p38, while MK5 plays a functional role in the p38 MAPK pathway although their direct interaction has been difficult to detect. MK2 and MK3 are closely related and show, thus far, indistinguishable substrate specificity, while MK5 shows a distinct spectrum of substrates. MK2 and MK3 are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 115.85  E-value: 1.19e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLnlrnassRERRAAEQEAQL---LSQlkHPNIVTYKESWE---GGDGLLYIVM 83
Cdd:cd14089    7 QVLGLGINGKVLECFHKKTGEKFALKVL-------RDNPKARREVELhwrASG--CPHIVRIIDVYEntyQGRKCLLVVM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  84 GFCEGGDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTN---IIKVGDLGIARVLENHC 160
Cdd:cd14089   78 ECMEGGELFSRIQERADSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGpnaILKLTDFGFAKETTTKK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 161 DMAsTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMA-------TLKHAFNAKDMNSlvyRIIEGKLP-PMP--RDY 230
Cdd:cd14089  158 SLQ-TPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLcgyppfySNHGLAISPGMKK---RIRNGQYEfPNPewSNV 233
                        250       260       270
                 ....*....|....*....|....*....|
gi 148839316 231 SPELAELIRTMLSKRPEERPSVRSILRQPY 260
Cdd:cd14089  234 SEEAKDLIRGLLKTDPSERLTIEEVMNHPW 263
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
6-262 1.20e-28

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: 116.90  E-value: 1.20e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRE---RRAAEQEAQLLSQLKHPNIVTYKESWeGGDGLLYIV 82
Cdd:cd07841    2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGERKEAKdgiNFTALREIKLLQELKHPNIIGLLDVF-GHKSNINLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  83 MGFCEGgDLyRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLEN-HCD 161
Cdd:cd07841   81 FEFMET-DL-EKVIKDKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLARSFGSpNRK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 162 MASTLIgTPYYMSPEL-FSNKPYNYKSDVWALGCCVYEMAT-------------LKHAFNA---------KDMNSLVYRI 218
Cdd:cd07841  159 MTHQVV-TRWYRAPELlFGARHYGVGVDMWSVGCIFAELLLrvpflpgdsdidqLGKIFEAlgtpteenwPGVTSLPDYV 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 148839316 219 IEGKLPPMPRDY-----SPELAELIRTMLSKRPEERPSVRSILRQPYIK 262
Cdd:cd07841  238 EFKPFPPTPLKQifpaaSDDALDLLQRLLTLNPNKRITARQALEHPYFS 286
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
11-249 1.27e-28

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: 115.95  E-value: 1.27e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  11 VVGKGSYGEVTLVKHR---RDGKQYVIKKLN----LRNASSRERRAAEQeaQLLSQLKH-PNIVTYKESWEGgDGLLYIV 82
Cdd:cd05583    1 VLGTGAYGKVFLVRKVgghDAGKLYAMKVLKkatiVQKAKTAEHTMTER--QVLEAVRQsPFLVTLHYAFQT-DAKLHLI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  83 MGFCEGGDLYRKLKeQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHC-D 161
Cdd:cd05583   78 LDYVNGGELFTHLY-QREHF-TESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKEFLPGEnD 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 162 MASTLIGTPYYMSPELFSNKP--YNYKSDVWALGCCVYEMATLKHAF---NAKDMNSLVYRIIEGKLPPMPRDYSPELAE 236
Cdd:cd05583  156 RAYSFCGTIEYMAPEVVRGGSdgHDKAVDWWSLGVLTYELLTGASPFtvdGERNSQSEISKRILKSHPPIPKTFSAEAKD 235
                        250
                 ....*....|...
gi 148839316 237 LIRTMLSKRPEER 249
Cdd:cd05583  236 FILKLLEKDPKKR 248
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
3-249 1.27e-28

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: 118.20  E-value: 1.27e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   3 LAAYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRER-RAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLYI 81
Cdd:cd05617   14 LQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDiDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  82 VMGFCEGGDLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCD 161
Cdd:cd05617   94 VIEYVNGGDLMFHMQRQRK--LPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGD 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 162 MASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNA----KDMNS--LVYRIIEGKLPPMPRDYSPELA 235
Cdd:cd05617  172 TTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIitdnPDMNTedYLFQVILEKPIRIPRFLSVKAS 251
                        250
                 ....*....|....
gi 148839316 236 ELIRTMLSKRPEER 249
Cdd:cd05617  252 HVLKGFLNKDPKER 265
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
2-263 1.35e-28

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: 115.91  E-value: 1.35e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   2 PLAAYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRnaSSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLlYI 81
Cdd:cd06645    9 PQEDFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLE--PGEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKL-WI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  82 VMGFCEGGDLyRKLKEQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCD 161
Cdd:cd06645   86 CMEFCGGGSL-QDIYHVTGPL-SESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITATIA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 162 MASTLIGTPYYMSPELFS---NKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLVYRIIEGKLPPMPRD---YSPEL 234
Cdd:cd06645  164 KRKSFIGTPYWMAPEVAAverKGGYNQLCDIWAVGITAIELAELQPPmFDLHPMRALFLMTKSNFQPPKLKDkmkWSNSF 243
                        250       260
                 ....*....|....*....|....*....
gi 148839316 235 AELIRTMLSKRPEERPSVRSILRQPYIKR 263
Cdd:cd06645  244 HHFVKMALTKNPKKRPTAEKLLQHPFVTQ 272
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
10-249 1.44e-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: 117.52  E-value: 1.44e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQY---VIKKlNLRNAS------SRERRAAEQEAQllsqlkHPNIVTYKESWEgGDGLLY 80
Cdd:cd05588    1 RVIGRGSYAKVLMVELKKTKRIYamkVIKK-ELVNDDedidwvQTEKHVFETASN------HPFLVGLHSCFQ-TESRLF 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  81 IVMGFCEGGDLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHC 160
Cdd:cd05588   73 FVIEFVNGGDLMFHMQRQRR--LPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPG 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 161 DMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAF------NAKDMNS--LVYRIIEGKLPPMPRDYSP 232
Cdd:cd05588  151 DTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPFdivgssDNPDQNTedYLFQVILEKPIRIPRSLSV 230
                        250
                 ....*....|....*..
gi 148839316 233 ELAELIRTMLSKRPEER 249
Cdd:cd05588  231 KAASVLKGFLNKNPAER 247
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
4-261 3.31e-28

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: 114.99  E-value: 3.31e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   4 AAYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERrAAEQEAQLLSQLKHPNIVTYKESWEGGDGLlYIVM 83
Cdd:cd14169    3 SVYELKEKLGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKEA-MVENEIAVLRRINHENIVSLEDIYESPTHL-YLAM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  84 GFCEGGDLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLT---RTNIIKVGDLGIARVLENhc 160
Cdd:cd14169   81 ELVTGGELFDRIIERGS--YTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYAtpfEDSKIMISDFGLSKIEAQ-- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 161 DMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKL---PPMPRDYSPELAEL 237
Cdd:cd14169  157 GMLSTACGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILKAEYefdSPYWDDISESAKDF 236
                        250       260
                 ....*....|....*....|....
gi 148839316 238 IRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd14169  237 IRHLLERDPEKRFTCEQALQHPWI 260
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
11-260 3.43e-28

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: 114.43  E-value: 3.43e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  11 VVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLlYIVMGFCEGGD 90
Cdd:cd14082   10 VLGSGQFGIVYGGKHRKTGRDVAIKVIDKLRFPTKQESQLRNEVAILQQLSHPGVVNLECMFETPERV-FVVMEKLHGDM 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  91 LYRKLKEQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTN---IIKVGDLGIARVLENHcDMASTLI 167
Cdd:cd14082   89 LEMILSSEKGRL-PERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEpfpQVKLCDFGFARIIGEK-SFRRSVV 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 168 GTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNA-KDMN------SLVYriiegklPPMP-RDYSPELAELIR 239
Cdd:cd14082  167 GTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEdEDINdqiqnaAFMY-------PPNPwKEISPDAIDLIN 239
                        250       260
                 ....*....|....*....|.
gi 148839316 240 TMLSKRPEERPSVRSILRQPY 260
Cdd:cd14082  240 NLLQVKMRKRYSVDKSLSHPW 260
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
2-262 4.23e-28

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: 115.21  E-value: 4.23e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   2 PLAAYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRErrAAEQEAQLLSQLKHPNIVTYKESWEGGDGLlYI 81
Cdd:cd06654   18 PKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKKE--LIINEILVMRENKNPNIVNYLDSYLVGDEL-WV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  82 VMGFCEGGDLYRKLKEQkgqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCD 161
Cdd:cd06654   95 VMEYLAGGSLTDVVTET---CMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQS 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 162 MASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPM--PRDYSPELAELIR 239
Cdd:cd06654  172 KRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELqnPEKLSAIFRDFLN 251
                        250       260
                 ....*....|....*....|...
gi 148839316 240 TMLSKRPEERPSVRSILRQPYIK 262
Cdd:cd06654  252 RCLEMDVEKRGSAKELLQHQFLK 274
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
12-261 4.84e-28

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: 114.35  E-value: 4.84e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAA----EQEAQLLSQLKHPNIVTYKESWEGGDGLLyIVMGFCE 87
Cdd:cd14194   13 LGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRRGVSrediEREVSILKEIQHPNVITLHEVYENKTDVI-LILELVA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  88 GGDLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNI----IKVGDLGIARVLENHCDMA 163
Cdd:cd14194   92 GGELFDFLAEKES--LTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVpkprIKIIDFGLAHKIDFGNEFK 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 164 StLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRI--IEGKLPPMPRDYSPELA-ELIRT 240
Cdd:cd14194  170 N-IFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVsaVNYEFEDEYFSNTSALAkDFIRR 248
                        250       260
                 ....*....|....*....|.
gi 148839316 241 MLSKRPEERPSVRSILRQPYI 261
Cdd:cd14194  249 LLVKDPKKRMTIQDSLQHPWI 269
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
2-261 5.08e-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: 113.76  E-value: 5.08e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   2 PLAAYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKklnLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLyI 81
Cdd:cd14111    1 PQKPYTFLDEKARGRFGVIRRCRENATGKNFPAK---IVPYQAEEKQGVLQEYEILKSLHHERIMALHEAYITPRYLV-L 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  82 VMGFCEGGDLYRKLKEQKgqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHC- 160
Cdd:cd14111   77 IAEFCSGKELLHSLIDRF--RYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSAQSFNPLSl 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 161 DMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPP--MPRDYSPELAELI 238
Cdd:cd14111  155 RQLGRRTGTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKILVAKFDAfkLYPNVSQSASLFL 234
                        250       260
                 ....*....|....*....|...
gi 148839316 239 RTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd14111  235 KKVLSSYPWSRPTTKDCFAHAWL 257
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
12-201 6.56e-28

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: 114.29  E-value: 6.56e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKK----LNLRNassRERRAAEqeAQLLSQLKHPNIVTYKESWEG-----GDGLLYIV 82
Cdd:cd14038    2 LGTGGFGNVLRWINQETGEQVAIKQcrqeLSPKN---RERWCLE--IQIMKRLNHPNVVAARDVPEGlqklaPNDLPLLA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  83 MGFCEGGDLYRKLKEQKGQL-LPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTN---IIKVGDLGIARVLEn 158
Cdd:cd14038   77 MEYCQGGDLRKYLNQFENCCgLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGEqrlIHKIIDLGYAKELD- 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 148839316 159 HCDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMAT 201
Cdd:cd14038  156 QGSLCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECIT 198
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
10-261 8.10e-28

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: 113.28  E-value: 8.10e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQY---VIKKLNLRNASsreRRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLlYIVMGFC 86
Cdd:cd14074    9 ETLGRGHFAVVKLARHVFTGEKVavkVIDKTKLDDVS---KAHLFQEVRCMKLVQHPNVVRLYEVIDTQTKL-YLILELG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  87 EGGDLYRK-LKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNV-FLTRTNIIKVGDLGIARVLENHcDMAS 164
Cdd:cd14074   85 DGGDMYDYiMKHENG--LNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVvFFEKQGLVKLTDFGFSNKFQPG-EKLE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 TLIGTPYYMSPELFSNKPYNY-KSDVWALGCCVYEMATLKHAFN-AKDMNSLVyRIIEGKLpPMPRDYSPELAELIRTML 242
Cdd:cd14074  162 TSCGSLAYSAPEILLGDEYDApAVDIWSLGVILYMLVCGQPPFQeANDSETLT-MIMDCKY-TVPAHVSPECKDLIRRML 239
                        250
                 ....*....|....*....
gi 148839316 243 SKRPEERPSVRSILRQPYI 261
Cdd:cd14074  240 IRDPKKRASLEEIENHPWL 258
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
9-249 1.02e-27

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: 114.64  E-value: 1.02e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRER-RAAEQEAQLLSQLKHPNIVTYKESWEGGDgLLYIVMGFCE 87
Cdd:cd05574    6 IKLLGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMIKRNKvKRVLTEREILATLDHPFLPTLYASFQTST-HLCFVMDYCP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  88 GGDLYRKLKEQKGQLLPEnQVVEWFV-QIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGD----------------- 149
Cdd:cd05574   85 GGELFRLLQKQPGKRLPE-EVARFYAaEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDfdlskqssvtpppvrks 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 150 -LGIARVLENHCDMASTLI-----------GTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYR 217
Cdd:cd05574  164 lRKGSRRSSVKSIEKETFVaepsarsnsfvGTEEYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTTPFKGSNRDETFSN 243
                        250       260       270
                 ....*....|....*....|....*....|....
gi 148839316 218 IIEGKL--PPMPRDySPELAELIRTMLSKRPEER 249
Cdd:cd05574  244 ILKKELtfPESPPV-SSEAKDLIRKLLVKDPSKR 276
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
6-262 1.18e-27

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: 114.77  E-value: 1.18e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKE----SWEGGDGL-LY 80
Cdd:cd07855    7 YEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIPNAFDVVTTAKRTLRELKILRHFKHDNIIAIRDilrpKVPYADFKdVY 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  81 IVMGFCEGgDLYRKLkeQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVL---- 156
Cdd:cd07855   87 VVLDLMES-DLHHII--HSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMARGLctsp 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 157 ENHCDMASTLIGTPYYMSPEL-FSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDM-----------------------N 212
Cdd:cd07855  164 EEHKYFMTEYVATRWYRAPELmLSLPEYTQAIDMWSVGCIFAEMLGRRQLFPGKNYvhqlqliltvlgtpsqavinaigA 243
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 148839316 213 SLVYRIIE--GKLPPMP-----RDYSPELAELIRTMLSKRPEERPSVRSILRQPYIK 262
Cdd:cd07855  244 DRVRRYIQnlPNKQPVPwetlyPKADQQALDLLSQMLRFDPSERITVAEALQHPFLA 300
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
2-264 1.34e-27

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: 114.38  E-value: 1.34e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   2 PLAAYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRER-RAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLY 80
Cdd:cd06635   23 PEKLFSDLREIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEKwQDIIKEVKFLQRIKHPNSIEYKGCYLR-EHTAW 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  81 IVMGFCEGGDlyRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENhc 160
Cdd:cd06635  102 LVMEYCLGSA--SDLLEVHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIASP-- 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 161 dmASTLIGTPYYMSPEL---FSNKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLvYRIIEGKLPPM-PRDYSPELA 235
Cdd:cd06635  178 --ANSFVGTPYWMAPEVilaMDEGQYDGKVDVWSLGITCIELAERKPPlFNMNAMSAL-YHIAQNESPTLqSNEWSDYFR 254
                        250       260
                 ....*....|....*....|....*....
gi 148839316 236 ELIRTMLSKRPEERPSVRSILRQPYIKRQ 264
Cdd:cd06635  255 NFVDSCLQKIPQDRPTSEELLKHMFVLRE 283
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
8-258 1.57e-27

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: 112.54  E-value: 1.57e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   8 YLRVVGKGSYGEVTLVKHRrdGKQYVIKKLnLRNASSRERRAAEqEAQLLSQLKHPNIVT-YKESWEGGDglLYIVMGFC 86
Cdd:cd05059    8 FLKELGSGQFGVVHLGKWR--GKIDVAIKM-IKEGSMSEDDFIE-EAKVMMKLSHPKLVQlYGVCTKQRP--IFIVTEYM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  87 EGGDLYRKLKEQKGQLLPEnQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIAR-VLEnhcDMAST 165
Cdd:cd05059   82 ANGCLLNYLRERRGKFQTE-QLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLARyVLD---DEYTS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 LIGTPY---YMSPELFSNKPYNYKSDVWALGCCVYEMATL-KHAFNAKDMNSLVYRIIEGKLPPMPRDYSPELAELIRTM 241
Cdd:cd05059  158 SVGTKFpvkWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSEgKMPYERFSNSEVVEHISQGYRLYRPHLAPTEVYTIMYSC 237
                        250
                 ....*....|....*..
gi 148839316 242 LSKRPEERPSVRSILRQ 258
Cdd:cd05059  238 WHEKPEERPTFKILLSQ 254
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
6-260 2.36e-27

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL2, also called p56 KKIAMRE, is expressed in testis, kidney, lung, and brain. It functions mainly in mature neurons and plays an important role in learning and memory. Inactivation of CDKL3, also called NKIAMRE (NKIATRE in rat), by translocation is associated with mild mental retardation. It has been reported that CDKL3 is lost in leukemic cells having a chromosome arm 5q deletion, and may contribute to the transformed phenotype. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 112.52  E-value: 2.36e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLlYIVMGF 85
Cdd:cd07846    3 YENLGLVGEGSYGMVMKCRHKETGQIVAIKKFLESEDDKMVKKIAMREIKMLKQLRHENLVNLIEVFRRKKRW-YLVFEF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGGDLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMAST 165
Cdd:cd07846   82 VDHTVLDDLEKYPNG--LDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 LIGTPYYMSPELFSNKP-YNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEG---------------------KL 223
Cdd:cd07846  160 YVATRWYRAPELLVGDTkYGKAVDVWAVGCLVTEMLTGEPLFPGDSDIDQLYHIIKClgnliprhqelfqknplfagvRL 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 148839316 224 P------PMPRDY---SPELAELIRTMLSKRPEERPSVRSILRQPY 260
Cdd:cd07846  240 PevkevePLERRYpklSGVVIDLAKKCLHIDPDKRPSCSELLHHEF 285
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
8-258 2.98e-27

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: 112.42  E-value: 2.98e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   8 YLRVVGKGSYGEVTLVKHR--RDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKE-SWEGGDGLLYIVMG 84
Cdd:cd14205    8 FLQQLGKGNFGSVEMCRYDplQDNTGEVVAVKKLQHSTEEHLRDFEREIEILKSLQHDNIVKYKGvCYSAGRRNLRLIME 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGGDLYRKLKEQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENhcDMAS 164
Cdd:cd14205   88 YLPYGSLRDYLQKHKERI-DHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLPQ--DKEY 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 TLIGTP-----YYMSPELFSNKPYNYKSDVWALGCCVYEMAT------------LKHAFNAKDMNSLVYRIIE-----GK 222
Cdd:cd14205  165 YKVKEPgespiFWYAPESLTESKFSVASDVWSFGVVLYELFTyieksksppaefMRMIGNDKQGQMIVFHLIEllknnGR 244
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 148839316 223 LpPMPRDYSPELAELIRTMLSKRPEERPSVRSILRQ 258
Cdd:cd14205  245 L-PRPDGCPDEIYMIMTECWNNNVNQRPSFRDLALR 279
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
10-267 3.30e-27

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: 113.14  E-value: 3.30e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRA-AEQEAQLLSQLKHPNIVTYKESWEGGDGLLyIVMGFCEG 88
Cdd:cd05632    8 RVLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKGESmALNEKQILEKVNSQFVVNLAYAYETKDALC-LVLTIMNG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  89 GDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIA-RVLENhcDMASTLI 167
Cdd:cd05632   87 GDLKFHIYNMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAvKIPEG--ESIRGRV 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 168 GTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDmNSLVYRIIEGKLPPMPRDYSPELAE----LIRTMLS 243
Cdd:cd05632  165 GTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRK-EKVKREEVDRRVLETEEVYSAKFSEeaksICKMLLT 243
                        250       260
                 ....*....|....*....|....*....
gi 148839316 244 KRPEERPSVR-----SILRQPYIkRQISF 267
Cdd:cd05632  244 KDPKQRLGCQeegagEVKRHPFF-RNMNF 271
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
6-263 4.08e-27

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: 113.34  E-value: 4.08e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRerRAAEQEAQLLSQLKHPNIV-TYKESWEGGDGL------ 78
Cdd:cd07854    7 YMDLRPLGCGSNGLVFSAVDSDCDKRVAVKKIVLTDPQSV--KHALREIKIIRRLDHDNIVkVYEVLGPSGSDLtedvgs 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  79 ------LYIVMGFCEGgDLyRKLKEQkgQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFL-TRTNIIKVGDLG 151
Cdd:cd07854   85 ltelnsVYIVQEYMET-DL-ANVLEQ--GPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFInTEDLVLKIGDFG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 152 IARVLENHCDMASTL---IGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAFNA------------------- 208
Cdd:cd07854  161 LARIVDPHYSHKGYLsegLVTKWYRSPRlLLSPNNYTKAIDMWAAGCIFAEMLTGKPLFAGaheleqmqlilesvpvvre 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148839316 209 KDMNSL-----VYRIIEGKLPPMP-RDYSPELA----ELIRTMLSKRPEERPSVRSILRQPYIKR 263
Cdd:cd07854  241 EDRNELlnvipSFVRNDGGEPRRPlRDLLPGVNpealDFLEQILTFNPMDRLTAEEALMHPYMSC 305
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
6-260 8.90e-27

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: 111.61  E-value: 8.90e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLV--KHRRDGKQYVIKKLNlrnaSSRERR-----AAEQEAQLLSQLKHPNIVTYKESW-EGGDG 77
Cdd:cd07842    2 YEIEGCIGRGTYGRVYKAkrKNGKDGKEYAIKKFK----GDKEQYtgisqSACREIALLRELKHENVVSLVEVFlEHADK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  78 LLYIVMGFCEGgDLYRKLK---EQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTR----TNIIKVGDL 150
Cdd:cd07842   78 SVYLLFDYAEH-DLWQIIKfhrQAKRVSIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVMGegpeRGVVKIGDL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 151 GIARVLENHCDMASTLIG---TPYYMSPEL-FSNKPYNYKSDVWALGCCVYEMATLKHAF---NAKDMNSLVY------R 217
Cdd:cd07842  157 GLARLFNAPLKPLADLDPvvvTIWYRAPELlLGARHYTKAIDIWAIGCIFAELLTLEPIFkgrEAKIKKSNPFqrdqleR 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 148839316 218 IIEGKLPPMPRDYspelaELIRTMlskrPEERPSVRSILRQPY 260
Cdd:cd07842  237 IFEVLGTPTEKDW-----PDIKKM----PEYDTLKSDTKASTY 270
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
8-258 9.41e-27

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: 110.93  E-value: 9.41e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   8 YLRVVGKGSYGEVTLVKH--RRD--GKQYVIKKLNlRNASSRERRAAEQEAQLLSQLKHPNIVTYKE-SWEGGDGLLYIV 82
Cdd:cd05038    8 FIKQLGEGHFGSVELCRYdpLGDntGEQVAVKSLQ-PSGEEQHMSDFKREIEILRTLDHEYIVKYKGvCESPGRRSLRLI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  83 MGFCEGGDLYRKLKEQKGQLLpENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCD- 161
Cdd:cd05038   87 MEYLPSGSLRDYLQRHRDQID-LKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAKVLPEDKEy 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 162 -MASTLIGTP-YYMSPELFSNKPYNYKSDVWALGCCVYEMAT------------LKHAFNAKDMNS---LVYRIIEGKLP 224
Cdd:cd05038  166 yYVKEPGESPiFWYAPECLRESRFSSASDVWSFGVTLYELFTygdpsqsppalfLRMIGIAQGQMIvtrLLELLKSGERL 245
                        250       260       270
                 ....*....|....*....|....*....|....
gi 148839316 225 PMPRDYSPELAELIRTMLSKRPEERPSVRSILRQ 258
Cdd:cd05038  246 PRPPSCPDEVYDLMKECWEYEPQDRPSFSDLILI 279
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
10-255 9.58e-27

Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. FAK is a cytoplasmic (or nonreceptor) PTK that contains an autophosphorylation site and a FERM domain at the N-terminus, a central tyr kinase domain, proline-rich regions, and a C-terminal FAT (focal adhesion targeting) domain. FAK activity is dependent on integrin-mediated cell adhesion, which facilitates N-terminal autophosphorylation. Full activation is achieved by the phosphorylation of its two adjacent A-loop tyrosines. FAK is important in mediating signaling initiated at sites of cell adhesions and at growth factor receptors. Through diverse molecular interactions, FAK functions as a biosensor or integrator to control cell motility. It is a key regulator of cell survival, proliferation, migration and invasion, and thus plays an important role in the development and progression of cancer. Src binds to autophosphorylated FAK forming the FAK-Src dual kinase complex, which is activated in a wide variety of tumor cells and generates signals promoting growth and metastasis. FAK is being developed as a target for cancer therapy. The FAK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 110.59  E-value: 9.58e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEV---TLVKHRRDGKQYVIKKLNlRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEggDGLLYIVMGFC 86
Cdd:cd05056   12 RCIGEGQFGDVyqgVYMSPENEKIAVAVKTCK-NCTSPSVREKFLQEAYIMRQFDHPHIVKLIGVIT--ENPVWIVMELA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  87 EGGDLyRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTL 166
Cdd:cd05056   89 PLGEL-RSYLQVNKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSRYMEDESYYKASK 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 167 IGTPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATL-KHAFNAKDMNSLVYRIIEGKLPPMPRDYSPELAELIRTMLSK 244
Cdd:cd05056  168 GKLPIkWMAPESINFRRFTSASDVWMFGVCMWEILMLgVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAY 247
                        250
                 ....*....|.
gi 148839316 245 RPEERPSVRSI 255
Cdd:cd05056  248 DPSKRPRFTEL 258
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
9-199 1.06e-26

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: 111.94  E-value: 1.06e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLnlRNASSRERRAAEQ---EAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGF 85
Cdd:cd05599    6 LKVIGRGAFGEVRLVRKKDTGHVYAMKKL--RKSEMLEKEQVAHvraERDILAEADNPWVVKLYYSFQD-EENLYLIMEF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGGDLYRKLkeQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLEN-HcdMAS 164
Cdd:cd05599   83 LPGGDMMTLL--MKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGLCTGLKKsH--LAY 158
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 148839316 165 TLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEM 199
Cdd:cd05599  159 STVGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEM 193
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
12-261 1.13e-26

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: 110.81  E-value: 1.13e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNL----------RNASSRERRAAE--------------QEAQLLSQLKHPNIVT 67
Cdd:cd14200    8 IGKGSYGVVKLAYNESDDKYYAMKVLSKkkllkqygfpRRPPPRGSKAAQgeqakplaplervyQEIAILKKLDHVNIVK 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  68 YKESWEG-GDGLLYIVMgfceggDLYRK---LKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTN 143
Cdd:cd14200   88 LIEVLDDpAEDNLYMVF------DLLRKgpvMEVPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDDG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 144 IIKVGDLGIARVLENHCDMASTLIGTPYYMSPELFSNKPYNYKS---DVWALG----CCVYEMATLKHAFNAKDMNSLVY 216
Cdd:cd14200  162 HVKIADFGVSNQFEGNDALLSSTAGTPAFMAPETLSDSGQSFSGkalDVWAMGvtlyCFVYGKCPFIDEFILALHNKIKN 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 148839316 217 RIIEgkLPPMPrDYSPELAELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd14200  242 KPVE--FPEEP-EISEELKDLILKMLDKNPETRITVPEIKVHPWV 283
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
10-262 1.31e-26

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: 111.54  E-value: 1.31e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLNlRNASSRER--RAAEQEAQLLS-QLKHPNIVTYKESWEGGDGLLYiVMGFC 86
Cdd:cd05590    1 RVLGKGSFGKVMLARLKESGRLYAVKVLK-KDVILQDDdvECTMTEKRILSlARNHPFLTQLYCCFQTPDRLFF-VMEFV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  87 EGGDLYRKLkeQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARvlENHCD--MAS 164
Cdd:cd05590   79 NGGDLMFHI--QKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCK--EGIFNgkTTS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 TLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLpPMPRDYSPELAELIRTMLSK 244
Cdd:cd05590  155 TFCGTPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEV-VYPTWLSQDAVDILKAFMTK 233
                        250       260
                 ....*....|....*....|....
gi 148839316 245 RPEERPSV------RSILRQPYIK 262
Cdd:cd05590  234 NPTMRLGSltlggeEAILRHPFFK 257
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
11-258 1.56e-26

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: 109.69  E-value: 1.56e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  11 VVGKGSYGEVTLVKHRrdGKQYVIKKLNLR-----NASSRERRaaeQEAQLLSQLKHPNIVTYKeswegGDGL----LYI 81
Cdd:cd14148    1 IIGVGGFGKVYKGLWR--GEEVAVKAARQDpdediAVTAENVR---QEARLFWMLQHPNIIALR-----GVCLnpphLCL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  82 VMGFCEGGDLYRKLKeqkGQLLPENQVVEWFVQIAMALQYLHEKH---ILHRDLKTQNVFLTR--------TNIIKVGDL 150
Cdd:cd14148   71 VMEYARGGALNRALA---GKKVPPHVLVNWAVQIARGMNYLHNEAivpIIHRDLKSSNILILEpienddlsGKTLKITDF 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 151 GIARVLENHCDMASTliGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLP-PMPRD 229
Cdd:cd14148  148 GLAREWHKTTKMSAA--GTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYREIDALAVAYGVAMNKLTlPIPST 225
                        250       260
                 ....*....|....*....|....*....
gi 148839316 230 YSPELAELIRTMLSKRPEERPSVRSILRQ 258
Cdd:cd14148  226 CPEPFARLLEECWDPDPHGRPDFGSILKR 254
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
9-259 1.73e-26

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: 109.80  E-value: 1.73e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQL-KHPNIVTYKESWeGGDGLLYIVMGFCE 87
Cdd:cd14051    5 VEKIGSGEFGSVYKCINRLDGCVYAIKKSKKPVAGSVDEQNALNEVYAHAVLgKHPHVVRYYSAW-AEDDHMIIQNEYCN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  88 GGDLYRKLKE--QKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNII-------------------- 145
Cdd:cd14051   84 GGSLADAISEneKAGERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFISRTPNPvsseeeeedfegeednpesn 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 146 ----KVGDLGiarvlenHCdmasTLIGTPY-------YMSPEL----FSNKPynyKSDVWALGCCVYEMA---TLKHafN 207
Cdd:cd14051  164 evtyKIGDLG-------HV----TSISNPQveegdcrFLANEIlqenYSHLP---KADIFALALTVYEAAgggPLPK--N 227
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 148839316 208 AKDMnslvYRIIEGKLPPMPRdYSPELAELIRTMLSKRPEERPSVRSILRQP 259
Cdd:cd14051  228 GDEW----HEIRQGNLPPLPQ-CSPEFNELLRSMIHPDPEKRPSAAALLQHP 274
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
6-261 1.87e-26

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: 110.22  E-value: 1.87e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRR-DGKQYVIKKLNLRNASSRERRAAE-----QEAQLLSQLKHPNIVTYKESWEGgDGLL 79
Cdd:cd14096    3 YRLINKIGEGAFSNVYKAVPLRnTGKPVAIKVVRKADLSSDNLKGSSranilKEVQIMKRLSHPNIVKLLDFQES-DEYY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  80 YIVMGFCEGGDLYrklkeqkgqllpeNQVVEW-----------FVQIAMALQYLHEKHILHRDLKTQNVFLTRT------ 142
Cdd:cd14096   82 YIVLELADGGEIF-------------HQIVRLtyfsedlsrhvITQVASAVKYLHEIGVVHRDIKPENLLFEPIpfipsi 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 143 ---------------------------NIIKVGDLGIARVLENhcDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCC 195
Cdd:cd14096  149 vklrkadddetkvdegefipgvggggiGIVKLADFGLSKQVWD--SNTKTPCGTVGYTAPEVVKDERYSKKVDMWALGCV 226
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148839316 196 VYEMATLKHAFNAKDMNSLVYRIIEGK---LPPMPRDYSPELAELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd14096  227 LYTLLCGFPPFYDESIETLTEKISRGDytfLSPWWDEISKSAKDLISHLLTVDPAKRYDIDEFLAHPWI 295
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
12-258 1.92e-26

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: 109.73  E-value: 1.92e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSY-GEVTLVKHRRDGKQYVIkklnlrnasSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLyIVMGFCEGGD 90
Cdd:cd14147   19 VYRGSWrGELVAVKAARQDPDEDI---------SVTAESVRQEARLFAMLAHPNIIALKAVCLEEPNLC-LVMEYAAGGP 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  91 LYRKLKeqkGQLLPENQVVEWFVQIAMALQYLHEKHI---LHRDLKTQNVFLTRTNI--------IKVGDLGIARvlENH 159
Cdd:cd14147   89 LSRALA---GRRVPPHVLVNWAVQIARGMHYLHCEALvpvIHRDLKSNNILLLQPIEnddmehktLKITDFGLAR--EWH 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 160 CDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLP-PMPRDYSPELAELI 238
Cdd:cd14147  164 KTTQMSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRGIDCLAVAYGVAVNKLTlPIPSTCPEPFAQLM 243
                        250       260
                 ....*....|....*....|
gi 148839316 239 RTMLSKRPEERPSVRSILRQ 258
Cdd:cd14147  244 ADCWAQDPHRRPDFASILQQ 263
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
9-249 3.07e-26

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: 109.70  E-value: 3.07e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKH---RRDGKQYVIKKLN----LRNASSRERRAAEQeaQLLSQLKH-PNIVTYKESWEGgDGLLY 80
Cdd:cd05613    5 LKVLGTGAYGKVFLVRKvsgHDAGKLYAMKVLKkatiVQKAKTAEHTRTER--QVLEHIRQsPFLVTLHYAFQT-DTKLH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  81 IVMGFCEGGDLYRKLKEQkgQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIAR-VLENH 159
Cdd:cd05613   82 LILDYINGGELFTHLSQR--ERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKeFLLDE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 160 CDMASTLIGTPYYMSPELF--SNKPYNYKSDVWALGCCVYEMATLKHAFNA---KDMNSLVYRIIEGKLPPMPRDYSPEL 234
Cdd:cd05613  160 NERAYSFCGTIEYMAPEIVrgGDSGHDKAVDWWSLGVLMYELLTGASPFTVdgeKNSQAEISRRILKSEPPYPQEMSALA 239
                        250
                 ....*....|....*
gi 148839316 235 AELIRTMLSKRPEER 249
Cdd:cd05613  240 KDIIQRLLMKDPKKR 254
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
12-263 3.45e-26

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: 109.17  E-value: 3.45e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAeQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGFCEGGD- 90
Cdd:cd06622    9 LGKGNYGSVYKVLHRPTGVTMAMKEIRLELDESKFNQII-MELDILHKAVSPYIVDFYGAFFI-EGAVYMCMEYMDAGSl 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  91 --LYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKH-ILHRDLKTQNVFLTRTNIIKVGDLGIARVLEnhCDMASTLI 167
Cdd:cd06622   87 dkLYAGGVATEG--IPEDVLRRITYAVVKGLKFLKEEHnIIHRDVKPTNVLVNGNGQVKLCDFGVSGNLV--ASLAKTNI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 168 GTPYYMSPELFS------NKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYR---IIEGKLPPMPRDYSPELAELI 238
Cdd:cd06622  163 GCQSYMAPERIKsggpnqNPTYTVQSDVWSLGLSILEMALGRYPYPPETYANIFAQlsaIVDGDPPTLPSGYSDDAQDFV 242
                        250       260
                 ....*....|....*....|....*
gi 148839316 239 RTMLSKRPEERPSVRSILRQPYIKR 263
Cdd:cd06622  243 AKCLNKIPNRRPTYAQLLEHPWLVK 267
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
9-249 3.64e-26

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: 110.51  E-value: 3.64e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQE---------AQLLSQLKHpnivTYKEsweggDGLL 79
Cdd:cd05597    6 LKVIGRGAFGEVAVVKLKSTEKVYAMKILNKWEMLKRAETACFREerdvlvngdRRWITKLHY----AFQD-----ENYL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  80 YIVMGFCEGGDLYrKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLG-IARVLEN 158
Cdd:cd05597   77 YLVMDYYCGGDLL-TLLSKFEDRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFGsCLKLRED 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 159 HCDMASTLIGTPYYMSPELF-----SNKPYNYKSDVWALGCCVYEMATLKHAFNAKdmnSLV--Y-RIIEGK----LPPM 226
Cdd:cd05597  156 GTVQSSVAVGTPDYISPEILqamedGKGRYGPECDWWSLGVCMYEMLYGETPFYAE---SLVetYgKIMNHKehfsFPDD 232
                        250       260
                 ....*....|....*....|...
gi 148839316 227 PRDYSPELAELIRTMLSkRPEER 249
Cdd:cd05597  233 EDDVSEEAKDLIRRLIC-SRERR 254
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
11-298 3.96e-26

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: 110.09  E-value: 3.96e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  11 VVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRA-AEQEAQLLSQLKHPNIVTYKESWEGGDGLlYIVMGFCEGG 89
Cdd:cd05601    8 VIGRGHFGEVQVVKEKATGDIYAMKVLKKSETLAQEEVSfFEEERDIMAKANSPWITKLQYAFQDSENL-YLVMEYHPGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  90 DLYRKLKEQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTL-IG 168
Cdd:cd05601   87 DLLSLLSRYDDIF-EESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSAAKLSSDKTVTSKMpVG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 169 TPYYMSPELFSNKPYNYKS------DVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGK----LPPMPRdYSPELAELI 238
Cdd:cd05601  166 TPDYIAPEVLTSMNGGSKGtygvecDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIMNFKkflkFPEDPK-VSESAVDLI 244
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 239 RTMLSKrPEERPSVRSILRQPyikrqisFFLEatkikTSKNNIKNgdsQSKPFATVVSGE 298
Cdd:cd05601  245 KGLLTD-AKERLGYEGLCCHP-------FFSG-----IDWNNLRQ---TVPPFVPTLTSD 288
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
12-193 4.01e-26

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: 108.75  E-value: 4.01e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNlrNASSRERRAAEQEAQLLSQLKHPNI-----VTYKesweggDGLLYIVMGFC 86
Cdd:cd14154    1 LGKGFFGQAIKVTHRETGEVMVMKELI--RFDEEAQRNFLKEVKVMRSLDHPNVlkfigVLYK------DKKLNLITEYI 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  87 EGGDLYRKLKEqKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARV-----LENHCD 161
Cdd:cd14154   73 PGGTLKDVLKD-MARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLARLiveerLPSGNM 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 148839316 162 MAS---------------TLIGTPYYMSPELFSNKPYNYKSDVWALG 193
Cdd:cd14154  152 SPSetlrhlkspdrkkryTVVGNPYWMAPEMLNGRSYDEKVDIFSFG 198
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
12-266 4.80e-26

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: 108.99  E-value: 4.80e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERR-AAEQEAQLLSQlKHPNIVTYKES--WEGGdglLYIVMGFCEG 88
Cdd:cd06616   14 IGRGAFGTVNKMLHKPSGTIMAVKRIRSTVDEKEQKRlLMDLDVVMRSS-DCPYIVKFYGAlfREGD---CWICMELMDI 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  89 G--DLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEK-HILHRDLKTQNVFLTRTNIIKVGDLGIARVLENhcDMAST 165
Cdd:cd06616   90 SldKFYKYVYEVLDSVIPEEILGKIAVATVKALNYLKEElKIIHRDVKPSNILLDRNGNIKLCDFGISGQLVD--SIAKT 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 L-IGTPYYMSPELF----SNKPYNYKSDVWALGCCVYEMATLKHAFNAkdMNSL---VYRIIEGKLPPMPRD----YSPE 233
Cdd:cd06616  168 RdAGCRPYMAPERIdpsaSRDGYDVRSDVWSLGITLYEVATGKFPYPK--WNSVfdqLTQVVKGDPPILSNSeereFSPS 245
                        250       260       270
                 ....*....|....*....|....*....|...
gi 148839316 234 LAELIRTMLSKRPEERPSVRSILRQPYIKRQIS 266
Cdd:cd06616  246 FVNFVNLCLIKDESKRPKYKELLKHPFIKMYEE 278
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
12-199 6.32e-26

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: 107.56  E-value: 6.32e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKlnlrNASSRERRAAEQEAQLLSQLKHPNIVTYKeswegG----DGLLYIVMGFCE 87
Cdd:cd14155    1 IGSGFFSEVYKVRHRTSGQVMALKM----NTLSSNRANMLREVQLMNRLSHPNILRFM-----GvcvhQGQLHALTEYIN 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  88 GGDLYrklkeqkgQLLPENQVVEWFVQ------IAMALQYLHEKHILHRDLKTQNVFLTRTN---IIKVGDLGIARVLEN 158
Cdd:cd14155   72 GGNLE--------QLLDSNEPLSWTVRvklaldIARGLSYLHSKGIFHRDLTSKNCLIKRDEngyTAVVGDFGLAEKIPD 143
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 148839316 159 HCDMASTL--IGTPYYMSPELFSNKPYNYKSDVWALGCCVYEM 199
Cdd:cd14155  144 YSDGKEKLavVGSPYWMAPEVLRGEPYNEKADVFSYGIILCEI 186
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
8-262 6.69e-26

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKN has a C-terminal catalytic domain that is highly homologous to PKCs. Its unique N-terminal regulatory region contains antiparallel coiled-coil (ACC) domains. In mammals, there are three PKN isoforms from different genes (designated PKN-alpha, beta, and gamma), which show different enzymatic properties, tissue distribution, and varied functions. PKN can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytokeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. The PKN subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 109.31  E-value: 6.69e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   8 YLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSR--------ERRAAEqeaqLLSQLKHPNIVTYKESWEGGDGLL 79
Cdd:cd05589    3 CIAVLGRGHFGKVLLAEYKPTGELFAIKALKKGDIIARdeveslmcEKRIFE----TVNSARHPFLVNLFACFQTPEHVC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  80 YiVMGFCEGGDLYRKLKEQkgqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENH 159
Cdd:cd05589   79 F-VMEYAAGGDLMMHIHED---VFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGF 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 160 CDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLpPMPRDYSPELAELIR 239
Cdd:cd05589  155 GDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEV-RYPRFLSTEAISIMR 233
                        250       260
                 ....*....|....*....|....*...
gi 148839316 240 TMLSKRPEER--PSVR---SILRQPYIK 262
Cdd:cd05589  234 RLLRKNPERRlgASERdaeDVKKQPFFR 261
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
12-199 6.72e-26

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: 107.58  E-value: 6.72e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRNassrERRAAEQEAQLLSQLKHPNIVTYKeswegG----DGLLYIVMGFCE 87
Cdd:cd14065    1 LGKGFFGEVYKVTHRETGKVMVMKELKRFD----EQRSFLKEVKLMRRLSHPNILRFI-----GvcvkDNKLNFITEYVN 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  88 GGDLYRKLKEQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIK---VGDLGIARVLENHCDMAS 164
Cdd:cd14065   72 GGTLEELLKSMDEQL-PWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVREANRGRnavVADFGLAREMPDEKTKKP 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 148839316 165 ------TLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEM 199
Cdd:cd14065  151 drkkrlTVVGSPYWMAPEMLRGESYDEKVDVFSFGIVLCEI 191
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
15-209 6.98e-26

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L1, also called PITSLRE, exists in different isoforms which are named using the alias CDK11(p). The CDC2L1 gene produces two protein products, CDK11(p110) and CDK11(p58). CDC2L1 is also represented by the caspase-processed CDK11(p46). CDK11(p110), the major isoform, associates with cyclin L and is expressed throughout the cell cycle. It is involved in RNA processing and the regulation of transcription. CDK11(p58) associates with cyclin D3 and is expressed during the G2/M phase of the cell cycle. It plays roles in spindle morphogenesis, centrosome maturation, sister chromatid cohesion, and the completion of mitosis. CDK11(p46) is formed from the larger isoforms by caspases during TNFalpha- and Fas-induced apoptosis. It functions as a downstream effector kinase in apoptotic signaling pathways and interacts with eukaryotic initiation factor 3f (eIF3f), p21-activated kinase (PAK1), and Ran-binding protein (RanBPM). CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 108.47  E-value: 6.98e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  15 GSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGgDGL--LYIVMGFCEGgDLY 92
Cdd:cd07843   16 GTYGVVYRARDKKTGEIVALKKLKMEKEKEGFPITSLREINILLKLQHPNIVTVKEVVVG-SNLdkIYMVMEYVEH-DLK 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  93 RKLKEQKGQLLPeNQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTLIGTPYY 172
Cdd:cd07843   94 SLMETMKQPFLQ-SEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLAREYGSPLKPYTQLVVTLWY 172
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 148839316 173 MSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAFNAK 209
Cdd:cd07843  173 RAPElLLGAKEYSTAIDMWSVGCIFAELLTKKPLFPGK 210
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
10-261 7.57e-26

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: 107.77  E-value: 7.57e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLNlrnASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLYIVMGFCEGG 89
Cdd:cd14172   10 QVLGLGVNGKVLECFHRRTGQKCALKLLY---DSPKARREVEHHWRASGGPHIVHILDVYENMHHGKRCLLIIMECMEGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  90 DLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLT---RTNIIKVGDLGIARVLENHcDMASTL 166
Cdd:cd14172   87 ELFSRIQERGDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTskeKDAVLKLTDFGFAKETTVQ-NALQTP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 167 IGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLV----YRIIEGKLP-PMPR--DYSPELAELIR 239
Cdd:cd14172  166 CYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTGQAISpgmkRRIRMGQYGfPNPEwaEVSEEAKQLIR 245
                        250       260
                 ....*....|....*....|..
gi 148839316 240 TMLSKRPEERPSVRSILRQPYI 261
Cdd:cd14172  246 HLLKTDPTERMTITQFMNHPWI 267
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
12-257 1.14e-25

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: 107.02  E-value: 1.14e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNlrnASSRERRAAEQEAQLLSQLK-HPNIV-TYKESWEGGDglLYI-VMGFCEG 88
Cdd:cd13987    1 LGEGTYGKVLLAVHKGSGTKMALKFVP---KPSTKLKDFLREYNISLELSvHPHIIkTYDVAFETED--YYVfAQEYAPY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  89 GDLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNI--IKVGDLGIARvlenhcdMASTL 166
Cdd:cd13987   76 GDLFSIIPPQVG--LPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDCrrVKLCDFGLTR-------RVGST 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 167 I----GTPYYMSPELFSNKPY-----NYKSDVWALGCCVYEMATLKHAFN-AKDMNSLVYRIIE------GKLPPMPRDY 230
Cdd:cd13987  147 VkrvsGTIPYTAPEVCEAKKNegfvvDPSIDVWAFGVLLFCCLTGNFPWEkADSDDQFYEEFVRwqkrknTAVPSQWRRF 226
                        250       260
                 ....*....|....*....|....*..
gi 148839316 231 SPELAELIRTMLSKRPEERPSVRSILR 257
Cdd:cd13987  227 TPKALRMFKKLLAPEPERRCSIKEVFK 253
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
9-256 1.33e-25

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: 107.43  E-value: 1.33e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEV------TLVKHRRDGKqYVIKKLNlRNASSRERRAAEQEAQLLSQLKHPNIVTykesweggdgLL--- 79
Cdd:cd05032   11 IRELGQGSFGMVyeglakGVVKGEPETR-VAIKTVN-ENASMRERIEFLNEASVMKEFNCHHVVR----------LLgvv 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  80 ------YIVMGFCEGGDLYRKLKEQK--------GQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNII 145
Cdd:cd05032   79 stgqptLVVMELMAKGDLKSYLRSRRpeaennpgLGPPTLQKFIQMAAEIADGMAYLAAKKFVHRDLAARNCMVAEDLTV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 146 KVGDLGIARVLENHcdmastligtPYY------------MSPELFSNKPYNYKSDVWALGCCVYEMATL-KHAFNAKDMN 212
Cdd:cd05032  159 KIGDFGMTRDIYET----------DYYrkggkgllpvrwMAPESLKDGVFTTKSDVWSFGVVLWEMATLaEQPYQGLSNE 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 148839316 213 SLVYRIIEGKLPPMPRDYSPELAELIRTMLSKRPEERPSVRSIL 256
Cdd:cd05032  229 EVLKFVIDGGHLDLPENCPDKLLELMRMCWQYNPKMRPTFLEIV 272
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
8-249 1.51e-25

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: 107.11  E-value: 1.51e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   8 YLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSR-ERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLyIVMGFC 86
Cdd:cd05609    4 TIKLISNGAYGAVYLVRHRETRQRFAMKKINKQNLILRnQIQQVFVERDILTFAENPFVVSMYCSFETKRHLC-MVMEYV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  87 EGGDLYRKLKeqKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARV---------LE 157
Cdd:cd05609   83 EGGDCATLLK--NIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSKIglmslttnlYE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 158 NHCD------MASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPRD-- 229
Cdd:cd05609  161 GHIEkdtrefLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIEWPEGDda 240
                        250       260
                 ....*....|....*....|
gi 148839316 230 YSPELAELIRTMLSKRPEER 249
Cdd:cd05609  241 LPDDAQDLITRLLQQNPLER 260
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
9-256 1.93e-25

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: 106.64  E-value: 1.93e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGevTLVKHRRDGkQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKesweggdGLLY-----IVM 83
Cdd:cd14150    5 LKRIGTGSFG--TVFRGKWHG-DVAVKILKVTEPTPEQLQAFKNEMQVLRKTRHVNILLFM-------GFMTrpnfaIIT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  84 GFCEGGDLYRKLK--EQKGQLLpenQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLE--NH 159
Cdd:cd14150   75 QWCEGSSLYRHLHvtETRFDTM---QLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLATVKTrwSG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 160 CDMASTLIGTPYYMSPELF---SNKPYNYKSDVWALGCCVYEM--ATLKHAfNAKDMNSLVYRIIEGKLPPMPRDYSPEL 234
Cdd:cd14150  152 SQQVEQPSGSILWMAPEVIrmqDTNPYSFQSDVYAYGVVLYELmsGTLPYS-NINNRDQIIFMVGRGYLSPDLSKLSSNC 230
                        250       260
                 ....*....|....*....|....*.
gi 148839316 235 AELIRTMLSK----RPEERPSVRSIL 256
Cdd:cd14150  231 PKAMKRLLIDclkfKREERPLFPQIL 256
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
52-251 2.06e-25

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: 105.83  E-value: 2.06e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  52 QEAQLLSQLKHPNIV------TYKESweggdglLYIVMGFCEGGDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEK 125
Cdd:cd05034   39 QEAQIMKKLRHDKLVqlyavcSDEEP-------IYIVTELMSKGSLLDYLRTGEGRALRLPQLIDMAAQIASGMAYLESR 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 126 HILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTLIGTPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATLKH 204
Cdd:cd05034  112 NYIHRDLAARNILVGENNVCKVADFGLARLIEDDEYTAREGAKFPIkWTAPEAALYGRFTIKSDVWSFGILLYEIVTYGR 191
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 148839316 205 AFNAKDMNSLVYRIIE-GKLPPMPRDYSPELAELIRTMLSKRPEERPS 251
Cdd:cd05034  192 VPYPGMTNREVLEQVErGYRMPKPPGCPDELYDIMLQCWKKEPEERPT 239
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
8-260 2.19e-25

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: 106.59  E-value: 2.19e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   8 YLRVVGKGSYGevTLV-KHRRDGKQYVIKKLnLRNASSrerrAAEQEAQLLSQL-KHPNIVTYKESwEGGDGLLYIVMGF 85
Cdd:cd13982    5 SPKVLGYGSEG--TIVfRGTFDGRPVAVKRL-LPEFFD----FADREVQLLRESdEHPNVIRYFCT-EKDRQFLYIALEL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGG--DLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNI-----IKVGDLGIARVLEn 158
Cdd:cd13982   77 CAASlqDLVESPRESKLFLRPGLEPVRLLRQIASGLAHLHSLNIVHRDLKPQNILISTPNAhgnvrAMISDFGLCKKLD- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 159 hcDMASTLI------GTPYYMSPELFSNKPYN---YKSDVWALGCCVYEMATL-KHAFNAK---DMNslvyrIIEGK--L 223
Cdd:cd13982  156 --VGRSSFSrrsgvaGTSGWIAPEMLSGSTKRrqtRAVDIFSLGCVFYYVLSGgSHPFGDKlerEAN-----ILKGKysL 228
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 148839316 224 PPMPRD--YSPELAELIRTMLSKRPEERPSVRSILRQPY 260
Cdd:cd13982  229 DKLLSLgeHGPEAQDLIERMIDFDPEKRPSAEEVLNHPF 267
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
12-262 2.79e-25

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: 106.24  E-value: 2.79e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAA----EQEAQLLSQLKHPNIVTYKESWEGGDGLLyIVMGFCE 87
Cdd:cd14195   13 LGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSSSRRGVSreeiEREVNILREIQHPNIITLHDIFENKTDVV-LILELVS 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  88 GGDLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNI----IKVGDLGIARVLENHCDMA 163
Cdd:cd14195   92 GGELFDFLAEKES--LTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVpnprIKLIDFGIAHKIEAGNEFK 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 164 StLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRiIEGKLPPMPRDYSPELAEL----IR 239
Cdd:cd14195  170 N-IFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTN-ISAVNYDFDEEYFSNTSELakdfIR 247
                        250       260
                 ....*....|....*....|...
gi 148839316 240 TMLSKRPEERPSVRSILRQPYIK 262
Cdd:cd14195  248 RLLVKDPKKRMTIAQSLEHSWIK 270
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
12-261 2.83e-25

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: 105.77  E-value: 2.83e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLnlRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLyIVMGFCEGGDL 91
Cdd:cd14103    1 LGRGKFGTVYRCVEKATGKELAAKFI--KCRKAKDREDVRNEIEIMNQLRHPRLLQLYDAFETPREMV-LVMEYVAGGEL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  92 YRKLKEQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVF-LTRT-NIIKVGDLGIARVLENHCDMaSTLIGT 169
Cdd:cd14103   78 FERVVDDDFEL-TERDCILFMRQICEGVQYMHKQGILHLDLKPENILcVSRTgNQIKIIDFGLARKYDPDKKL-KVLFGT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 170 PYYMSPELFSNKPYNYKSDVWALGCCVY-------------EMATLKHAFNAK-DMNSLVYRIIegklppmprdySPELA 235
Cdd:cd14103  156 PEFVAPEVVNYEPISYATDMWSVGVICYvllsglspfmgdnDAETLANVTRAKwDFDDEAFDDI-----------SDEAK 224
                        250       260
                 ....*....|....*....|....*.
gi 148839316 236 ELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd14103  225 DFISKLLVKDPRKRMSAAQCLQHPWL 250
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
10-261 2.87e-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: 106.23  E-value: 2.87e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERrAAEQEAQLLSQLKHPNIVTYKESWEGGDGLlYIVMGFCEGG 89
Cdd:cd14183   12 RTIGDGNFAVVKECVERSTGREYALKIINKSKCRGKEH-MIQNEVSILRRVKHPNIVLLIEEMDMPTEL-YLVMELVKGG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  90 DLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTR----TNIIKVGDLGIARVLENHCdmaST 165
Cdd:cd14183   90 DLFDAITSTNK--YTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEhqdgSKSLKLGDFGLATVVDGPL---YT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAF--NAKDMNSLVYRIIEGKLP-PMP--RDYSPELAELIRT 240
Cdd:cd14183  165 VCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFrgSGDDQEVLFDQILMGQVDfPSPywDNVSDSAKELITM 244
                        250       260
                 ....*....|....*....|.
gi 148839316 241 MLSKRPEERPSVRSILRQPYI 261
Cdd:cd14183  245 MLQVDVDQRYSALQVLEHPWV 265
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
9-225 3.40e-25

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: 106.62  E-value: 3.40e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGFCEG 88
Cdd:cd07848    6 LGVVGEGAYGVVLKCRHKETKEIVAIKKFKDSEENEEVKETTLRELKMLRTLKQENIVELKEAFRR-RGKLYLVFEYVEK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  89 GDLyrKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMAST-LI 167
Cdd:cd07848   85 NML--ELLEEMPNGVPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLSEGSNANYTeYV 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 168 GTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRI--IEGKLPP 225
Cdd:cd07848  163 ATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQPLFPGESEIDQLFTIqkVLGPLPA 222
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
12-261 3.40e-25

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: 105.81  E-value: 3.40e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLR--NASSR--ERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLyIVMGFCE 87
Cdd:cd14196   13 LGSGQFAIVKKCREKSTGLEYAAKFIKKRqsRASRRgvSREEIEREVSILRQVLHPNIITLHDVYENRTDVV-LILELVS 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  88 GGDLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNI----IKVGDLGIARVLENHCDMA 163
Cdd:cd14196   92 GGELFDFLAQKES--LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIEDGVEFK 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 164 StLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVyriieGKLPPMPRDY-------SPELA- 235
Cdd:cd14196  170 N-IFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETL-----ANITAVSYDFdeeffshTSELAk 243
                        250       260
                 ....*....|....*....|....*.
gi 148839316 236 ELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd14196  244 DFIRKLLVKETRKRLTIQEALRHPWI 269
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
10-278 4.47e-25

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: 106.66  E-value: 4.47e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLNlrnASSRERRAAEQEAQLlSQLKH-PNIVTYKESWEGGDGLLYIVMGFCEG 88
Cdd:cd14170    8 QVLGLGINGKVLQIFNKRTQEKFALKMLQ---DCPKARREVELHWRA-SQCPHiVRIVDVYENLYAGRKCLLIVMECLDG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  89 GDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLT--RTN-IIKVGDLGIARVLENHCDMAsT 165
Cdd:cd14170   84 GELFSRIQDRGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTskRPNaILKLTDFGFAKETTSHNSLT-T 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 LIGTPYYMSPELFSNKPYNYKSDVWALGC------CVYEMATLKHAFNAKDMNSLVYRIIEGKLP-PMPRDYSPELAELI 238
Cdd:cd14170  163 PCYTPYYVAPEVLGPEKYDKSCDMWSLGVimyillCGYPPFYSNHGLAISPGMKTRIRMGQYEFPnPEWSEVSEEVKMLI 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 148839316 239 RTMLSKRPEERPSVRSILRQPYIKRqiSFFLEATKIKTSK 278
Cdd:cd14170  243 RNLLKTEPTQRMTITEFMNHPWIMQ--STKVPQTPLHTSR 280
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
12-261 5.36e-25

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: 105.26  E-value: 5.36e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRNA-SSR---ERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLYIvMGFCE 87
Cdd:cd14105   13 LGSGQFAVVKKCREKSTGLEYAAKFIKKRRSkASRrgvSREDIEREVSILRQVLHPNIITLHDVFENKTDVVLI-LELVA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  88 GGDLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNI----IKVGDLGIARVLENHCDMA 163
Cdd:cd14105   92 GGELFDFLAEKES--LSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNVpiprIKLIDFGLAHKIEDGNEFK 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 164 StLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPRDYS--PELA-ELIRT 240
Cdd:cd14105  170 N-IFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVNYDFDDEYFSntSELAkDFIRQ 248
                        250       260
                 ....*....|....*....|.
gi 148839316 241 MLSKRPEERPSVRSILRQPYI 261
Cdd:cd14105  249 LLVKDPRKRMTIQESLRHPWI 269
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
12-256 6.53e-25

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: 105.14  E-value: 6.53e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDgkqYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDglLYIVMGFCEGGDL 91
Cdd:cd14151   16 IGSGSFGTVYKGKWHGD---VAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQ--LAIVTQWCEGSSL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  92 YRKLK--EQKGQLLpenQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLE--NHCDMASTLI 167
Cdd:cd14151   91 YHHLHiiETKFEMI---KLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSrwSGSHQFEQLS 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 168 GTPYYMSPELF---SNKPYNYKSDVWALGCCVYEMATLKHAF-NAKDMNSLVYRIIEGKLPP---MPRDYSPE-LAELIR 239
Cdd:cd14151  168 GSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPYsNINNRDQIIFMVGRGYLSPdlsKVRSNCPKaMKRLMA 247
                        250
                 ....*....|....*..
gi 148839316 240 TMLSKRPEERPSVRSIL 256
Cdd:cd14151  248 ECLKKKRDERPLFPQIL 264
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
9-245 6.97e-25

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: 108.18  E-value: 6.97e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAA-EQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGFCE 87
Cdd:cd05623   77 LKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAETACfREERDVLVNGDSQWITTLHYAFQD-DNNLYLVMDYYV 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  88 GGDLYRKLKEQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLG-IARVLENHCDMASTL 166
Cdd:cd05623  156 GGDLLTLLSKFEDRL-PEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGsCLKLMEDGTVQSSVA 234
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 167 IGTPYYMSPELFS-----NKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGK----LPPMPRDYSPELAEL 237
Cdd:cd05623  235 VGTPDYISPEILQamedgKGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKerfqFPTQVTDVSENAKDL 314

                 ....*...
gi 148839316 238 IRTMLSKR 245
Cdd:cd05623  315 IRRLICSR 322
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
12-260 7.24e-25

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: 104.59  E-value: 7.24e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRnasSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLYIVMgFCEGGDL 91
Cdd:cd14107   10 IGRGTFGFVKRVTHKGNGECCAAKFIPLR---SSTRARAFQERDILARLSHRRLTCLLDQFETRKTLILILE-LCSSEEL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  92 YRKLKeQKGqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFL---TRTNIiKVGDLGIARVLENhCDMASTLIG 168
Cdd:cd14107   86 LDRLF-LKG-VVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMvspTREDI-KICDFGFAQEITP-SEHQFSKYG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 169 TPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKL---PPMPRDYSPELAELIRTMLSKR 245
Cdd:cd14107  162 SPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVVswdTPEITHLSEDAKDFIKRVLQPD 241
                        250
                 ....*....|....*
gi 148839316 246 PEERPSVRSILRQPY 260
Cdd:cd14107  242 PEKRPSASECLSHEW 256
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
12-261 7.26e-25

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


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 105.43  E-value: 7.26e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLN----LRNASSRER---RAAE-----------------QEAQLLSQLKHPNIVT 67
Cdd:cd14199   10 IGKGSYGVVKLAYNEDDNTYYAMKVLSkkklMRQAGFPRRpppRGARaapegctqprgpiervyQEIAILKKLDHPNVVK 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  68 YKESWEG-GDGLLYIVMGFCEGGDLyrkLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIK 146
Cdd:cd14199   90 LVEVLDDpSEDHLYMVFELVKQGPV---MEVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLVGEDGHIK 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 147 VGDLGIARVLENHCDMASTLIGTPYYMSPELFSNKPYNYKS---DVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKL 223
Cdd:cd14199  167 IADFGVSNEFEGSDALLTNTVGTPAFMAPETLSETRKIFSGkalDVWAMGVTLYCFVFGQCPFMDERILSLHSKIKTQPL 246
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 148839316 224 P-PMPRDYSPELAELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd14199  247 EfPDQPDISDDLKDLLFRMLDKNPESRISVPEIKLHPWV 285
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
10-267 8.17e-25

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: 106.55  E-value: 8.17e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNA-SSRERRAAEQEAQLLS-QLKHPNIVTYKESWEGGDGLLYiVMGFCE 87
Cdd:cd05619   11 KMLGKGSFGKVFLAELKGTNQFFAIKALKKDVVlMDDDVECTMVEKRVLSlAWEHPFLTHLFCTFQTKENLFF-VMEYLN 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  88 GGDLYRKLKEQKGQLLPENQVveWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARvlENHCDMA--ST 165
Cdd:cd05619   90 GGDLMFHIQSCHKFDLPRATF--YAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCK--ENMLGDAktST 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLvYRIIEGKLPPMPRDYSPELAELIRTMLSKR 245
Cdd:cd05619  166 FCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEEL-FQSIRMDNPFYPRWLEKEAKDILVKLFVRE 244
                        250       260
                 ....*....|....*....|..
gi 148839316 246 PEERPSVRSILRQPYIKRQISF 267
Cdd:cd05619  245 PERRLGVRGDIRQHPFFREINW 266
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
6-201 8.94e-25

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: 105.91  E-value: 8.94e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKE-------SWEGGDGL 78
Cdd:cd07865   14 YEKLAKIGQGTFGEVFKARHRKTGQIVALKKVLMENEKEGFPITALREIKILQLLKHENVVNLIEicrtkatPYNRYKGS 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  79 LYIVMGFCEGgDLYRKLKEQKGQL-LPENQVVewFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVL- 156
Cdd:cd07865   94 IYLVFEFCEH-DLAGLLSNKNVKFtLSEIKKV--MKMLLNGLYYIHRNKILHRDMKAANILITKDGVLKLADFGLARAFs 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 148839316 157 ---ENHCDMASTLIGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMAT 201
Cdd:cd07865  171 lakNSQPNRYTNRVVTLWYRPPElLLGERDYGPPIDMWGAGCIMAEMWT 219
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
9-249 1.07e-24

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: 107.40  E-value: 1.07e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAA-EQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGFCE 87
Cdd:cd05624   77 IKVIGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRAETACfREERNVLVNGDCQWITTLHYAFQD-ENYLYLVMDYYV 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  88 GGDLYRKLKEQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLG-IARVLENHCDMASTL 166
Cdd:cd05624  156 GGDLLTLLSKFEDKL-PEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFGsCLKMNDDGTVQSSVA 234
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 167 IGTPYYMSPELFSNK-----PYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEG----KLPPMPRDYSPELAEL 237
Cdd:cd05624  235 VGTPDYISPEILQAMedgmgKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHeerfQFPSHVTDVSEEAKDL 314
                        250
                 ....*....|..
gi 148839316 238 IRTMLSKRpEER 249
Cdd:cd05624  315 IQRLICSR-ERR 325
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
34-256 1.17e-24

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


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 104.79  E-value: 1.17e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  34 IKKLNLRNASSR----ERRAAEqEAQLLSQLKHPNIVTYKESWEGGDGLLYIVMGFCEG--GDLYRKLKEQKGQLLPENQ 107
Cdd:cd14001   33 VKKINSKCDKGQrslyQERLKE-EAKILKSLNHPNIVGFRAFTKSEDGSLCLAMEYGGKslNDLIEERYEAGLGPFPAAT 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 108 VVEWFVQIAMALQYLH-EKHILHRDLKTQNVfLTRTN--IIKVGDLGIARVLENHCDMAST----LIGTPYYMSPE-LFS 179
Cdd:cd14001  112 ILKVALSIARALEYLHnEKKILHGDIKSGNV-LIKGDfeSVKLCDFGVSLPLTENLEVDSDpkaqYVGTEPWKAKEaLEE 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 180 NKPYNYKSDVWALGCCVYEMATLK--H-------------AFNAKDMNSLVYRIIEGKLPPMPRD-YSPE---LAELIRT 240
Cdd:cd14001  191 GGVITDKADIFAYGLVLWEMMTLSvpHlnlldiedddedeSFDEDEEDEEAYYGTLGTRPALNLGeLDDSyqkVIELFYA 270
                        250
                 ....*....|....*.
gi 148839316 241 MLSKRPEERPSVRSIL 256
Cdd:cd14001  271 CTQEDPKDRPSAAHIV 286
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
9-256 1.31e-24

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: 104.20  E-value: 1.31e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLvKHRRDGKQYVIKKLNlrnASSRERRAAEQEAQLLSQLKHPNIV-----TYKESweggdglLYIVM 83
Cdd:cd05067   12 VERLGAGQFGEVWM-GYYNGHTKVAIKSLK---QGSMSPDAFLAEANLMKQLQHQRLVrlyavVTQEP-------IYIIT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  84 GFCEGGDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMA 163
Cdd:cd05067   81 EYMENGSLVDFLKTPSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLIEDNEYTA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 164 STLIGTPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIE-GKLPPMPRDYSPELAELIRTM 241
Cdd:cd05067  161 REGAKFPIkWTAPEAINYGTFTIKSDVWSFGILLTEIVTHGRIPYPGMTNPEVIQNLErGYRMPRPDNCPEELYQLMRLC 240
                        250
                 ....*....|....*...
gi 148839316 242 LSKRPEERPS---VRSIL 256
Cdd:cd05067  241 WKERPEDRPTfeyLRSVL 258
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
9-263 1.53e-24

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: 105.21  E-value: 1.53e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLNL------RNASSRErraaeqeAQLLSQLKHPNIVTYKESWEGgDGLLYIV 82
Cdd:cd06615    6 LGELGAGNGGVVTKVLHRPSGLIMARKLIHLeikpaiRNQIIRE-------LKVLHECNSPYIVGFYGAFYS-DGEISIC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  83 MGFCEGGDLYRKLKeqKGQLLPENQVVEWFVQIAMALQYLHEKH-ILHRDLKTQNVFLTRTNIIKVGDLGIARVLENhcD 161
Cdd:cd06615   78 MEHMDGGSLDQVLK--KAGRIPENILGKISIAVLRGLTYLREKHkIMHRDVKPSNILVNSRGEIKLCDFGVSGQLID--S 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 162 MASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMAT------------LKHAFNAKDMNS---------------- 213
Cdd:cd06615  154 MANSFVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIgrypipppdakeLEAMFGRPVSEGeakeshrpvsghppds 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 148839316 214 --------LVYRIIEGKLPPMPRD-YSPELAELIRTMLSKRPEERPSVRSILRQPYIKR 263
Cdd:cd06615  234 prpmaifeLLDYIVNEPPPKLPSGaFSDEFQDFVDKCLKKNPKERADLKELTKHPFIKR 292
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
12-260 1.82e-24

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: 104.12  E-value: 1.82e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGFCEGgDL 91
Cdd:cd07860    8 IGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHT-ENKLYLVFEFLHQ-DL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  92 YRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTLIGTPY 171
Cdd:cd07860   86 KKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEVVTLW 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 172 YMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRII--------------------EGKLPPMPR-- 228
Cdd:cd07860  166 YRAPEiLLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFrtlgtpdevvwpgvtsmpdyKPSFPKWARqd 245
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 148839316 229 --DYSPELAE----LIRTMLSKRPEERPSVRSILRQPY 260
Cdd:cd07860  246 fsKVVPPLDEdgrdLLSQMLHYDPNKRISAKAALAHPF 283
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
6-263 2.12e-24

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: 105.33  E-value: 2.12e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKL--NLRNASSRER--RaaeqEAQLLSQLK-HPNIV----TYKESwegGD 76
Cdd:cd07852    9 YEILKKLGKGAYGIVWKAIDKKTGEVVALKKIfdAFRNATDAQRtfR----EIMFLQELNdHPNIIkllnVIRAE---ND 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  77 GLLYIVMGFCEGgDLYRKLKeqKGqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVL 156
Cdd:cd07852   82 KDIYLVFEYMET-DLHAVIR--AN-ILEDIHKQYIMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGLARSL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 157 ENHCDMASTLIGTPY-----YMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAF-------------------NAKDM 211
Cdd:cd07852  158 SQLEEDDENPVLTDYvatrwYRAPEiLLGSTRYTKGVDMWSVGCILGEMLLGKPLFpgtstlnqlekiievigrpSAEDI 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148839316 212 NSLV----YRIIEgKLPPMPR--------DYSPELAELIRTMLSKRPEERPSVRSILRQPYIKR 263
Cdd:cd07852  238 ESIQspfaATMLE-SLPPSRPksldelfpKASPDALDLLKKLLVFNPNKRLTAEEALRHPYVAQ 300
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
6-260 2.64e-24

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: 103.65  E-value: 2.64e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGF 85
Cdd:cd07861    2 YTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIRLESEEEGVPSTAIREISLLKELQHPNIVCLEDVLMQ-ENRLYLVFEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGgDLYRKLKE-QKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMAS 164
Cdd:cd07861   81 LSM-DLKKYLDSlPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARAFGIPVRVYT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 TLIGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRII------------------------ 219
Cdd:cd07861  160 HEVVTLWYRAPEvLLGSPRYSTPVDIWSIGTIFAEMATKKPLFHGDSEIDQLFRIFrilgtptediwpgvtslpdykntf 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 148839316 220 ----EGKLPPMPRDYSPELAELIRTMLSKRPEERPSVRSILRQPY 260
Cdd:cd07861  240 pkwkKGSLRTAVKNLDEDGLDLLEKMLIYDPAKRISAKKALVHPY 284
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
9-256 2.88e-24

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


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 103.44  E-value: 2.88e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLvkHRRD------GKQYVIKKLNlRNASSRERRAAEQEAQLLSQLKHPNIVTYKESW-EGGDGLLYI 81
Cdd:cd05080    9 IRDLGEGHFGKVSL--YCYDptndgtGEMVAVKALK-ADCGPQHRSGWKQEIDILKTLYHENIVKYKGCCsEQGGKSLQL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  82 VMGFCEGGDLYRKLKEQKGQLlpeNQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIAR-VLENHC 160
Cdd:cd05080   86 IMEYVPLGSLRDYLPKHSIGL---AQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAKaVPEGHE 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 161 DMASTLIG-TP-YYMSPELFSNKPYNYKSDVWALGCCVYEMAT-----------LKHAFNAKDMNSLVYRIIE----GKL 223
Cdd:cd05080  163 YYRVREDGdSPvFWYAPECLKEYKFYYASDVWSFGVTLYELLThcdssqspptkFLEMIGIAQGQMTVVRLIEllerGER 242
                        250       260       270
                 ....*....|....*....|....*....|...
gi 148839316 224 PPMPRDYSPELAELIRTMLSKRPEERPSVRSIL 256
Cdd:cd05080  243 LPCPDKCPQEVYHLMKNCWETEASFRPTFENLI 275
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
10-262 3.28e-24

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: 104.26  E-value: 3.28e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLNLR--------NASSRERR--AAEQEAQLLSQLkhpnIVTYKESWEggdglL 79
Cdd:cd05620    1 KVLGKGSFGKVLLAELKGKGEYFAVKALKKDvvlidddvECTMVEKRvlALAWENPFLTHL----YCTFQTKEH-----L 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  80 YIVMGFCEGGDLYRKLKEqKGQlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARvlENH 159
Cdd:cd05620   72 FFVMEFLNGGDLMFHIQD-KGR-FDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCK--ENV 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 160 C--DMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLvYRIIEGKLPPMPRDYSPELAEL 237
Cdd:cd05620  148 FgdNRASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDEL-FESIRVDTPHYPRWITKESKDI 226
                        250       260
                 ....*....|....*....|....*.
gi 148839316 238 IRTMLSKRPEERPSVRSILR-QPYIK 262
Cdd:cd05620  227 LEKLFERDPTRRLGVVGNIRgHPFFK 252
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
10-258 3.90e-24

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


Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 102.88  E-value: 3.90e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEV---TLVKHRRD--GKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVtykesweggdGLL----- 79
Cdd:cd05044    1 KFLGSGAFGEVfegTAKDILGDgsGETKVAVKTLRKGATDQEKAEFLKEAHLMSNFKHPNIL----------KLLgvcld 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  80 ----YIVMGFCEGGDLY---RKLKEQKGQ--LLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTN----IIK 146
Cdd:cd05044   71 ndpqYIILELMEGGDLLsylRAARPTAFTppLLTLKDLLSICVDVAKGCVYLEDMHFVHRDLAARNCLVSSKDyrerVVK 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 147 VGDLGIARVLENHcdmastligtPYY------------MSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSL 214
Cdd:cd05044  151 IGDFGLARDIYKN----------DYYrkegegllpvrwMAPESLVDGVFTTQSDVWAFGVLMWEILTLGQQPYPARNNLE 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 148839316 215 VYRII--EGKLPPmPRDYSPELAELIRTMLSKRPEERPSVRSILRQ 258
Cdd:cd05044  221 VLHFVraGGRLDQ-PDNCPDDLYELMLRCWSTDPEERPSFARILEQ 265
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
12-260 4.33e-24

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: 103.14  E-value: 4.33e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESwEGGDGLLYIVMGFCEGgDL 91
Cdd:cd07835    7 IGEGTYGVVYKARDKLTGEIVALKKIRLETEDEGVPSTAIREISLLKELNHPNIVRLLDV-VHSENKLYLVFEFLDL-DL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  92 YRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARV----LENHCDMASTLi 167
Cdd:cd07835   85 KKYMDSSPLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLARAfgvpVRTYTHEVVTL- 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 168 gtpYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRII-------EGKLP---PMPrDY------ 230
Cdd:cd07835  164 ---WYRAPEiLLGSKHYSTPVDIWSVGCIFAEMVTRRPLFPGDSEIDQLFRIFrtlgtpdEDVWPgvtSLP-DYkptfpk 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 148839316 231 -------------SPELAELIRTMLSKRPEERPSVRSILRQPY 260
Cdd:cd07835  240 warqdlskvvpslDEDGLDLLSQMLVYDPAKRISAKAALQHPY 282
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
11-257 4.66e-24

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: 102.81  E-value: 4.66e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  11 VVGKGSYGEVtlvkHRrdGKQY---VIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKesweggdGL------LYI 81
Cdd:cd14063    7 VIGKGRFGRV----HR--GRWHgdvAIKLLNIDYLNEEQLEAFKEEVAAYKNTRHDNLVLFM-------GAcmdpphLAI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  82 VMGFCEGGDLYRKLKEQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFL--TRTNIIKVGDLGIARVL--- 156
Cdd:cd14063   74 VTSLCKGRTLYSLIHERKEKF-DFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLenGRVVITDFGLFSLSGLLqpg 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 157 -ENHCDMASTliGTPYYMSPEL----------FSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPP 225
Cdd:cd14063  153 rREDTLVIPN--GWLCYLAPEIiralspdldfEESLPFTKASDVYAFGTVWYELLAGRWPFKEQPAESIIWQVGCGKKQS 230
                        250       260       270
                 ....*....|....*....|....*....|...
gi 148839316 226 MPRDYSP-ELAELIRTMLSKRPEERPSVRSILR 257
Cdd:cd14063  231 LSQLDIGrEVKDILMQCWAYDPEKRPTFSDLLR 263
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
6-261 5.09e-24

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: 104.31  E-value: 5.09e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAeQEAQLLSQLKHPNIV---------TYKESWEggd 76
Cdd:cd07849    7 YQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKISPFEHQTYCLRTL-REIKILLRFKHENIIgildiqrppTFESFKD--- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  77 glLYIVMGFCEGgDLYRKLKEQKgqllPENQVVEWFV-QIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARV 155
Cdd:cd07849   83 --VYIVQELMET-DLYKLIKTQH----LSNDHIQYFLyQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLARI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 156 LENHCDMASTL---IGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKD----------------MNSLv 215
Cdd:cd07849  156 ADPEHDHTGFLteyVATRWYRAPEiMLNSKGYTKAIDIWSVGCILAEMLSNRPLFPGKDylhqlnlilgilgtpsQEDL- 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148839316 216 YRIIEGK-------LPPMPR--------DYSPELAELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd07849  235 NCIISLKarnyiksLPFKPKvpwnklfpNADPKALDLLDKMLTFNPHKRITVEEALAHPYL 295
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
6-261 6.31e-24

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: 101.89  E-value: 6.31e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRErrAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLYIvMGF 85
Cdd:cd14114    4 YDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPHESDKE--TVRKEIQIMNQLHHPKLINLHDAFEDDNEMVLI-LEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGGDLYRKLKEQkGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLT--RTNIIKVGDLGIARVLeNHCDMA 163
Cdd:cd14114   81 LSGGELFERIAAE-HYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTtkRSNEVKLIDFGLATHL-DPKESV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 164 STLIGTPYYMSPELFSNKPYNYKSDVWALGCCVY-------------EMATLKhafNAK----DMNSLVYRIIegklppm 226
Cdd:cd14114  159 KVTTGTAEFAAPEIVEREPVGFYTDMWAVGVLSYvllsglspfagenDDETLR---NVKscdwNFDDSAFSGI------- 228
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 148839316 227 prdySPELAELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd14114  229 ----SEEAKDFIRKLLLADPNKRMTIHQALEHPWL 259
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
9-259 7.49e-24

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: 102.41  E-value: 7.49e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQL-KHPNIVTYKESWEGGDGLLyIVMGFCE 87
Cdd:cd14138   10 LEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLgQHSHVVRYYSAWAEDDHML-IQNEYCN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  88 GGDLYRKLKE--QKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTN-------------------IIK 146
Cdd:cd14138   89 GGSLADAISEnyRIMSYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFISRTSipnaaseegdedewasnkvIFK 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 147 VGDLG-IARVLENHCDMastliGTPYYMSPELFS-NKPYNYKSDVWALGCCVYEMATLKHAFNAKDMnslVYRIIEGKLP 224
Cdd:cd14138  169 IGDLGhVTRVSSPQVEE-----GDSRFLANEVLQeNYTHLPKADIFALALTVVCAAGAEPLPTNGDQ---WHEIRQGKLP 240
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 148839316 225 PMPRDYSPELAELIRTMLSKRPEERPSVRSILRQP 259
Cdd:cd14138  241 RIPQVLSQEFLDLLKVMIHPDPERRPSAVALVKHS 275
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
12-261 8.46e-24

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: 101.62  E-value: 8.46e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKklNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLyIVMGFCEGGDL 91
Cdd:cd14191   10 LGSGKFGQVFRLVEKKTKKVWAGK--FFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIV-MVLEMVSGGEL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  92 YRKLKEQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVF-LTRTNI-IKVGDLGIARVLENHCDMaSTLIGT 169
Cdd:cd14191   87 FERIIDEDFEL-TERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTkIKLIDFGLARRLENAGSL-KVLFGT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 170 PYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPRDY---SPELAELIRTMLSKRP 246
Cdd:cd14191  165 PEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFdeiSDDAKDFISNLLKKDM 244
                        250
                 ....*....|....*
gi 148839316 247 EERPSVRSILRQPYI 261
Cdd:cd14191  245 KARLTCTQCLQHPWL 259
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
9-260 1.12e-23

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: 101.66  E-value: 1.12e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKqYVIKKLNlrnASSRERRAAEQEAQLLSQLKHPN------IVTYKESweggdglLYIV 82
Cdd:cd05072   12 VKKLGAGQFGEVWMGYYNNSTK-VAVKTLK---PGTMSVQAFLEEANLMKTLQHDKlvrlyaVVTKEEP-------IYII 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  83 MGFCEGGDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDM 162
Cdd:cd05072   81 TEYMAKGSLLDFLKSDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIEDNEYT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 163 ASTLIGTPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATL-KHAFNAKDMNSLVYRIIEGKLPPMPRDYSPELAELIRT 240
Cdd:cd05072  161 AREGAKFPIkWTAPEAINFGSFTIKSDVWSFGILLYEIVTYgKIPYPGMSNSDVMSALQRGYRMPRMENCPDELYDIMKT 240
                        250       260
                 ....*....|....*....|...
gi 148839316 241 MLSKRPEERPS---VRSILRQPY 260
Cdd:cd05072  241 CWKEKAEERPTfdyLQSVLDDFY 263
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
4-291 1.24e-23

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: 103.11  E-value: 1.24e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   4 AAYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGL----- 78
Cdd:cd07880   15 DRYRDLKQVGSGAYGTVCSALDRRTGAKVAIKKLYRPFQSELFAKRAYRELRLLKHMKHENVIGLLDVFTPDLSLdrfhd 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  79 LYIVMGFCeGGDLYRKLKEQKgqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARvlEN 158
Cdd:cd07880   95 FYLVMPFM-GTDLGKLMKHEK---LSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLAR--QT 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 159 HCDMASTLIgTPYYMSPELFSN-KPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPmPRDYSPEL-AE 236
Cdd:cd07880  169 DSEMTGYVV-TRWYRAPEVILNwMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHLDQLMEIMKVTGTP-SKEFVQKLqSE 246
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 148839316 237 LIRTMLSKRPE-ERPSVRSILrqPYIKRQISFFLEATKIKTSKNNIKNGDSQSKPF 291
Cdd:cd07880  247 DAKNYVKKLPRfRKKDFRSLL--PNANPLAVNVLEKMLVLDAESRITAAEALAHPY 300
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
10-262 1.32e-23

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: 101.48  E-value: 1.32e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVkhrRDGKQYVIKKLNLRNASSRERRAAE----QEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGF 85
Cdd:cd14117   12 RPLGKGKFGNVYLA---REKQSKFIVALKVLFKSQIEKEGVEhqlrREIEIQSHLRHPNILRLYNYFHD-RKRIYLILEY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGGDLYRKLkeQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIArvLENHCDMAST 165
Cdd:cd14117   88 APRGELYKEL--QKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWS--VHAPSLRRRT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRI--IEGKLPPMPRDYSpelAELIRTMLS 243
Cdd:cd14117  164 MCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIvkVDLKFPPFLSDGS---RDLISKLLR 240
                        250
                 ....*....|....*....
gi 148839316 244 KRPEERPSVRSILRQPYIK 262
Cdd:cd14117  241 YHPSERLPLKGVMEHPWVK 259
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
12-256 1.39e-23

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


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 101.65  E-value: 1.39e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDgkqYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDglLYIVMGFCEGGDL 91
Cdd:cd14149   20 IGSGSFGTVYKGKWHGD---VAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMTKDN--LAIVTQWCEGSSL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  92 YRKL--KEQKGQLLpenQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLE--NHCDMASTLI 167
Cdd:cd14149   95 YKHLhvQETKFQMF---QLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSrwSGSQQVEQPT 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 168 GTPYYMSPELF---SNKPYNYKSDVWALGCCVYEMATLKHAFN-AKDMNSLVYRIIEGKLPP----MPRDYSPELAELIR 239
Cdd:cd14149  172 GSILWMAPEVIrmqDNNPFSFQSDVYSYGIVLYELMTGELPYShINNRDQIIFMVGRGYASPdlskLYKNCPKAMKRLVA 251
                        250
                 ....*....|....*..
gi 148839316 240 TMLSKRPEERPSVRSIL 256
Cdd:cd14149  252 DCIKKVKEERPLFPQIL 268
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
10-283 1.90e-23

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: 102.19  E-value: 1.90e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLN---LRNASSRERRAAEQEAQLLSQlKHPNIVTYKESWEGGDGLLYiVMGFC 86
Cdd:cd05591    1 KVLGKGSFGKVMLAERKGTDEVYAIKVLKkdvILQDDDVDCTMTEKRILALAA-KHPFLTALHSCFQTKDRLFF-VMEYV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  87 EGGDLYRKLkeQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTL 166
Cdd:cd05591   79 NGGDLMFQI--QRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGKTTTTF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 167 IGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLpPMPRDYSPELAELIRTMLSKRP 246
Cdd:cd05591  157 CGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDV-LYPVWLSKEAVSILKAFMTKNP 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 148839316 247 EER----PSV---RSILRQPYIkRQISF-FLEATKIKTS-KNNIKN 283
Cdd:cd05591  236 AKRlgcvASQggeDAIRQHPFF-REIDWeALEQRKVKPPfKPKIKT 280
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
12-263 2.10e-23

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: 101.30  E-value: 2.10e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNlRNASSRERRAAEQEAQLLsQLKH--PNIVT-YKESWEGGDGLLYI-VMGFCe 87
Cdd:cd06618   23 IGSGTCGQVYKMRHKKTGHVMAVKQMR-RSGNKEENKRILMDLDVV-LKSHdcPYIVKcYGYFITDSDVFICMeLMSTC- 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  88 ggdlYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKH-ILHRDLKTQNVFLTRTNIIKVGDLGIA-RVLEnhcDMAST 165
Cdd:cd06618  100 ----LDKLLKRIQGPIPEDILGKMTVSIVKALHYLKEKHgVIHRDVKPSNILLDESGNVKLCDFGISgRLVD---SKAKT 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 -LIGTPYYMSPELFS--NKP-YNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMP---RDYSPELAELI 238
Cdd:cd06618  173 rSAGCAAYMAPERIDppDNPkYDIRADVWSLGISLVELATGQFPYRNCKTEFEVLTKILNEEPPSLppnEGFSPDFCSFV 252
                        250       260
                 ....*....|....*....|....*
gi 148839316 239 RTMLSKRPEERPSVRSILRQPYIKR 263
Cdd:cd06618  253 DLCLTKDHRYRPKYRELLQHPFIRR 277
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
6-282 3.72e-23

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: 101.90  E-value: 3.72e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKE---SWEGGDGL--LY 80
Cdd:cd07879   17 YTSLKQVGSGAYGSVCSAIDKRTGEKVAIKKLSRPFQSEIFAKRAYRELTLLKHMQHENVIGLLDvftSAVSGDEFqdFY 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  81 IVMGFceggdLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARvlenHC 160
Cdd:cd07879   97 LVMPY-----MQTDLQKIMGHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGLAR----HA 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 161 DMAST-LIGTPYYMSPELFSN-KPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRI-----------------IEG 221
Cdd:cd07879  168 DAEMTgYVVTRWYRAPEVILNwMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQIlkvtgvpgpefvqkledKAA 247
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148839316 222 K-----LPPMPR-DYS-------PELAELIRTMLSKRPEERPSVRSILRQPYIK--RQISFFLEATKIKTSKNNIK 282
Cdd:cd07879  248 KsyiksLPKYPRkDFStlfpkasPQAVDLLEKMLELDVDKRLTATEALEHPYFDsfRDADEETEQQPYDDSLENEK 323
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
52-251 4.05e-23

Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes Ack1, thirty-eight-negative kinase 1 (Tnk1), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal catalytic domain, an SH3 domain, a Cdc42-binding CRIB domain, and a proline-rich region. They are mainly expressed in brain and skeletal tissues and are involved in the regulation of cell adhesion and growth, receptor degradation, and axonal guidance. Ack1 is also associated with androgen-independent prostate cancer progression. Tnk1 regulates TNFalpha signaling and may play an important role in cell death. The Ack-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 99.72  E-value: 4.05e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  52 QEAQLLSQLKHPNIVTykesweggdglLY---------IVMGFCEGGDLYRKLKEQKGQLlPENQVVEWFVQIAMALQYL 122
Cdd:cd05040   47 KEVNAMHSLDHPNLIR-----------LYgvvlssplmMVTELAPLGSLLDRLRKDQGHF-LISTLCDYAVQIANGMAYL 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 123 HEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMastligtpYYMS-----------PELFSNKPYNYKSDVWA 191
Cdd:cd05040  115 ESKRFIHRDLAARNILLASKDKVKIGDFGLMRALPQNEDH--------YVMQehrkvpfawcaPESLKTRKFSHASDVWM 186
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148839316 192 LGCCVYEMATLKH----AFNAKDMNSLVYRiiEGKLPPMPRDYSPELAELIRTMLSKRPEERPS 251
Cdd:cd05040  187 FGVTLWEMFTYGEepwlGLNGSQILEKIDK--EGERLERPDDCPQDIYNVMLQCWAHKPADRPT 248
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
10-261 5.07e-23

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: 99.62  E-value: 5.07e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLK-HPNIVTYKESWEGGDGLLyIVMGFCEG 88
Cdd:cd14197   15 RELGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQDCRMEIIHEIAVLELAQaNPWVINLHEVYETASEMI-LVLEYAAG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  89 GDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNI---IKVGDLGIARVLENHCDMASt 165
Cdd:cd14197   94 GEIFNQCVADREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESPlgdIKIVDFGLSRILKNSEELRE- 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPRDY---SPELAELIRTML 242
Cdd:cd14197  173 IMGTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQMNVSYSEEEFehlSESAIDFIKTLL 252
                        250
                 ....*....|....*....
gi 148839316 243 SKRPEERPSVRSILRQPYI 261
Cdd:cd14197  253 IKKPENRATAEDCLKHPWL 271
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
9-255 5.13e-23

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: 99.43  E-value: 5.13e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEV--TLVKHRRdgkQYVIKKLnlRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLlYIVMGFC 86
Cdd:cd05148   11 ERKLGSGYFGEVweGLWKNRV---RVAIKIL--KSDDLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGEPV-YIITELM 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  87 EGGDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMAS-T 165
Cdd:cd05148   85 EKGSLLAFLRSPEGQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLARLIKEDVYLSSdK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 LIgtPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVY-RIIEGKLPPMPRDYSPELAELIRTMLS 243
Cdd:cd05148  165 KI--PYkWTAPEAASHGTFSTKSDVWSFGILLYEMFTYGQVPYPGMNNHEVYdQITAGYRMPCPAKCPQEIYKIMLECWA 242
                        250
                 ....*....|..
gi 148839316 244 KRPEERPSVRSI 255
Cdd:cd05148  243 AEPEDRPSFKAL 254
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
13-260 6.91e-23

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: 100.08  E-value: 6.91e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  13 GKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIV-----TYKESWEGGD--GLLYIVMGF 85
Cdd:cd07866   17 GEGTFGEVYKARQIKTGRVVALKKILMHNEKDGFPITALREIKILKKLKHPNVVplidmAVERPDKSKRkrGSVYMVTPY 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGgDLYRKLKEQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLE------NH 159
Cdd:cd07866   97 MDH-DLSGLLENPSVKL-TESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADFGLARPYDgpppnpKG 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 160 CDMAST-----LIGTPYYMSPEL-FSNKPYNYKSDVWALGCCVYEMATLKHAFNAK---DMNSLVYRII----------- 219
Cdd:cd07866  175 GGGGGTrkytnLVVTRWYRPPELlLGERRYTTAVDIWGIGCVFAEMFTRRPILQGKsdiDQLHLIFKLCgtpteetwpgw 254
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 148839316 220 ------EGKL--PPMPR-------DYSPELAELIRTMLSKRPEERPSVRSILRQPY 260
Cdd:cd07866  255 rslpgcEGVHsfTNYPRtleerfgKLGPEGLDLLSKLLSLDPYKRLTASDALEHPY 310
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
12-249 7.03e-23

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: 100.72  E-value: 7.03e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRA---AEQEAQLLSQLKH-PNIVTYKESWEGgDGLLYIVMGFCE 87
Cdd:cd05586    1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVAKKEVAhtiGERNILVRTALDEsPFIVGLKFSFQT-PTDLYLVTDYMS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  88 GGDLYRKLkeQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTLI 167
Cdd:cd05586   80 GGELFWHL--QKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSKADLTDNKTTNTFC 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 168 GTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLpPMPRD-YSPELAELIRTMLSKR 245
Cdd:cd05586  158 GTTEYLAPEvLLDEKGYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKV-RFPKDvLSDEGRSFVKGLLNRN 236

                 ....
gi 148839316 246 PEER 249
Cdd:cd05586  237 PKHR 240
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
9-249 7.26e-23

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: 100.76  E-value: 7.26e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKH---RRDGKQYVIKKLNlRNASSRERRAAEQ---EAQLLSQLKH-PNIVTYKESWEGgDGLLYI 81
Cdd:cd05614    5 LKVLGTGAYGKVFLVRKvsgHDANKLYAMKVLR-KAALVQKAKTVEHtrtERNVLEHVRQsPFLVTLHYAFQT-DAKLHL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  82 VMGFCEGGDLYRKLKEQkgQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIAR-VLENHC 160
Cdd:cd05614   83 ILDYVSGGELFTHLYQR--DHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSKeFLTEEK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 161 DMASTLIGTPYYMSPELFSNKPYNYKS-DVWALGCCVYEMATLKHAFN---AKDMNSLVYRIIEGKLPPMPRDYSPELAE 236
Cdd:cd05614  161 ERTYSFCGTIEYMAPEIIRGKSGHGKAvDWWSLGILMFELLTGASPFTlegEKNTQSEVSRRILKCDPPFPSFIGPVARD 240
                        250
                 ....*....|...
gi 148839316 237 LIRTMLSKRPEER 249
Cdd:cd05614  241 LLQKLLCKDPKKR 253
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
6-260 7.59e-23

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: 99.43  E-value: 7.59e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGF 85
Cdd:cd07839    2 YEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEGVPSSALREICLLKELKHKNIVRLYDVLHS-DKKLTLVFEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGgDLYRKLKEQKGQllPENQVVEWFV-QIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMAS 164
Cdd:cd07839   81 CDQ-DLKKYFDSCNGD--IDPEIVKSFMfQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARAFGIPVRCYS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 TLIGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATL-KHAFNAKDMNSLVYRIIE-------------GKLP----- 224
Cdd:cd07839  158 AEVVTLWYRPPDvLFGAKLYSTSIDMWSAGCIFAELANAgRPLFPGNDVDDQLKRIFRllgtpteeswpgvSKLPdykpy 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 148839316 225 PM-----------PRdYSPELAELIRTMLSKRPEERPSVRSILRQPY 260
Cdd:cd07839  238 PMypattslvnvvPK-LNSTGRDLLQNLLVCNPVQRISAEEALQHPY 283
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
11-260 9.06e-23

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: 99.27  E-value: 9.06e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  11 VVGKGSYGEVTLVKHRRDGKQYVIKKLNLrnasSRERRAAEQ----------EAQLLSQLK-HPNIVTYKESWEGgDGLL 79
Cdd:cd14181   17 VIGRGVSSVVRRCVHRHTGQEFAVKIIEV----TAERLSPEQleevrsstlkEIHILRQVSgHPSIITLIDSYES-STFI 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  80 YIVMGFCEGGDLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENH 159
Cdd:cd14181   92 FLVFDLMRRGELFDYLTEKVT--LSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFSCHLEPG 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 160 cDMASTLIGTPYYMSPELF------SNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKL---PPMPRDY 230
Cdd:cd14181  170 -EKLRELCGTPGYLAPEILkcsmdeTHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIMEGRYqfsSPEWDDR 248
                        250       260       270
                 ....*....|....*....|....*....|
gi 148839316 231 SPELAELIRTMLSKRPEERPSVRSILRQPY 260
Cdd:cd14181  249 SSTVKDLISRLLVVDPEIRLTAEQALQHPF 278
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
1-249 1.02e-22

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 100.44  E-value: 1.02e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   1 MPLAAYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAE--QEAQLLSQLKHPNIVTYKESWEGgDGL 78
Cdd:PTZ00426  27 MKYEDFNFIRTLGTGSFGRVILATYKNEDFPPVAIKRFEKSKIIKQKQVDHvfSERKILNYINHPFCVNLYGSFKD-ESY 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  79 LYIVMGFCEGGDLYRKLKEQKgqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLEN 158
Cdd:PTZ00426 106 LYLVLEFVIGGEFFTFLRRNK--RFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFAKVVDT 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 159 HcdmASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLpPMPRDYSPELAELI 238
Cdd:PTZ00426 184 R---TYTLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFYANEPLLIYQKILEGII-YFPKFLDNNCKHLM 259
                        250
                 ....*....|.
gi 148839316 239 RTMLSKRPEER 249
Cdd:PTZ00426 260 KKLLSHDLTKR 270
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
5-215 1.12e-22

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: 98.50  E-value: 1.12e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   5 AYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNAssRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLyIVMG 84
Cdd:cd14192    5 AVCPHEVLGGGRFGQVHKCTELSTGLTLAAKIIKVKGA--KEREEVKNEINIMNQLNHVNLIQLYDAFESKTNLT-LIME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGGDLYRKLKEQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRT--NIIKVGDLGIARVLENHCDM 162
Cdd:cd14192   82 YVDGGELFDRITDESYQL-TELDAILFTRQICEGVHYLHQHYILHLDLKPENILCVNStgNQIKIIDFGLARRYKPREKL 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 148839316 163 ASTLiGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAF----NAKDMNSLV 215
Cdd:cd14192  161 KVNF-GTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFlgetDAETMNNIV 216
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
12-251 1.13e-22

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: 98.37  E-value: 1.13e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVtlVKHRRDGKQYVIKKLNLRNASSR-ERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLYIVMGFCEGGD 90
Cdd:cd14064    1 IGSGSFGKV--YKGRCRNKIVAIKRYRANTYCSKsDVDMFCREVSILCRLNHPCVIQFVGACLDDPSQFAIVTQYVSGGS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  91 LYRKLKEQKGQLLPENQVVeWFVQIAMALQYLHE--KHILHRDLKTQNVFLTRTNIIKVGDLGIARVLEN-HCDMASTLI 167
Cdd:cd14064   79 LFSLLHEQKRVIDLQSKLI-IAVDVAKGMEYLHNltQPIIHRDLNSHNILLYEDGHAVVADFGESRFLQSlDEDNMTKQP 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 168 GTPYYMSPELFS-NKPYNYKSDVWALGCCVYEMAT-------LKHAFNAKDMnslVYRIIEgklPPMPRDYSPELAELIR 239
Cdd:cd14064  158 GNLRWMAPEVFTqCTRYSIKADVFSYALCLWELLTgeipfahLKPAAAAADM---AYHHIR---PPIGYSIPKPISSLLM 231
                        250
                 ....*....|..
gi 148839316 240 TMLSKRPEERPS 251
Cdd:cd14064  232 RGWNAEPESRPS 243
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
9-257 1.42e-22

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: 98.85  E-value: 1.42e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHR----RDGKQYVIKKLNlrnASSRERRAAE--QEAQLLSQLKHPNIVTYKE-SWEGGDGLLYI 81
Cdd:cd05079    9 IRDLGEGHFGKVELCRYDpegdNTGEQVAVKSLK---PESGGNHIADlkKEIEILRNLYHENIVKYKGiCTEDGGNGIKL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  82 VMGFCEGGDLYRKLKEQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLEN--- 158
Cdd:cd05079   86 IMEFLPSGSLKEYLPRNKNKI-NLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETdke 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 159 HCDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAK---------------DMNSLVYRIIEGKL 223
Cdd:cd05079  165 YYTVKDDLDSPVFWYAPECLIQSKFYIASDVWSFGVTLYELLTYCDSESSPmtlflkmigpthgqmTVTRLVRVLEEGKR 244
                        250       260       270
                 ....*....|....*....|....*....|....
gi 148839316 224 PPMPRDYSPELAELIRTMLSKRPEERPSVRSILR 257
Cdd:cd05079  245 LPRPPNCPEEVYQLMRKCWEFQPSKRTTFQNLIE 278
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
6-262 1.74e-22

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: 100.46  E-value: 1.74e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRA-AEQEAQLLSQLKHPNIVTYKESWEgGDGLLYIVMG 84
Cdd:cd05621   54 YDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSAfFWEERDIMAFANSPWVVQLFCAFQ-DDKYLYMVME 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGGDLYRKLKEQKgqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLEN----HC 160
Cdd:cd05621  133 YMPGGDLVNLMSNYD---VPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGTCMKMDEtgmvHC 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 161 DMAstlIGTPYYMSPELFSNKP----YNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLP---PMPRDYSPE 233
Cdd:cd05621  210 DTA---VGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMDHKNSlnfPDDVEISKH 286
                        250       260       270
                 ....*....|....*....|....*....|.
gi 148839316 234 LAELIRTMLSKRPEE--RPSVRSILRQPYIK 262
Cdd:cd05621  287 AKNLICAFLTDREVRlgRNGVEEIKQHPFFR 317
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
12-261 1.77e-22

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: 99.71  E-value: 1.77e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNlrnassRERRAAEQEAQLLSQL-KHPNIVTYKESWEGGDgLLYIVMGFCEGGD 90
Cdd:cd14176   27 IGVGSYSVCKRCIHKATNMEFAVKIID------KSKRDPTEEIEILLRYgQHPNIITLKDVYDDGK-YVYVVTELMKGGE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  91 LYRKLKEQKgqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLT----RTNIIKVGDLGIARVLENHCDMASTL 166
Cdd:cd14176  100 LLDKILRQK--FFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVdesgNPESIRICDFGFAKQLRAENGLLMTP 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 167 IGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAF-NAKD--MNSLVYRIIEGKLpPMPRDY----SPELAELIR 239
Cdd:cd14176  178 CYTANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFaNGPDdtPEEILARIGSGKF-SLSGGYwnsvSDTAKDLVS 256
                        250       260
                 ....*....|....*....|..
gi 148839316 240 TMLSKRPEERPSVRSILRQPYI 261
Cdd:cd14176  257 KMLHVDPHQRLTAALVLRHPWI 278
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
12-258 1.83e-22

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: 97.71  E-value: 1.83e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKqYVIKklNLRNASSRERRAAEqEAQLLSQLKHPNIVT-YKESWEGGDglLYIVMGFCEGGD 90
Cdd:cd05112   12 IGSGQFGLVHLGYWLNKDK-VAIK--TIREGAMSEEDFIE-EAEVMMKLSHPKLVQlYGVCLEQAP--ICLVFEFMEHGC 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  91 LYRKLKEQKGQLLPENqVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENhcDMASTLIGTP 170
Cdd:cd05112   86 LSDYLRTQRGLFSAET-LLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTRFVLD--DQYTSSTGTK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 171 Y---YMSPELFSNKPYNYKSDVWALGCCVYEM-ATLKHAFNAKDMNSLVYRIIEGKLPPMPRDYSPELAELIRTMLSKRP 246
Cdd:cd05112  163 FpvkWSSPEVFSFSRYSSKSDVWSFGVLMWEVfSEGKIPYENRSNSEVVEDINAGFRLYKPRLASTHVYEIMNHCWKERP 242
                        250
                 ....*....|..
gi 148839316 247 EERPSVRSILRQ 258
Cdd:cd05112  243 EDRPSFSLLLRQ 254
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
11-197 2.13e-22

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: 97.68  E-value: 2.13e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  11 VVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNasSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLyIVMGFCEGGD 90
Cdd:cd14190   11 VLGGGKFGKVHTCTEKRTGLKLAAKVINKQN--SKDKEMVLLEIQVMNQLNHRNLIQLYEAIETPNEIV-LFMEYVEGGE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  91 LYRKLKEQKGQLLPENQVVewFV-QIAMALQYLHEKHILHRDLKTQNVFLTRT--NIIKVGDLGIARVLeNHCDMASTLI 167
Cdd:cd14190   88 LFERIVDEDYHLTEVDAMV--FVrQICEGIQFMHQMRVLHLDLKPENILCVNRtgHQVKIIDFGLARRY-NPREKLKVNF 164
                        170       180       190
                 ....*....|....*....|....*....|
gi 148839316 168 GTPYYMSPELFSNKPYNYKSDVWALGCCVY 197
Cdd:cd14190  165 GTPEFLSPEVVNYDQVSFPTDMWSMGVITY 194
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
6-260 2.26e-22

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Pho85 is a multifunctional CDK in yeast. It is regulated by 10 different cyclins (Pcls) and plays a role in G1 progression, cell polarity, phosphate and glycogen metabolism, gene expression, and in signaling changes in the environment. It is not essential for yeast viability and is the functional homolog of mammalian CDK5, which plays a role in central nervous system development. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The Pho85 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 97.94  E-value: 2.26e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLrNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLyIVMGF 85
Cdd:cd07836    2 FKQLEKLGEGTYATVYKGRNRTTGEIVALKEIHL-DAEEGTPSTAIREISLMKELKHENIVRLHDVIHTENKLM-LVFEY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGgDLyRKLKEQKGQL--LPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMA 163
Cdd:cd07836   80 MDK-DL-KKYMDTHGVRgaLDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARAFGIPVNTF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 164 STLIGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAF---NAKDMNSLVYRI-----------------IEGK 222
Cdd:cd07836  158 SNEVVTLWYRAPDvLLGSRTYSTSIDIWSVGCIMAEMITGRPLFpgtNNEDQLLKIFRImgtptestwpgisqlpeYKPT 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 148839316 223 LPPMPR--------DYSPELAELIRTMLSKRPEERPSVRSILRQPY 260
Cdd:cd07836  238 FPRYPPqdlqqlfpHADPLGIDLLHRLLQLNPELRISAHDALQHPW 283
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
1-262 2.48e-22

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: 100.46  E-value: 2.48e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   1 MPLAAYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRA-AEQEAQLLSQLKHPNIVTYKESWEgGDGLL 79
Cdd:cd05622   70 MKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAfFWEERDIMAFANSPWVVQLFYAFQ-DDRYL 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  80 YIVMGFCEGGDLYRKLKEQKgqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLEN- 158
Cdd:cd05622  149 YMVMEYMPGGDLVNLMSNYD---VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKe 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 159 ---HCDMAstlIGTPYYMSPELFSNKP----YNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLP---PMPR 228
Cdd:cd05622  226 gmvRCDTA---VGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSltfPDDN 302
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 148839316 229 DYSPELAELIRTMLSKRPEE--RPSVRSILRQPYIK 262
Cdd:cd05622  303 DISKEAKNLICAFLTDREVRlgRNGVEEIKRHLFFK 338
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
10-255 2.70e-22

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: 97.92  E-value: 2.70e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTL-----VKHRRDGKQYVIKKLNlRNASSRERRAAEQEAQLLSQLKHPNIVT-YKESWEGGDglLYIVM 83
Cdd:cd05049   11 RELGEGAFGKVFLgecynLEPEQDKMLVAVKTLK-DASSPDARKDFEREAELLTNLQHENIVKfYGVCTEGDP--LLMVF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  84 GFCEGGDLYRKLK------------EQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLG 151
Cdd:cd05049   88 EYMEHGDLNKFLRshgpdaaflaseDSAPGELTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCLVGTNLVVKIGDFG 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 152 IARvlenhcDMAStligTPYY------------MSPELFSNKPYNYKSDVWALGCCVYEMATL-KHAFNAKDMNSLVYRI 218
Cdd:cd05049  168 MSR------DIYS----TDYYrvgghtmlpirwMPPESILYRKFTTESDVWSFGVVLWEIFTYgKQPWFQLSNTEVIECI 237
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 148839316 219 IEGKLPPMPRDYSPELAELIRTMLSKRPEERPSVRSI 255
Cdd:cd05049  238 TQGRLLQRPRTCPSEVYAVMLGCWKREPQQRLNIKDI 274
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
12-261 2.76e-22

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


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 98.16  E-value: 2.76e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNlrnassRERRAAEQEAQLLSQL-KHPNIVTYKESWEGGDgLLYIVMGFCEGGD 90
Cdd:cd14178   11 IGIGSYSVCKRCVHKATSTEYAVKIID------KSKRDPSEEIEILLRYgQHPNIITLKDVYDDGK-FVYLVMELMRGGE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  91 LYRKLKEQKgqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLT----RTNIIKVGDLGIARVLENHCDMASTL 166
Cdd:cd14178   84 LLDRILRQK--CFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMdesgNPESIRICDFGFAKQLRAENGLLMTP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 167 IGTPYYMSPELFSNKPYNYKSDVWALGCCVYEM-ATLKHAFNAKD--MNSLVYRIIEGKLPPMPRDY---SPELAELIRT 240
Cdd:cd14178  162 CYTANFVAPEVLKRQGYDAACDIWSLGILLYTMlAGFTPFANGPDdtPEEILARIGSGKYALSGGNWdsiSDAAKDIVSK 241
                        250       260
                 ....*....|....*....|.
gi 148839316 241 MLSKRPEERPSVRSILRQPYI 261
Cdd:cd14178  242 MLHVDPHQRLTAPQVLRHPWI 262
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
10-258 3.31e-22

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: 97.06  E-value: 3.31e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYV---IKKLNlRNASSRERRAAEQEAQLLSQLKHPNI------VTYKESweggdglLY 80
Cdd:cd05033   10 KVIGGGEFGEVCSGSLKLPGKKEIdvaIKTLK-SGYSDKQRLDFLTEASIMGQFDHPNVirlegvVTKSRP-------VM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  81 IVMGFCEGGDLYRKLKEQKGQLLPEnQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHC 160
Cdd:cd05033   82 IVTEYMENGSLDKFLRENDGKFTVT-QLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLSRRLEDSE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 161 DMASTLIG-TPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATlkhaFNAK---DM-NSLVYRIIEG--KLPPmPRDYSP 232
Cdd:cd05033  161 ATYTTKGGkIPIrWTAPEAIAYRKFTSASDVWSFGIVMWEVMS----YGERpywDMsNQDVIKAVEDgyRLPP-PMDCPS 235
                        250       260
                 ....*....|....*....|....*.
gi 148839316 233 ELAELIRTMLSKRPEERPSVRSILRQ 258
Cdd:cd05033  236 ALYQLMLDCWQKDRNERPTFSQIVST 261
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
6-260 3.44e-22

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: 96.98  E-value: 3.44e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNlRNASSRERraAEQEAQLLSQLKHPNIVTYKESWEGGDGLLyIVMGF 85
Cdd:cd14665    2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIE-RGEKIDEN--VQREIINHRSLRHPNIVRFKEVILTPTHLA-IVMEY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGGDLYRKLKeQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNI--IKVGDLGIARVLENHCDMA 163
Cdd:cd14665   78 AAGGELFERIC-NAGRF-SEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAprLKICDFGYSKSSVLHSQPK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 164 STlIGTPYYMSPELFSNKPYNYK-SDVWALGCCVYEMATLKHAF----NAKDMNSLVYRIIEGKLpPMPRDY--SPELAE 236
Cdd:cd14665  156 ST-VGTPAYIAPEVLLKKEYDGKiADVWSCGVTLYVMLVGAYPFedpeEPRNFRKTIQRILSVQY-SIPDYVhiSPECRH 233
                        250       260
                 ....*....|....*....|....
gi 148839316 237 LIRTMLSKRPEERPSVRSILRQPY 260
Cdd:cd14665  234 LISRIFVADPATRITIPEIRNHEW 257
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
41-256 3.81e-22

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: 96.66  E-value: 3.81e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  41 NASSRERRAAEQEAQL--LSQLKHPNIVTY-----KESWEGGDGLLYIVMGFCEGGDLyRKLKEQKGQLlPENQVVEWFV 113
Cdd:cd14012   34 KTSNGKKQIQLLEKELesLKKLRHPNLVSYlafsiERRGRSDGWKVYLLTEYAPGGSL-SELLDSVGSV-PLDTARRWTL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 114 QIAMALQYLHEKHILHRDLKTQNVFLTR---TNIIKVGDLGIARVLENHCDMAS-TLIGTPYYMSPELF-SNKPYNYKSD 188
Cdd:cd14012  112 QLLEALEYLHRNGVVHKSLHAGNVLLDRdagTGIVKLTDYSLGKTLLDMCSRGSlDEFKQTYWLPPELAqGSKSPTRKTD 191
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148839316 189 VWALGCCVYEMATLKHAFNAKDMNSLVyriiegklpPMPRDYSPELAELIRTMLSKRPEERPSVRSIL 256
Cdd:cd14012  192 VWDLGLLFLQMLFGLDVLEKYTSPNPV---------LVSLDLSASLQDFLSKCLSLDPKKRPTALELL 250
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
5-260 4.52e-22

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: 97.34  E-value: 4.52e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   5 AYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLrNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLYiVMG 84
Cdd:cd07870    1 SYLNLEKLGEGSYATVYKGISRINGQLVALKVISM-KTEEGVPFTAIREASLLKGLKHANIVLLHDIIHTKETLTF-VFE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGgDLYRKLKEQKGQLLPENqVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMAS 164
Cdd:cd07870   79 YMHT-DLAQYMIQHPGGLHPYN-VRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLARAKSIPSQTYS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 TLIGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAF----NAKDMNSLVYRII-------------------E 220
Cdd:cd07870  157 SEVVTLWYRPPDvLLGATDYSSALDIWGAGCIFIEMLQGQPAFpgvsDVFEQLEKIWTVLgvptedtwpgvsklpnykpE 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 148839316 221 GKLPPMPRDY---------SPELAELIRTMLSKRPEERPSVRSILRQPY 260
Cdd:cd07870  237 WFLPCKPQQLrvvwkrlsrPPKAEDLASQMLMMFPKDRISAQDALLHPY 285
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
6-260 5.86e-22

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: 98.20  E-value: 5.86e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGL-----LY 80
Cdd:cd07878   17 YQNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLSRPFQSLIHARRTYRELRLLKHMKHENVIGLLDVFTPATSIenfneVY 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  81 IVMGFCeGGDLYRKLKEQKgqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLEnhc 160
Cdd:cd07878   97 LVTNLM-GADLNNIVKCQK---LSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLARQAD--- 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 161 DMASTLIGTPYYMSPELFSN-KPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIE------------------- 220
Cdd:cd07878  170 DEMTGYVATRWYRAPEIMLNwMHYNQTVDIWSVGCIMAELLKGKALFPGNDYIDQLKRIMEvvgtpspevlkkissehar 249
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 148839316 221 ---GKLPPMP--------RDYSPELAELIRTMLSKRPEERPSVRSILRQPY 260
Cdd:cd07878  250 kyiQSLPHMPqqdlkkifRGANPLAIDLLEKMLVLDSDKRISASEALAHPY 300
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
6-264 6.11e-22

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: 97.02  E-value: 6.11e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNlrnassRERRAAEQEAQLLSQL-KHPNIVTYKESWEGGDGLlYIVMG 84
Cdd:cd14175    3 YVVKETIGVGSYSVCKRCVHKATNMEYAVKVID------KSKRDPSEEIEILLRYgQHPNIITLKDVYDDGKHV-YLVTE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGGDLYRKLKEQKgqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTN----IIKVGDLGIARVLENHC 160
Cdd:cd14175   76 LMRGGELLDKILRQK--FFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVDESgnpeSLRICDFGFAKQLRAEN 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 161 DMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFN---AKDMNSLVYRIIEGKLPPMPRDY---SPEL 234
Cdd:cd14175  154 GLLMTPCYTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFAngpSDTPEEILTRIGSGKFTLSGGNWntvSDAA 233
                        250       260       270
                 ....*....|....*....|....*....|
gi 148839316 235 AELIRTMLSKRPEERPSVRSILRQPYIKRQ 264
Cdd:cd14175  234 KDLVSKMLHVDPHQRLTAKQVLQHPWITQK 263
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
13-262 6.58e-22

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: 97.37  E-value: 6.58e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  13 GKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRErraaeqeAQLLSQLK-HPNIVTYKESWEggDGL-LYIVMGFCEGGD 90
Cdd:cd14092   15 GDGSFSVCRKCVHKKTGQEFAVKIVSRRLDTSRE-------VQLLRLCQgHPNIVKLHEVFQ--DELhTYLVMELLRGGE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  91 LYRKLKEQKgqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTN---IIKVGDLGIARVLENhCDMASTLI 167
Cdd:cd14092   86 LLERIRKKK--RFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDddaEIKIVDFGFARLKPE-NQPLKTPC 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 168 GTPYYMSPELFSNKP----YNYKSDVWALGCCVYEMATLKHAFNAKDMN----SLVYRIIEGKLP---PMPRDYSPELAE 236
Cdd:cd14092  163 FTLPYAAPEVLKQALstqgYDESCDLWSLGVILYTMLSGQVPFQSPSRNesaaEIMKRIKSGDFSfdgEEWKNVSSEAKS 242
                        250       260
                 ....*....|....*....|....*.
gi 148839316 237 LIRTMLSKRPEERPSVRSILRQPYIK 262
Cdd:cd14092  243 LIQGLLTVDPSKRLTMSELRNHPWLQ 268
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
12-260 6.88e-22

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: 98.03  E-value: 6.88e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQY---VIKKLNLRNASSRERRAAEQEAQLLSqlKHPNIVTYKESWEGGDGLlYIVMGFCEG 88
Cdd:cd05610   12 ISRGAFGKVYLGRKKNNSKLYavkVVKKADMINKNMVHQVQAERDALALS--KSPFIVHLYYSLQSANNV-YLVMEYLIG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  89 GDLyRKLKEQKGqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENH----CDMAS 164
Cdd:cd05610   89 GDV-KSLLHIYG-YFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKVTLNRelnmMDILT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 T-------------------------------------------------LIGTPYYMSPELFSNKPYNYKSDVWALGCC 195
Cdd:cd05610  167 TpsmakpkndysrtpgqvlslisslgfntptpyrtpksvrrgaarvegerILGTPDYLAPELLLGKPHGPAVDWWALGVC 246
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148839316 196 VYEMATLKHAFNaKDMNSLVYRIIEGKLPPMP---RDYSPELAELIRTMLSKRPEERPSVRSILRQPY 260
Cdd:cd05610  247 LFEFLTGIPPFN-DETPQQVFQNILNRDIPWPegeEELSVNAQNAIEILLTMDPTKRAGLKELKQHPL 313
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
6-262 7.04e-22

Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TDY subtype and is composed of Group D plant MAPKs including Arabidopsis thaliana MPK18 (AtMPK18), Oryza sativa Blast- and Wound-induced MAPK1 (OsBWMK1), OsWJUMK1 (Wound- and JA-Uninducible MAPK1), Zea mays MPK6, and the Medicago sativa TDY1 gene product. OsBWMK1 enhances resistance to pathogenic infections. It mediates stress-activated defense responses by activating a transcription factor that affects the expression of stress-related genes. AtMPK18 is involved in microtubule-related functions. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20 while Oryza sativa contains at least 17 MAPKs. Arabidopsis thaliana contains more TEY-type MAPKs than TDY-type, whereas the reverse is true for Oryza sativa. The TDY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 97.93  E-value: 7.04e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLN--LRNASSRERraAEQEAQLLSQLKHPNIVTYK------ESWEGGDg 77
Cdd:cd07859    2 YKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKINdvFEHVSDATR--ILREIKLLRLLRHPDIVEIKhimlppSRREFKD- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  78 lLYIVMGFCEGgDLYRKLKEQKgQLLPENQVVeWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLE 157
Cdd:cd07859   79 -IYVVFELMES-DLHQVIKAND-DLTPEHHQF-FLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLARVAF 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 158 NhcDMASTLIGTPY-----YMSPEL---FSNKpYNYKSDVWALGCCVYEMATLKHAFNAKDM------------------ 211
Cdd:cd07859  155 N--DTPTAIFWTDYvatrwYRAPELcgsFFSK-YTPAIDIWSIGCIFAEVLTGKPLFPGKNVvhqldlitdllgtpspet 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148839316 212 -----NSLVYRIIEGKLPPMPRDYS-------PELAELIRTMLSKRPEERPSVRSILRQPYIK 262
Cdd:cd07859  232 isrvrNEKARRYLSSMRKKQPVPFSqkfpnadPLALRLLERLLAFDPKDRPTAEEALADPYFK 294
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
9-258 7.30e-22

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: 95.82  E-value: 7.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRrdGKQYVIKklNLRNASSRERRAAEqeAQLLSQLKHPNIVTYKESWEGGDGLLYIVMGFCEG 88
Cdd:cd05082   11 LQTIGKGEFGDVMLGDYR--GNKVAVK--CIKNDATAQAFLAE--ASVMTQLRHSNLVQLLGVIVEEKGGLYIVTEYMAK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  89 GDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTLIG 168
Cdd:cd05082   85 GSLVDYLRSRGRSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEASSTQDTGKLPVK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 169 tpyYMSPELFSNKPYNYKSDVWALGCCVYEMATL-KHAFNAKDMNSLVYRIIEGKLPPMPRDYSPELAELIRTMLSKRPE 247
Cdd:cd05082  165 ---WTAPEALREKKFSTKSDVWSFGILLWEIYSFgRVPYPRIPLKDVVPRVEKGYKMDAPDGCPPAVYDVMKNCWHLDAA 241
                        250
                 ....*....|.
gi 148839316 248 ERPSVRSILRQ 258
Cdd:cd05082  242 MRPSFLQLREQ 252
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
11-260 7.84e-22

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: 96.27  E-value: 7.84e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  11 VVGKGSYGEVTLVKHRRDGKQYVIKKLNL------RNASSRERRAAEQEAQLLSQL-KHPNIVTYKESWEGgDGLLYIVM 83
Cdd:cd14093   10 ILGRGVSSTVRRCIEKETGQEFAVKIIDItgekssENEAEELREATRREIEILRQVsGHPNIIELHDVFES-PTFIFLVF 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  84 GFCEGGDLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHcDMA 163
Cdd:cd14093   89 ELCRKGELFDYLTEVVT--LSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATRLDEG-EKL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 164 STLIGTPYYMSPEL-----FSNKP-YNYKSDVWALGCCVYemaTLKHAF----NAKDMNSLvYRIIEGKL---PPMPRDY 230
Cdd:cd14093  166 RELCGTPGYLAPEVlkcsmYDNAPgYGKEVDMWACGVIMY---TLLAGCppfwHRKQMVML-RNIMEGKYefgSPEWDDI 241
                        250       260       270
                 ....*....|....*....|....*....|
gi 148839316 231 SPELAELIRTMLSKRPEERPSVRSILRQPY 260
Cdd:cd14093  242 SDTAKDLISKLLVVDPKKRLTAEEALEHPF 271
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
12-256 8.72e-22

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: 95.59  E-value: 8.72e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLrNASSRERRAAEQEAQLLSQLKHPNIV------TYKESweggdglLYIVMGF 85
Cdd:cd05041    3 IGRGNFGDVYRGVLKPDNTEVAVKTCRE-TLPPDLKRKFLQEARILKQYDHPNIVkligvcVQKQP-------IMIVMEL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGGDLYRKLKEQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARvlENHCDMAST 165
Cdd:cd05041   75 VPGGSLLTFLRKKGARL-TVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSR--EEEDGEYTV 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 LIGT---PY-YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIE--GKLPPmprdysPEL--AEL 237
Cdd:cd05041  152 SDGLkqiPIkWTAPEALNYGRYTSESDVWSFGILLWEIFSLGATPYPGMSNQQTREQIEsgYRMPA------PELcpEAV 225
                        250       260
                 ....*....|....*....|..
gi 148839316 238 IRTMLS---KRPEERPSVRSIL 256
Cdd:cd05041  226 YRLMLQcwaYDPENRPSFSEIY 247
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
5-261 1.04e-21

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: 95.37  E-value: 1.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   5 AYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRnasSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLYIvMG 84
Cdd:cd14110    4 TYAFQTEINRGRFSVVRQCEEKRSGQMLAAKIIPYK---PEDKQLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLI-EE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGGDLYRKLKEQkgQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENhcDMAS 164
Cdd:cd14110   80 LCSGPELLYNLAER--NSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLGNAQPFNQ--GKVL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 TLIGTPYY---MSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAkDMNSLVYRIIEGKLPPMPRDYsPELAE----L 237
Cdd:cd14110  156 MTDKKGDYvetMAPELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSS-DLNWERDRNIRKGKVQLSRCY-AGLSGgavnF 233
                        250       260
                 ....*....|....*....|....
gi 148839316 238 IRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd14110  234 LKSTLCAKPWGRPTASECLQNPWL 257
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
12-255 1.16e-21

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: 95.38  E-value: 1.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKklnlrnaSSRERRAAE------QEAQLLSQLKHPNIV------TYKESweggdglL 79
Cdd:cd05084    4 IGRGNFGEVFSGRLRADNTPVAVK-------SCRETLPPDlkakflQEARILKQYSHPNIVrligvcTQKQP-------I 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  80 YIVMGFCEGGDLYRKLKEQkGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENH 159
Cdd:cd05084   70 YIVMELVQGGDFLTFLRTE-GPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSREEEDG 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 160 CDMAS-TLIGTPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIE--GKLPPmPRDYSPELA 235
Cdd:cd05084  149 VYAATgGMKQIPVkWTAPEALNYGRYSSESDVWSFGILLWETFSLGAVPYANLSNQQTREAVEqgVRLPC-PENCPDEVY 227
                        250       260
                 ....*....|....*....|
gi 148839316 236 ELIRTMLSKRPEERPSVRSI 255
Cdd:cd05084  228 RLMEQCWEYDPRKRPSFSTV 247
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
12-261 1.31e-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: 97.06  E-value: 1.31e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNlrNA------SSRERRaaeqEAQLLSQLKHPNIVTYK--------ESWEGgdg 77
Cdd:cd07858   13 IGRGAYGIVCSAKNSETNEKVAIKKIA--NAfdnridAKRTLR----EIKLLRHLDHENVIAIKdimppphrEAFND--- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  78 lLYIVMGFCEGgDLYRKLKEQkgQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLE 157
Cdd:cd07858   84 -VYIVYELMDT-DLHQIIRSS--QTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLARTTS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 158 NHCDMASTLIGTPYYMSPELFSN-KPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIE---------------- 220
Cdd:cd07858  160 EKGDFMTEYVVTRWYRAPELLLNcSEYTTAIDVWSVGCIFAELLGRKPLFPGKDYVHQLKLITEllgspseedlgfirne 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 148839316 221 ------GKLPPMPR--------DYSPELAELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd07858  240 karryiRSLPYTPRqsfarlfpHANPLAIDLLEKMLVFDPSKRITVEEALAHPYL 294
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
6-260 1.44e-21

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: 95.22  E-value: 1.44e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNlrnassRERRAAEQEAQLL---SQLKHPNIVTYKESWEGGDGLLyIV 82
Cdd:cd14662    2 YELVKDIGSGNFGVARLMRNKETKELVAVKYIE------RGLKIDENVQREIinhRSLRHPNIIRFKEVVLTPTHLA-IV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  83 MGFCEGGDLYRKLKEqKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFL--TRTNIIKVGDLGIARVLENHC 160
Cdd:cd14662   75 MEYAAGGELFERICN-AGRF-SEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLdgSPAPRLKICDFGYSKSSVLHS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 161 DMASTlIGTPYYMSPELFSNKPYNYK-SDVWALGCCVYEMATLKHAF----NAKDMNSLVYRI--IEGKLPpmprDY--- 230
Cdd:cd14662  153 QPKST-VGTPAYIAPEVLSRKEYDGKvADVWSCGVTLYVMLVGAYPFedpdDPKNFRKTIQRImsVQYKIP----DYvrv 227
                        250       260       270
                 ....*....|....*....|....*....|
gi 148839316 231 SPELAELIRTMLSKRPEERPSVRSILRQPY 260
Cdd:cd14662  228 SQDCRHLLSRIFVANPAKRITIPEIKNHPW 257
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
13-251 1.71e-21

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


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 94.63  E-value: 1.71e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  13 GKGSYGEVTLVKHRrdGKQYVIKKLNlRNASSRERRaaeQEAQLLSQLKHPNIVTYKESwegGDGLLYIVMGFCEGGDLY 92
Cdd:cd14068    3 GDGGFGSVYRAVYR--GEDVAVKIFN-KHTSFRLLR---QELVVLSHLHHPSLVALLAA---GTAPRMLVMELAPKGSLD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  93 RKLKEQKGQLlpeNQVVEWFV--QIAMALQYLHEKHILHRDLKTQNV--FLTRTN---IIKVGDLGIArvlENHCDMA-S 164
Cdd:cd14068   74 ALLQQDNASL---TRTLQHRIalHVADGLRYLHSAMIIYRDLKPHNVllFTLYPNcaiIAKIADYGIA---QYCCRMGiK 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 TLIGTPYYMSPELF-SNKPYNYKSDVWALGCCVYEMATL--KHAFNAKDMNSLVYRIIEGKLPPMPRDYS----PELAEL 237
Cdd:cd14068  148 TSEGTPGFRAPEVArGNVIYNQQADVYSFGLLLYDILTCgeRIVEGLKFPNEFDELAIQGKLPDPVKEYGcapwPGVEAL 227
                        250
                 ....*....|....
gi 148839316 238 IRTMLSKRPEERPS 251
Cdd:cd14068  228 IKDCLKENPQCRPT 241
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
12-261 1.77e-21

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: 95.41  E-value: 1.77e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLK---HPNIVTYKE--SWEGGDGLLYIVMGFC 86
Cdd:cd07863    8 IGVGAYGTVYKARDPHSGHFVALKSVRVQTNEDGLPLSTVREVALLKRLEafdHPNIVRLMDvcATSRTDRETKVTLVFE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  87 E-GGDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLEnhCDMAST 165
Cdd:cd07863   88 HvDQDLRTYLDKVPPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLARIYS--CQMALT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 -LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAF---NAKDMNSLVYRIIegKLPP---MPRDYS------- 231
Cdd:cd07863  166 pVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFcgnSEADQLGKIFDLI--GLPPeddWPRDVTlprgafs 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 148839316 232 -----------PEL----AELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd07863  244 prgprpvqsvvPEIeesgAQLLLEMLTFNPHKRISAFRALQHPFF 288
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
11-258 1.87e-21

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


Pssm-ID: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 95.11  E-value: 1.87e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  11 VVGKGSYGEVTLVKHRRDGKQY--VIKKLNlRNASSRERRAAEQEAQLLSQL-KHPNIVTYKESWEGgDGLLYIVMGFCE 87
Cdd:cd05047    2 VIGEGNFGQVLKARIKKDGLRMdaAIKRMK-EYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEH-RGYLYLAIEYAP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  88 GGDLYRKLKEQK--------------GQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIA 153
Cdd:cd05047   80 HGNLLDFLRKSRvletdpafaianstASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 154 RVLENHcdMASTLIGTPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLVYRIIEGKLPPMPRDYS 231
Cdd:cd05047  160 RGQEVY--VKKTMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTpYCGMTCAELYEKLPQGYRLEKPLNCD 237
                        250       260
                 ....*....|....*....|....*..
gi 148839316 232 PELAELIRTMLSKRPEERPSVRSILRQ 258
Cdd:cd05047  238 DEVYDLMRQCWREKPYERPSFAQILVS 264
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
12-251 2.29e-21

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: 95.89  E-value: 2.29e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSReRRAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGFCEGGDL 91
Cdd:cd06650   13 LGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAI-RNQIIRELQVLHECNSPYIVGFYGAFYS-DGEISICMEHMDGGSL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  92 YRKLKeqKGQLLPENQVVEWFVQIAMALQYLHEKH-ILHRDLKTQNVFLTRTNIIKVGDLGIARVLENhcDMASTLIGTP 170
Cdd:cd06650   91 DQVLK--KAGRIPEQILGKVSIAVIKGLTYLREKHkIMHRDVKPSNILVNSRGEIKLCDFGVSGQLID--SMANSFVGTR 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 171 YYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAF---NAKDMNSLVYRIIEG---KLPPMPR-----------DYSPE 233
Cdd:cd06650  167 SYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIpppDAKELELMFGCQVEGdaaETPPRPRtpgrplssygmDSRPP 246
                        250       260
                 ....*....|....*....|
gi 148839316 234 LA--ELIRTMLSKRPEERPS 251
Cdd:cd06650  247 MAifELLDYIVNEPPPKLPS 266
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
12-255 2.35e-21

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: 95.71  E-value: 2.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERR-AAEQEAQllsqlKHPNIVTYKESWEggDGL-LYIVMGFCEGG 89
Cdd:cd14180   14 LGEGSFSVCRKCRHRQSGQEYAVKIISRRMEANTQREvAALRLCQ-----SHPNIVALHEVLH--DQYhTYLVMELLRGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  90 DLYRKLKEQkgQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFL---TRTNIIKVGDLGIARVLENHCDMASTL 166
Cdd:cd14180   87 ELLDRIKKK--ARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYadeSDGAVLKVIDFGFARLRPQGSRPLQTP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 167 IGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNS-------LVYRIIEGKLP---PMPRDYSPELAE 236
Cdd:cd14180  165 CFTLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSKRGKMfhnhaadIMHKIKEGDFSlegEAWKGVSEEAKD 244
                        250
                 ....*....|....*....
gi 148839316 237 LIRTMLSKRPEERPSVRSI 255
Cdd:cd14180  245 LVRGLLTVDPAKRLKLSEL 263
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
12-289 2.39e-21

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: 95.28  E-value: 2.39e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNlrnaSSRERRAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGFCEGGDL 91
Cdd:cd14085   11 LGRGATSVVYRCRQKGTQKPYAVKKLK----KTVDKKIVRTEIGVLLRLSHPNIIKLKEIFET-PTEISLVLELVTGGEL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  92 YRKLKEqKGqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRT---NIIKVGDLGIARVLENHCDMaSTLIG 168
Cdd:cd14085   86 FDRIVE-KG-YYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPapdAPLKIADFGLSKIVDQQVTM-KTVCG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 169 TPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVY-RIIEGK---LPPMPRDYSPELAELIRTMLSK 244
Cdd:cd14085  163 TPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYDERGDQYMFkRILNCDydfVSPWWDDVSLNAKDLVKKLIVL 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 148839316 245 RPEERPSVRSILRQPYIKRQISFFleaTKIKTSKNNIKNGDSQSK 289
Cdd:cd14085  243 DPKKRLTTQQALQHPWVTGKAANF---AHMDTAQKKLQEFNARRK 284
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
10-255 2.53e-21

Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The PDGFR subfamily consists of PDGFR alpha, PDGFR beta, KIT, CSF-1R, the mammalian FLT3, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. PDGFR kinase domains are autoinhibited by their juxtamembrane regions containing tyr residues. The binding to their ligands leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR subfamily receptors are important in the development of a variety of cells. PDGFRs are expressed in a many cells including fibroblasts, neurons, endometrial cells, mammary epithelial cells, and vascular smooth muscle cells. PDGFR signaling is critical in normal embryonic development, angiogenesis, and wound healing. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. Mammalian FLT3 plays an important role in the survival, proliferation, and differentiation of stem cells. The PDGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 95.24  E-value: 2.53e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGK-QYVIK---KLNLRNASSRERRAAEQEAQLLSQL-KHPNIVTYKESWEGGdGLLYIVMG 84
Cdd:cd05055   41 KTLGAGAFGKVVEATAYGLSKsDAVMKvavKMLKPTAHSSEREALMSELKIMSHLgNHENIVNLLGACTIG-GPILVITE 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGGDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMAS 164
Cdd:cd05055  120 YCCYGDLLNFLRRKRESFLTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTHGKIVKICDFGLARDIMNDSNYVV 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 TliGTPY----YMSPELFSNKPYNYKSDVWALGCCVYEMATLK-HAFNAKDMNSLVYRII-EGKLPPMPRDYSPELAELI 238
Cdd:cd05055  200 K--GNARlpvkWMAPESIFNCVYTFESDVWSYGILLWEIFSLGsNPYPGMPVDSKFYKLIkEGYRMAQPEHAPAEIYDIM 277
                        250
                 ....*....|....*..
gi 148839316 239 RTMLSKRPEERPSVRSI 255
Cdd:cd05055  278 KTCWDADPLKRPTFKQI 294
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
5-261 2.93e-21

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: 95.30  E-value: 2.93e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   5 AYCY--LRVVGKGSYGEVTLVKHRRDGKQYVIKKLnlRNaSSRERRAAEQEAQLLSQLKH------PNIVTYKESWEGgD 76
Cdd:cd14210   12 AYRYevLSVLGKGSFGQVVKCLDHKTGQLVAIKII--RN-KKRFHQQALVEVKILKHLNDndpddkHNIVRYKDSFIF-R 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  77 GLLYIVMgfcE--GGDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLT---RTNIiKVGDLG 151
Cdd:cd14210   88 GHLCIVF---EllSINLYELLKSNNFQGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKqpsKSSI-KVIDFG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 152 IArVLENHcdMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIE--GkLPPM--- 226
Cdd:cd14210  164 SS-CFEGE--KVYTYIQSRFYRAPEVILGLPYDTAIDMWSLGCILAELYTGYPLFPGENEEEQLACIMEvlG-VPPKsli 239
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148839316 227 ---------------PRDYS----------------------PELAELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd14210  240 dkasrrkkffdsngkPRPTTnskgkkrrpgskslaqvlkcddPSFLDFLKKCLRWDPSERMTPEEALQHPWI 311
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
1-256 3.17e-21

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: 94.32  E-value: 3.17e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   1 MPLAAYCYLRVVGKGSYGEVTLVKHRRDGKQYVikklNLRNASSRERRAAEQEAQLLSQLKHP-----NIVTYKESwegg 75
Cdd:cd05073    8 IPRESLKLEKKLGAGQFGEVWMATYNKHTKVAV----KTMKPGSMSVEAFLAEANVMKTLQHDklvklHAVVTKEP---- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  76 dglLYIVMGFCEGGDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARV 155
Cdd:cd05073   80 ---IYIITEFMAKGSLLDFLKSDEGSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 156 LENHCDMASTLIGTPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLpPMPR-DYSPE 233
Cdd:cd05073  157 IEDNEYTAREGAKFPIkWTAPEAINFGSFTIKSDVWSFGILLMEIVTYGRIPYPGMSNPEVIRALERGY-RMPRpENCPE 235
                        250       260
                 ....*....|....*....|....*....
gi 148839316 234 laELIRTML---SKRPEERPS---VRSIL 256
Cdd:cd05073  236 --ELYNIMMrcwKNRPEERPTfeyIQSVL 262
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
11-273 3.25e-21

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


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 95.07  E-value: 3.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  11 VVGKGSYGEVTLVKHRRDGKQY--VIKKLNlRNASSRERRAAEQEAQLLSQL-KHPNIVTYKESWEGgDGLLYIVMGFCE 87
Cdd:cd05089    9 VIGEGNFGQVIKAMIKKDGLKMnaAIKMLK-EFASENDHRDFAGELEVLCKLgHHPNIINLLGACEN-RGYLYIAIEYAP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  88 GGDLYRKLKEQK--------------GQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIA 153
Cdd:cd05089   87 YGNLLDFLRKSRvletdpafakehgtASTLTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVSKIADFGLS 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 154 RVLENHcdMASTLIGTPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLVYRIIEGKLPPMPRDYS 231
Cdd:cd05089  167 RGEEVY--VKKTMGRLPVrWMAIESLNYSVYTTKSDVWSFGVLLWEIVSLGGTpYCGMTCAELYEKLPQGYRMEKPRNCD 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 148839316 232 PELAELIRTMLSKRPEERPSVRSilrqpyIKRQISFFLEATK 273
Cdd:cd05089  245 DEVYELMRQCWRDRPYERPPFSQ------ISVQLSRMLEARK 280
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
12-260 3.56e-21

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: 93.95  E-value: 3.56e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYV---IKKLNlRNASSRERRAAEQEAQLLSQLKHPNIV-----TYKESWeggdgllYIVM 83
Cdd:cd05060    3 LGHGNFGSVRKGVYLMKSGKEVevaVKTLK-QEHEKAGKKEFLREASVMAQLDHPCIVrligvCKGEPL-------MLVM 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  84 GFCEGGDLYRKLkeQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLEnhcdma 163
Cdd:cd05060   75 ELAPLGPLLKYL--KKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMSRALG------ 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 164 stlIGTPYYMS------------PELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIE-GKLPPMPRDY 230
Cdd:cd05060  147 ---AGSDYYRAttagrwplkwyaPECINYGKFSSKSDVWSYGVTLWEAFSYGAKPYGEMKGPEVIAMLEsGERLPRPEEC 223
                        250       260       270
                 ....*....|....*....|....*....|...
gi 148839316 231 SPELAELIRTMLSKRPEERPS---VRSILRQPY 260
Cdd:cd05060  224 PQEIYSIMLSCWKYRPEDRPTfseLESTFRRDP 256
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
12-255 3.86e-21

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: 94.02  E-value: 3.86e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRaaeQEAQLLSQLKHPNIVTykesweggdgLL---------YIV 82
Cdd:cd05052   14 LGGGQYGEVYEGVWKKYNLTVAVKTLKEDTMEVEEFL---KEAAVMKEIKHPNLVQ----------LLgvctreppfYII 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  83 MGFCEGGDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENhcDM 162
Cdd:cd05052   81 TEFMPYGNLLDYLRECNREELNAVVLLYMATQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTG--DT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 163 ASTLIGTPY---YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMnSLVYRIIE-GKLPPMPRDYSPELAEL 237
Cdd:cd05052  159 YTAHAGAKFpikWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSpYPGIDL-SQVYELLEkGYRMERPEGCPPKVYEL 237
                        250
                 ....*....|....*...
gi 148839316 238 IRTMLSKRPEERPSVRSI 255
Cdd:cd05052  238 MRACWQWNPSDRPSFAEI 255
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
10-249 4.50e-21

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


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 94.72  E-value: 4.50e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERraaEQEAQLLSQlKHPNIVTYKESWEggDGL-LYIVMGFCEG 88
Cdd:cd14179   13 KPLGEGSFSICRKCLHKKTNQEYAVKIVSKRMEANTQR---EIAALKLCE-GHPNIVKLHEVYH--DQLhTFLVMELLKG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  89 GDLYRKLKeqKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNI---IKVGDLGIARVLENHCDMAST 165
Cdd:cd14179   87 GELLERIK--KKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESDnseIKIIDFGFARLKPPDNQPLKT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMN-------SLVYRIIEGKLP---PMPRDYSPELA 235
Cdd:cd14179  165 PCFTLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQCHDKSltctsaeEIMKKIKQGDFSfegEAWKNVSQEAK 244
                        250
                 ....*....|....
gi 148839316 236 ELIRTMLSKRPEER 249
Cdd:cd14179  245 DLIQGLLTVDPNKR 258
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
6-261 5.03e-21

Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases Sty1 and Hog1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs Sty1 from Schizosaccharomyces pombe, Hog1 from Saccharomyces cerevisiae, and similar proteins. Sty1 and Hog1 are stress-activated MAPKs that partipate in transcriptional regulation in response to stress. Sty1 is activated in response to oxidative stress, osmotic stress, and UV radiation. It is regulated by the MAP2K Wis1, which is activated by the MAP3Ks Wis4 and Win1, which receive signals of the stress condition from membrane-spanning histidine kinases Mak1-3. Activated Sty1 stabilizes the Atf1 transcription factor and induces transcription of Atf1-dependent genes of the core environmetal stress response. Hog1 is the key element in the high osmolarity glycerol (HOG) pathway and is activated upon hyperosmotic stress. Activated Hog1 accumulates in the nucleus and regulates stress-induced transcription. The HOG pathway is mediated by two transmembrane osmosensors, Sln1 and Sho1. MAPKs are important mediators of cellular responses to extracellular signals. The Sty1/Hog1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270843 [Multi-domain]  Cd Length: 328  Bit Score: 94.95  E-value: 5.03e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLYIVMGF 85
Cdd:cd07856   12 YSDLQPVGMGAFGLVCSARDQLTGQNVAVKKIMKPFSTPVLAKRTYRELKLLKHLRHENIISLSDIFISPLEDIYFVTEL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 cEGGDLYRKLKEQKgqllPENQVVEWFV-QIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHcdmAS 164
Cdd:cd07856   92 -LGTDLHRLLTSRP----LEKQFIQYFLyQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLARIQDPQ---MT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 TLIGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKD-MNSlvYRIIEGKL--PPMP------------- 227
Cdd:cd07856  164 GYVSTRYYRAPEiMLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDhVNQ--FSIITELLgtPPDDvinticsentlrf 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 148839316 228 ----------------RDYSPELAELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd07856  242 vqslpkrervpfsekfKNADPDAIDLLEKMLVFDPKKRISAAEALAHPYL 291
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
10-256 5.87e-21

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: 93.39  E-value: 5.87e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYV---IKKLNLrNASSRERRAAEQEAQLLSQLKHPNIVtYKESWEGGDGLLYIVMGFC 86
Cdd:cd05066   10 KVIGAGEFGEVCSGRLKLPGKREIpvaIKTLKA-GYTEKQRRDFLSEASIMGQFDHPNII-HLEGVVTRSKPVMIVTEYM 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  87 EGGDLYRKLKEQKGQLLPEnQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTL 166
Cdd:cd05066   88 ENGSLDAFLRKHDGQFTVI-QLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDPEAAYTT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 167 IGTPY---YMSPELFSNKPYNYKSDVWALGCCVYE-MATLKHAFNAKDMNSLVYRIIEGKLPPMPRDYSPELAELIRTML 242
Cdd:cd05066  167 RGGKIpirWTAPEAIAYRKFTSASDVWSYGIVMWEvMSYGERPYWEMSNQDVIKAIEEGYRLPAPMDCPAALHQLMLDCW 246
                        250
                 ....*....|....
gi 148839316 243 SKRPEERPSVRSIL 256
Cdd:cd05066  247 QKDRNERPKFEQIV 260
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
6-261 6.35e-21

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: 94.36  E-value: 6.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDgKQYVIKKLNLRNASSRERRA------AEQEAQLLSQLKHPNIVTYKESWEGGDGLL 79
Cdd:cd14041    8 YLLLHLLGRGGFSEVYKAFDLTE-QRYVAVKIHQLNKNWRDEKKenyhkhACREYRIHKELDHPRIVKLYDYFSLDTDSF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  80 YIVMGFCEGGDLYRKLKEQKgqLLPENQVVEWFVQIAMALQYLHEKH--ILHRDLKTQNVFL---TRTNIIKVGDLGIAR 154
Cdd:cd14041   87 CTVLEYCEGNDLDFYLKQHK--LMSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLvngTACGEIKITDFGLSK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 155 VLENH-------CDMASTLIGTPYYMSPELF--SNKP--YNYKSDVWALGC----CVYEMATLKHAFNAKDM--NSLVYR 217
Cdd:cd14041  165 IMDDDsynsvdgMELTSQGAGTYWYLPPECFvvGKEPpkISNKVDVWSVGVifyqCLYGRKPFGHNQSQQDIlqENTILK 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 148839316 218 IIEGKLPPMPrDYSPELAELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd14041  245 ATEVQFPPKP-VVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYL 287
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
3-219 6.59e-21

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: 93.92  E-value: 6.59e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   3 LAAYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAeQEAQLLSQLKHPNIVTYKESWEGgDGLLYIV 82
Cdd:cd07871    4 LETYVKLDKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTAI-REVSLLKNLKHANIVTLHDIIHT-ERCLTLV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  83 MGFCEGgDLYRKLkEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDM 162
Cdd:cd07871   82 FEYLDS-DLKQYL-DNCGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLARAKSVPTKT 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148839316 163 ASTLIGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAF---NAKDMNSLVYRII 219
Cdd:cd07871  160 YSNEVVTLWYRPPDvLLGSTEYSTPIDMWGVGCILYEMATGRPMFpgsTVKEELHLIFRLL 220
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
12-199 7.18e-21

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: 93.10  E-value: 7.18e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLnLRnASSRERRAAEQEAQLLSQLKHPNI-----VTYKesweggDGLLYIVMGFC 86
Cdd:cd14221    1 LGKGCFGQAIKVTHRETGEVMVMKEL-IR-FDEETQRTFLKEVKVMRCLEHPNVlkfigVLYK------DKRLNFITEYI 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  87 EGGDLYRKLKEQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMAS-- 164
Cdd:cd14221   73 KGGTLRGIIKSMDSHY-PWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLARLMVDEKTQPEgl 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 148839316 165 ------------TLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEM 199
Cdd:cd14221  152 rslkkpdrkkryTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEI 198
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
12-258 7.23e-21

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: 92.80  E-value: 7.23e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRrdGKQYVIKKLNlrnassRERRAAEQ---EAQLLSQLKHPNIVTYKESWEGGDGLlYIVMGFCEG 88
Cdd:cd05039   14 IGKGEFGDVMLGDYR--GQKVAVKCLK------DDSTAAQAflaEASVMTTLRHPNLVQLLGVVLEGNGL-YIVTEYMAK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  89 GDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTLIG 168
Cdd:cd05039   85 GSLVDYLRSRGRAVITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAKEASSNQDGGKLPIK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 169 tpyYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLVYRIIEGKLPPMPRDYSPELAELIRTMLSKRPE 247
Cdd:cd05039  165 ---WTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVpYPRIPLKDVVPHVEKGYRMEAPEGCPPEVYKVMKNCWELDPA 241
                        250
                 ....*....|.
gi 148839316 248 ERPSVRSILRQ 258
Cdd:cd05039  242 KRPTFKQLREK 252
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
9-259 8.70e-21

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: 93.07  E-value: 8.70e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQL-KHPNIVTYKESWEGGDGLLyIVMGFCE 87
Cdd:cd14139    5 LEKIGVGEFGSVYKCIKRLDGCVYAIKRSMRPFAGSSNEQLALHEVYAHAVLgHHPHVVRYYSAWAEDDHMI-IQNEYCN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  88 GGDLYRKLKE--QKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTN---------------------- 143
Cdd:cd14139   84 GGSLQDAISEntKSGNHFEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIFICHKMqsssgvgeevsneedeflsanv 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 144 IIKVGDLGIARVLENhcdmASTLIGTPYYMSPELFSNKpYNY--KSDVWALGCCVyemATLKHAFNAKDMNSLVYRIIEG 221
Cdd:cd14139  164 VYKIGDLGHVTSINK----PQVEEGDSRFLANEILQED-YRHlpKADIFALGLTV---ALAAGAEPLPTNGAAWHHIRKG 235
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 148839316 222 KLPPMPRDYSPELAELIRTMLSKRPEERPSVRSILRQP 259
Cdd:cd14139  236 NFPDVPQELPESFSSLLKNMIQPDPEQRPSATALARHT 273
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
11-261 8.82e-21

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: 93.05  E-value: 8.82e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  11 VVGKGSYGEVTLVKHRRDGKQYVIKKLNLRnaSSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLyIVMGFCEGGD 90
Cdd:cd14193   11 ILGGGRFGQVHKCEEKSSGLKLAAKIIKAR--SQKEKEEVKNEIEVMNQLNHANLIQLYDAFESRNDIV-LVMEYVDGGE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  91 LYRKLKEQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTR--TNIIKVGDLGIARVLENHCDMASTLiG 168
Cdd:cd14193   88 LFDRIIDENYNL-TELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSreANQVKIIDFGLARRYKPREKLRVNF-G 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 169 TPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLP---PMPRDYSPELAELIRTMLSKR 245
Cdd:cd14193  166 TPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILACQWDfedEEFADISEEAKDFISKLLIKE 245
                        250
                 ....*....|....*.
gi 148839316 246 PEERPSVRSILRQPYI 261
Cdd:cd14193  246 KSWRMSASEALKHPWL 261
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
11-258 9.88e-21

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: 92.38  E-value: 9.88e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  11 VVGKGSYGEVtlVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIV------TYKESweggdglLYIVMG 84
Cdd:cd05085    3 LLGKGNFGEV--YKGTLKDKTPVAVKTCKEDLPQELKIKFLSEARILKQYDHPNIVkligvcTQRQP-------IYIVME 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGGDLYRKLKEQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMAS 164
Cdd:cd05085   74 LVPGGDFLSFLRKKKDEL-KTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSRQEDDGVYSSS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 TLIGTPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIE-GKLPPMPRDYSPELAELIRTML 242
Cdd:cd05085  153 GLKQIPIkWTAPEALNYGRYSSESDVWSFGILLWETFSLGVCPYPGMTNQQAREQVEkGYRMSAPQRCPEDIYKIMQRCW 232
                        250
                 ....*....|....*.
gi 148839316 243 SKRPEERPSVRSILRQ 258
Cdd:cd05085  233 DYNPENRPKFSELQKE 248
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
6-260 1.09e-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: 94.34  E-value: 1.09e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGL-----LY 80
Cdd:cd07877   19 YQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDVFTPARSLeefndVY 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  81 IVMGFCeGGDLYRKLKEQKgqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARvlenHC 160
Cdd:cd07877   99 LVTHLM-GADLNNIVKCQK---LTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLAR----HT 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 161 DMAST-LIGTPYYMSPELFSN-KPYNYKSDVWALGCCVYEMATLKHAFNAKD----------------------MNSLVY 216
Cdd:cd07877  171 DDEMTgYVATRWYRAPEIMLNwMHYNQTVDIWSVGCIMAELLTGRTLFPGTDhidqlklilrlvgtpgaellkkISSESA 250
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 148839316 217 RIIEGKLPPMPR--------DYSPELAELIRTMLSKRPEERPSVRSILRQPY 260
Cdd:cd07877  251 RNYIQSLTQMPKmnfanvfiGANPLAVDLLEKMLVLDSDKRITAAQALAHAY 302
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
15-242 1.12e-20

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 92.61  E-value: 1.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  15 GSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAeqeaQLLSqlKHPN------IVTYKESWeggdgllYIVMGFCEG 88
Cdd:PHA03390  27 GKFGKVSVLKHKPTQKLFVQKIIKAKNFNAIEPMVH----QLMK--DNPNfiklyySVTTLKGH-------VLIMDYIKD 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  89 GDLYRKLKeqKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNI-IKVGDLGIARvlenHCDMASTLI 167
Cdd:PHA03390  94 GDLFDLLK--KEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRAKDrIYLCDYGLCK----IIGTPSCYD 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 168 GTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAF---NAKDMN--SLVYRIieGKLPPMPRDYSPELAELIRTML 242
Cdd:PHA03390 168 GTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFkedEDEELDleSLLKRQ--QKKLPFIKNVSKNANDFVQSML 245
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
6-250 1.12e-20

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: 93.77  E-value: 1.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGL------- 78
Cdd:cd13977    2 YSLIREVGRGSYGVVYEAVVRRTGARVAVKKIRCNAPENVELALREFWALSSIQRQHPNVIQLEECVLQRDGLaqrmshg 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  79 ----------------------------LYIVMGFCEGGDLYRKLKEQKgqllPENQVVEWFV-QIAMALQYLHEKHILH 129
Cdd:cd13977   82 ssksdlylllvetslkgercfdprsacyLWFVMEFCDGGDMNEYLLSRR----PDRQTNTSFMlQLSSALAFLHRNQIVH 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 130 RDLKTQNVFLTR---TNIIKVGDLGIARVLE------------NHCDMaSTLIGTPYYMSPELFSNKpYNYKSDVWALGC 194
Cdd:cd13977  158 RDLKPDNILISHkrgEPILKVADFGLSKVCSgsglnpeepanvNKHFL-SSACGSDFYMAPEVWEGH-YTAKADIFALGI 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 195 CVYEMA---TLKHAFNAKDM---------------------NSLVYRIIEGKLPPMPRDyspeLAELIRTMLSKRPEERP 250
Cdd:cd13977  236 IIWAMVeriTFRDGETKKELlgtyiqqgkeivplgeallenPKLELQIPLKKKKSMNDD----MKQLLRDMLAANPQERP 311
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
6-263 1.60e-20

Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs MPK1 from Saccharomyces cerevisiae, Pmk1 from Schizosaccharomyces pombe, and similar proteins. MPK1 (also called Slt2) and Pmk1 (also called Spm1) are stress-activated MAPKs that regulate the cell wall integrity pathway, and are therefore important in the maintainance of cell shape, cell wall construction, morphogenesis, and ion homeostasis. MPK1 is activated in response to cell wall stress including heat stimulation, osmotic shock, UV irradiation, and any agents that interfere with cell wall biogenesis such as chitin antagonists, caffeine, or zymolase. MPK1 is regulated by the MAP2Ks Mkk1/2, which are regulated by the MAP3K Bck1. Pmk1 is also activated by multiple stresses including elevated temperatures, hyper- or hypotonic stress, glucose deprivation, exposure to cell-wall damaging compounds, and oxidative stress. It is regulated by the MAP2K Pek1, which is regulated by the MAP3K Mkh1. MAPKs are important mediators of cellular responses to extracellular signals. The MPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 93.62  E-value: 1.60e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKH--RRDGKQYVIKKL-NLRNASSRERRAAeQEAQLLSQLK-HPNIVTYKES---WEGGDGL 78
Cdd:cd07857    2 YELIKELGQGAYGIVCSARNaeTSEEETVAIKKItNVFSKKILAKRAL-RELKLLRHFRgHKNITCLYDMdivFPGNFNE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  79 LYIVMGFCEGgDLYRKLKEqkGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIAR-VLE 157
Cdd:cd07857   81 LYLYEELMEA-DLHQIIRS--GQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLARgFSE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 158 NHCDMASTL---IGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIE------------- 220
Cdd:cd07857  158 NPGENAGFMteyVATRWYRAPEiMLSFQSYTKAIDVWSVGCILAELLGRKPVFKGKDYVDQLNQILQvlgtpdeetlsri 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 221 ------------GKLPPMP-----RDYSPELAELIRTMLSKRPEERPSVRSILRQPYIKR 263
Cdd:cd07857  238 gspkaqnyirslPNIPKKPfesifPNANPLALDLLEKLLAFDPTKRISVEEALEHPYLAI 297
pknD PRK13184
serine/threonine-protein kinase PknD;
6-272 1.61e-20

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 97.15  E-value: 1.61e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNlRNASSRE--RRAAEQEAQLLSQLKHPNIVTYKESWEGGDgLLYIVM 83
Cdd:PRK13184   4 YDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIR-EDLSENPllKKRFLREAKIAADLIHPGIVPVYSICSDGD-PVYYTM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  84 GFCEGGDLYRKLKE--QKGQL---LPENQVVEWFV----QIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIAR 154
Cdd:PRK13184  82 PYIEGYTLKSLLKSvwQKESLskeLAEKTSVGAFLsifhKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGAAI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 155 VLENHCD------------MASTL------IGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVY 216
Cdd:PRK13184 162 FKKLEEEdlldidvderniCYSSMtipgkiVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRKKGRKISY 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148839316 217 RiiEGKLPPMP----RDYSPELAELIRTMLSKRPEERPSVRSILR---QPYIKRQISFFLEAT 272
Cdd:PRK13184 242 R--DVILSPIEvapyREIPPFLSQIAMKALAVDPAERYSSVQELKqdlEPHLQGSPEWTVKAT 302
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
8-258 1.89e-20

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: 91.85  E-value: 1.89e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   8 YLRVVGKGSYGEVTLVKHRrdgKQYVIKKLNLRNASSRERRAAEqEAQLLSQLKHPNIV------TYKESweggdglLYI 81
Cdd:cd05114    8 FMKELGSGLFGVVRLGKWR---AQYKVAIKAIREGAMSEEDFIE-EAKVMMKLTHPKLVqlygvcTQQKP-------IYI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  82 VMGFCEGGDLYRKLKEQKGQLLPEnQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIAR-VLENHC 160
Cdd:cd05114   77 VTEFMENGCLLNYLRQRRGKLSRD-MLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRyVLDDQY 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 161 DMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATL-KHAFNAKDMNSLVYRIIEGKlppmpRDYSPELAELI- 238
Cdd:cd05114  156 TSSSGAKFPVKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTEgKMPFESKSNYEVVEMVSRGH-----RLYRPKLASKSv 230
                        250       260
                 ....*....|....*....|....
gi 148839316 239 -RTMLS---KRPEERPSVRSILRQ 258
Cdd:cd05114  231 yEVMYScwhEKPEGRPTFADLLRT 254
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
11-262 2.53e-20

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


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 91.45  E-value: 2.53e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  11 VVGKGSYGEVtLVKHR-RDGKQYVIKKLNlRNASSRERR-----AAEQEAQLLSQL----KHPNIVTYKESWEGGDGLLY 80
Cdd:cd14101    7 LLGKGGFGTV-YAGHRiSDGLQVAIKQIS-RNRVQQWSKlpgvnPVPNEVALLQSVgggpGHRGVIRLLDWFEIPEGFLL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  81 IVMGFCEGGDLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFL-TRTNIIKVGDLGIARVLenH 159
Cdd:cd14101   85 VLERPQHCQDLFDYITERGA--LDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVdLRTGDIKLIDFGSGATL--K 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 160 CDMASTLIGTPYYMSPELFSNKPYN-YKSDVWALGCCVYEMATLKHAFNaKDMNslvyrIIEGKlPPMPRDYSPELAELI 238
Cdd:cd14101  161 DSMYTDFDGTRVYSPPEWILYHQYHaLPATVWSLGILLYDMVCGDIPFE-RDTD-----ILKAK-PSFNKRVSNDCRSLI 233
                        250       260
                 ....*....|....*....|....
gi 148839316 239 RTMLSKRPEERPSVRSILRQPYIK 262
Cdd:cd14101  234 RSCLAYNPSDRPSLEQILLHPWMM 257
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
12-264 3.46e-20

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 92.90  E-value: 3.46e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLrNASSRERRAAEQ-------------EAQLLSQLKHPNIVTYKESWEGGDgL 78
Cdd:PTZ00024  17 LGEGTYGKVEKAYDTLTGKIVAIKKVKI-IEISNDVTKDRQlvgmcgihfttlrELKIMNEIKHENIMGLVDVYVEGD-F 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  79 LYIVMGFCEGgDLyRKLKEQKgQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIAR---- 154
Cdd:PTZ00024  95 INLVMDIMAS-DL-KKVVDRK-IRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLARrygy 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 155 -----VLENHCDMASTLIGTP-----YYMSPELF--SNKpYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIE-- 220
Cdd:PTZ00024 172 ppysdTLSKDETMQRREEMTSkvvtlWYRAPELLmgAEK-YHFAVDMWSVGCIFAELLTGKPLFPGENEIDQLGRIFEll 250
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148839316 221 -----------GKLP-------PMPRDYSPELA-------ELIRTMLSKRPEERPSVRSILRQPYIKRQ 264
Cdd:PTZ00024 251 gtpnednwpqaKKLPlyteftpRKPKDLKTIFPnasddaiDLLQSLLKLNPLERISAKEALKHEYFKSD 319
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
8-258 3.59e-20

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 91.49  E-value: 3.59e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   8 YLRVVGKGSYGEVTLVKHR----RDGKQYVIKKLnlRNASSRERRAAEQEAQLLSQLKHPNIVTYKE-SWEGGDGLLYIV 82
Cdd:cd05081    8 YISQLGKGNFGSVELCRYDplgdNTGALVAVKQL--QHSGPDQQRDFQREIQILKALHSDFIVKYRGvSYGPGRRSLRLV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  83 MGFCEGGDLYRKLKEQKGQLLPENQVVeWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENhcDM 162
Cdd:cd05081   86 MEYLPSGCLRDFLQRHRARLDASRLLL-YSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLLPL--DK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 163 ASTLIGTP-----YYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAF---------------NAKDMNSLVYRIIEGK 222
Cdd:cd05081  163 DYYVVREPgqspiFWYAPESLSDNIFSRQSDVWSFGVVLYELFTYCDKScspsaeflrmmgcerDVPALCRLLELLEEGQ 242
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 148839316 223 LPPMPRDYSPELAELIRTMLSKRPEERPSVRSILRQ 258
Cdd:cd05081  243 RLPAPPACPAEVHELMKLCWAPSPQDRPSFSALGPQ 278
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
12-260 3.65e-20

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: 90.79  E-value: 3.65e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVT--LVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTY-----KESWeggdgllYIVMG 84
Cdd:cd05116    3 LGSGNFGTVKkgYYQMKKVVKTVAVKILKNEANDPALKDELLREANVMQQLDNPYIVRMigiceAESW-------MLVME 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGGDLYRKLkeQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVL---ENHCD 161
Cdd:cd05116   76 MAELGPLNKFL--QKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKALradENYYK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 162 MASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATL-KHAFNAKDMNSLVYRIIEGKLPPMPRDYSPELAELIRT 240
Cdd:cd05116  154 AQTHGKWPVKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSYgQKPYKGMKGNEVTQMIEKGERMECPAGCPPEMYDLMKL 233
                        250       260
                 ....*....|....*....|...
gi 148839316 241 MLSKRPEERPSVRSI---LRQPY 260
Cdd:cd05116  234 CWTYDVDERPGFAAVelrLRNYY 256
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
12-251 3.73e-20

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


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 90.75  E-value: 3.73e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKqYVIKKLNLRNASSRerrAAEQEAQLLSQLKHPNIVT-YKESWEGGdglLYIVMGFCEGGD 90
Cdd:cd14203    3 LGQGCFGEVWMGTWNGTTK-VAIKTLKPGTMSPE---AFLEEAQIMKKLRHDKLVQlYAVVSEEP---IYIVTEFMSKGS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  91 LYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTLIGTP 170
Cdd:cd14203   76 LLDFLKDGEGKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQGAKFP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 171 Y-YMSPELFSNKPYNYKSDVWALGCCVYEMATlKHAFNAKDMNS--LVYRIIEGKLPPMPRDYSPELAELIRTMLSKRPE 247
Cdd:cd14203  156 IkWTAPEAALYGRFTIKSDVWSFGILLTELVT-KGRVPYPGMNNreVLEQVERGYRMPCPPGCPESLHELMCQCWRKDPE 234

                 ....
gi 148839316 248 ERPS 251
Cdd:cd14203  235 ERPT 238
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
5-260 4.05e-20

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


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 91.67  E-value: 4.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   5 AYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLrNASSRERRAAEQEAQLLSQLKHPNIVTY------KESweggdgl 78
Cdd:cd07844    1 TYKKLDKLGEGSYATVYKGRSKLTGQLVALKEIRL-EHEEGAPFTAIREASLLKDLKHANIVTLhdiihtKKT------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  79 LYIVMGFCEGgDLYRKLkEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLEN 158
Cdd:cd07844   73 LTLVFEYLDT-DLKQYM-DDCGGGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLARAKSV 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 159 HCDMASTLIGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAF----NAKDMNSLVYRII-------------- 219
Cdd:cd07844  151 PSKTYSNEVVTLWYRPPDvLLGSTEYSTSLDMWGVGCIFYEMATGRPLFpgstDVEDQLHKIFRVLgtpteetwpgvssn 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 148839316 220 EGKLPPMPRDYSPEL--------------AELIRTMLSKRPEERPSVRSILRQPY 260
Cdd:cd07844  231 PEFKPYSFPFYPPRPlinhaprldriphgEELALKFLQYEPKKRISAAEAMKHPY 285
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
12-255 4.45e-20

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: 91.18  E-value: 4.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRR---DGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLyIVMGFCEG 88
Cdd:cd05092   13 LGEGAFGKVFLAECHNllpEQDKMLVAVKALKEATESARQDFQREAELLTVLQHQHIVRFYGVCTEGEPLI-MVFEYMRH 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  89 GDLYRKLK----------EQKGQLLPE---NQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARv 155
Cdd:cd05092   92 GDLNRFLRshgpdakildGGEGQAPGQltlGQMLQIASQIASGMVYLASLHFVHRDLATRNCLVGQGLVVKIGDFGMSR- 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 156 lenhcDMAStligTPYY------------MSPELFSNKPYNYKSDVWALGCCVYEMATL-KHAFNAKDMNSLVYRIIEGK 222
Cdd:cd05092  171 -----DIYS----TDYYrvggrtmlpirwMPPESILYRKFTTESDIWSFGVVLWEIFTYgKQPWYQLSNTEAIECITQGR 241
                        250       260       270
                 ....*....|....*....|....*....|...
gi 148839316 223 LPPMPRDYSPELAELIRTMLSKRPEERPSVRSI 255
Cdd:cd05092  242 ELERPRTCPPEVYAIMQGCWQREPQQRHSIKDI 274
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
2-255 4.82e-20

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: 91.95  E-value: 4.82e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   2 PLAAYCYLRVVGKGSYGevtLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQL-KHPNIVTYKESWEGgDGLLY 80
Cdd:cd05099   19 PLGEGCFGQVVRAEAYG---IDKSRPDQTVTVAVKMLKDNATDKDLADLISEMELMKLIgKHKNIINLLGVCTQ-EGPLY 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  81 IVMGFCEGGDLYRKLKEQK---------GQLLPENQV-----VEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIK 146
Cdd:cd05099   95 VIVEYAAKGNLREFLRARRppgpdytfdITKVPEEQLsfkdlVSCAYQVARGMEYLESRRCIHRDLAARNVLVTEDNVMK 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 147 VGDLGIARVLENHCDMASTLIG-TPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLVYRIIEGKL 223
Cdd:cd05099  175 IADFGLARGVHDIDYYKKTSNGrLPVkWMAPEALFDRVYTHQSDVWSFGILMWEIFTLGGSpYPGIPVEELFKLLREGHR 254
                        250       260       270
                 ....*....|....*....|....*....|..
gi 148839316 224 PPMPRDYSPELAELIRTMLSKRPEERPSVRSI 255
Cdd:cd05099  255 MDKPSNCTHELYMLMRECWHAVPTQRPTFKQL 286
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
12-263 5.12e-20

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: 92.03  E-value: 5.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSReRRAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGFCEGGDL 91
Cdd:cd06649   13 LGAGNGGVVTKVQHKPSGLIMARKLIHLEIKPAI-RNQIIRELQVLHECNSPYIVGFYGAFYS-DGEISICMEHMDGGSL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  92 YRKLKEQKgqLLPENQVVEWFVQIAMALQYLHEKH-ILHRDLKTQNVFLTRTNIIKVGDLGIARVLENhcDMASTLIGTP 170
Cdd:cd06649   91 DQVLKEAK--RIPEEILGKVSIAVLRGLAYLREKHqIMHRDVKPSNILVNSRGEIKLCDFGVSGQLID--SMANSFVGTR 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 171 YYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAF---NAKDMNSLVYR-IIEGK------LPPMPR------------ 228
Cdd:cd06649  167 SYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYPIpppDAKELEAIFGRpVVDGEegephsISPRPRppgrpvsghgmd 246
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 229 -----------DY--------------SPELAELIRTMLSKRPEERPSVRSILRQPYIKR 263
Cdd:cd06649  247 srpamaifellDYivnepppklpngvfTPDFQEFVNKCLIKNPAERADLKMLMNHTFIKR 306
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
6-261 5.40e-20

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: 91.27  E-value: 5.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDgKQYVIKKLNLRNASSRERRA------AEQEAQLLSQLKHPNIVTYKESWEGGDGLL 79
Cdd:cd14040    8 YLLLHLLGRGGFSEVYKAFDLYE-QRYAAVKIHQLNKSWRDEKKenyhkhACREYRIHKELDHPRIVKLYDYFSLDTDTF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  80 YIVMGFCEGGDLYRKLKEQKgqLLPENQVVEWFVQIAMALQYLHE--KHILHRDLKTQNVFL---TRTNIIKVGDLGIAR 154
Cdd:cd14040   87 CTVLEYCEGNDLDFYLKQHK--LMSEKEARSIVMQIVNALRYLNEikPPIIHYDLKPGNILLvdgTACGEIKITDFGLSK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 155 VLENHC------DMASTLIGTPYYMSPELF--SNKP--YNYKSDVWALGC----CVYEMATLKHAFNAKDM--NSLVYRI 218
Cdd:cd14040  165 IMDDDSygvdgmDLTSQGAGTYWYLPPECFvvGKEPpkISNKVDVWSVGViffqCLYGRKPFGHNQSQQDIlqENTILKA 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 148839316 219 IEGKLPPMPRdYSPELAELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd14040  245 TEVQFPVKPV-VSNEAKAFIRRCLAYRKEDRFDVHQLASDPYL 286
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
12-258 5.54e-20

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: 90.65  E-value: 5.54e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAeqeaqllSQLKHPNIVT-YKESWEGGdgLLYIVMGFCEGGD 90
Cdd:cd13991   14 IGRGSFGEVHRMEDKQTGFQCAVKKVRLEVFRAEELMAC-------AGLTSPRVVPlYGAVREGP--WVNIFMDLKEGGS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  91 LYRKLKEQKgqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLT----RTNIIkvgDLGIARVLENHCDMASTL 166
Cdd:cd13991   85 LGQLIKEQG--CLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSsdgsDAFLC---DFGHAECLDPDGLGKSLF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 167 I-----GTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEgKLPPM---PRDYSPELAELI 238
Cdd:cd13991  160 TgdyipGTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPWTQYYSGPLCLKIAN-EPPPLreiPPSCAPLTAQAI 238
                        250       260
                 ....*....|....*....|
gi 148839316 239 RTMLSKRPEERPSVRSILRQ 258
Cdd:cd13991  239 QAGLRKEPVHRASAAELRRK 258
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
10-260 6.60e-20

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: 89.99  E-value: 6.60e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQ----YVIKKLNLRNASSRERRAAEQEAQLL---SQLKHPNIVTYKESWEGGDGLLyIV 82
Cdd:cd14005    6 DLLGKGGFGTVYSGVRIRDGLPvavkFVPKSRVTEWAMINGPVPVPLEIALLlkaSKPGVPGVIRLLDWYERPDGFL-LI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  83 MGF---CEggDLYRKLKEqKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLT-RTNIIKVGDLGIARVLEN 158
Cdd:cd14005   85 MERpepCQ--DLFDFITE-RGAL-SENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINlRTGEVKLIDFGCGALLKD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 159 HCdmASTLIGTPYYMSPELFSNKPYNYKS-DVWALGCCVYEMATLKHAFNAKDmnslvyRIIEGKlPPMPRDYSPELAEL 237
Cdd:cd14005  161 SV--YTDFDGTRVYSPPEWIRHGRYHGRPaTVWSLGILLYDMLCGDIPFENDE------QILRGN-VLFRPRLSKECCDL 231
                        250       260
                 ....*....|....*....|...
gi 148839316 238 IRTMLSKRPEERPSVRSILRQPY 260
Cdd:cd14005  232 ISRCLQFDPSKRPSLEQILSHPW 254
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
10-261 6.95e-20

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: 92.50  E-value: 6.95e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLN--LRNASSRERraAEQEAQLLSQLKHPNIVTYKESWEGGD----GLLYIVM 83
Cdd:cd07853    6 RPIGYGAFGVVWSVTDPRDGKRVALKKMPnvFQNLVSCKR--VFRELKMLCFFKHDNVLSALDILQPPHidpfEEIYVVT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  84 GFCEGgDLYRKLKEQkgQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLE--NHCD 161
Cdd:cd07853   84 ELMQS-DLHKIIVSP--QPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVEEpdESKH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 162 MASTLIgTPYYMSPELFSNKP-YNYKSDVWALGCCVYEMATLKHAFNAK-------------------DMNS----LVYR 217
Cdd:cd07853  161 MTQEVV-TQYYRAPEILMGSRhYTSAVDIWSVGCIFAELLGRRILFQAQspiqqldlitdllgtpsleAMRSacegARAH 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 148839316 218 IIEG--KLPPMPRDY------SPELAELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd07853  240 ILRGphKPPSLPVLYtlssqaTHEAVHLLCRMLVFDPDKRISAADALAHPYL 291
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
10-255 1.07e-19

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkB is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkB to its ligands, brain-derived neurotrophic factor (BDNF) or neurotrophin 4 (NT4), results in receptor oligomerization and activation of the catalytic domain. TrkB is broadly expressed in the nervous system and in some non-neural tissues. It plays important roles in cell proliferation, differentiation, and survival. BDNF/Trk signaling plays a key role in regulating activity-dependent synaptic plasticity. TrkB also contributes to protection against gp120-induced neuronal cell death. TrkB overexpression is associated with poor prognosis in neuroblastoma (NB) and other human cancers. It acts as a suppressor of anoikis (detachment-induced apoptosis) and contributes to tumor metastasis. The TrkB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 90.48  E-value: 1.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRR---DGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLyIVMGFC 86
Cdd:cd05093   11 RELGEGAFGKVFLAECYNlcpEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLI-MVFEYM 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  87 EGGDLYRKLKEQ--------KGQLLPE---NQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARV 155
Cdd:cd05093   90 KHGDLNKFLRAHgpdavlmaEGNRPAEltqSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRD 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 156 L--ENHCDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATL-KHAFNAKDMNSLVYRIIEGKLPPMPRDYSP 232
Cdd:cd05093  170 VysTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYgKQPWYQLSNNEVIECITQGRVLQRPRTCPK 249
                        250       260
                 ....*....|....*....|...
gi 148839316 233 ELAELIRTMLSKRPEERPSVRSI 255
Cdd:cd05093  250 EVYDLMLGCWQREPHMRLNIKEI 272
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
10-255 1.24e-19

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: 89.48  E-value: 1.24e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLlyiVMGFCEGG 89
Cdd:cd14025    2 EKVGSGGFGQVYKVRHKHWKTWLAIKCPPSLHVDDSERMELLEEAKKMEMAKFRHILPVYGICSEPVGL---VMEYMETG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  90 DLYRKLKEQKgqlLPENQVVEWFVQIAMALQYLH--EKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDM---AS 164
Cdd:cd14025   79 SLEKLLASEP---LPWELRFRIIHETAVGMNFLHcmKPPLLHLDLKPANILLDAHYHVKISDFGLAKWNGLSHSHdlsRD 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 TLIGTPYYMSPELF--SNKPYNYKSDVWALGCCVYEMATLKHAFNA-KDMNSLVYRIIEG---KLPPMPRDYSPELAELI 238
Cdd:cd14025  156 GLRGTIAYLPPERFkeKNRCPDTKHDVYSFAIVIWGILTQKKPFAGeNNILHIMVKVVKGhrpSLSPIPRQRPSECQQMI 235
                        250       260
                 ....*....|....*....|
gi 148839316 239 RTM---LSKRPEERPSVRSI 255
Cdd:cd14025  236 CLMkrcWDQDPRKRPTFQDI 255
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
13-261 1.24e-19

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: 89.49  E-value: 1.24e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  13 GKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRErraaeqeAQLLSQLKHPNIVTYKESWEGGDGLLYIVMGFCEGGDLY 92
Cdd:cd14109   13 KRAAQGAPFHVTERSTGRNFLAQLRYGDPFLMRE-------VDIHNSLDHPNIVQMHDAYDDEKLAVTVIDNLASTIELV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  93 RKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLtRTNIIKVGDLGIARVLENHcDMASTLIGTPYY 172
Cdd:cd14109   86 RDNLLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILL-QDDKLKLADFGQSRRLLRG-KLTTLIYGSPEF 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 173 MSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPRDYSP---ELAELIRTMLSKRPEER 249
Cdd:cd14109  164 VSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDRETLTNVRSGKWSFDSSPLGNisdDARDFIKKLLVYIPESR 243
                        250
                 ....*....|..
gi 148839316 250 PSVRSILRQPYI 261
Cdd:cd14109  244 LTVDEALNHPWF 255
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
10-261 1.34e-19

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


Pssm-ID: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 90.21  E-value: 1.34e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLnlrnassRERRAAEQEAQLLSQLK-HPNIVTYKESW---------EGGDGLL 79
Cdd:cd14171   12 QKLGTGISGPVRVCVKKSTGERFALKIL-------LDRPKARTEVRLHMMCSgHPNIVQIYDVYansvqfpgeSSPRARL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  80 YIVMGFCEGGDLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTN---IIKVGDLGIARVl 156
Cdd:cd14171   85 LIVMELMEGGELFDRISQHRH--FTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSedaPIKLCDFGFAKV- 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 157 eNHCDMASTLIgTPYYMSPELF---------------SNKPYNY-KS-DVWALGCCVYEMATLKHAFNAKD-----MNSL 214
Cdd:cd14171  162 -DQGDLMTPQF-TPYYVAPQVLeaqrrhrkersgiptSPTPYTYdKScDMWSLGVIIYIMLCGYPPFYSEHpsrtiTKDM 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 148839316 215 VYRIIEGKLPPMPRDY---SPELAELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd14171  240 KRKIMTGSYEFPEEEWsqiSEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
12-256 1.55e-19

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: 90.07  E-value: 1.55e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLV------KHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQL-KHPNIVTYKESWEGgDGLLYIVMG 84
Cdd:cd05098   21 LGEGCFGQVVLAeaigldKDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIgKHKNIINLLGACTQ-DGPLYVIVE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGGDLYRKLKEQK--------------GQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDL 150
Cdd:cd05098  100 YASKGNLREYLQARRppgmeycynpshnpEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIADF 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 151 GIARVLeNHCDM--ASTLIGTPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLVYRIIEGKLPPM 226
Cdd:cd05098  180 GLARDI-HHIDYykKTTNGRLPVkWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSpYPGVPVEELFKLLKEGHRMDK 258
                        250       260       270
                 ....*....|....*....|....*....|
gi 148839316 227 PRDYSPELAELIRTMLSKRPEERPSVRSIL 256
Cdd:cd05098  259 PSNCTNELYMMMRDCWHAVPSQRPTFKQLV 288
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
9-317 1.56e-19

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: 90.84  E-value: 1.56e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRA---AEQEaqLLSQLKHPNIVTYKESWEGGDGLlYIVMGF 85
Cdd:cd05598    6 IKTIGVGAFGEVSLVRKKDTNALYAMKTLRKKDVLKRNQVAhvkAERD--ILAEADNEWVVKLYYSFQDKENL-YFVMDY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGGDLYrKLKEQKGqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCD---- 161
Cdd:cd05598   83 IPGGDLM-SLLIKKG-IFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHDskyy 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 162 MASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRII----EGKLPPMPRdYSPELAEL 237
Cdd:cd05598  161 LAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAQTPAETQLKVInwrtTLKIPHEAN-LSPEAKDL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 238 IRTMLSKrPEER---PSVRSILRQPYIKRqISFfleatkiktsknniKNGDSQSKPFATVVSGEAE-SNHEVIHPQPLSS 313
Cdd:cd05598  240 ILRLCCD-AEDRlgrNGADEIKAHPFFAG-IDW--------------EKLRKQKAPYIPTIRHPTDtSNFDPVDPEKLRS 303

                 ....
gi 148839316 314 EGSQ 317
Cdd:cd05598  304 SDEE 307
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
6-261 1.58e-19

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: 89.25  E-value: 1.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVtlVK-HRRDGKQYVIKKLnLRNASSRERRAAEqEAQLLSQLK------HPNIVTYKESWEGGDGL 78
Cdd:cd14133    1 YEVLEVLGKGTFGQV--VKcYDLLTGEEVALKI-IKNNKDYLDQSLD-EIRLLELLNkkdkadKYHIVRLKDVFYFKNHL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  79 LyIVmgfCE--GGDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLT--RTNIIKVGDLGIAR 154
Cdd:cd14133   77 C-IV---FEllSQNLYEFLKQNKFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLAsySRCQIKIIDFGSSC 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 155 VLENHCdmaSTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIE--GKLPP------M 226
Cdd:cd14133  153 FLTQRL---YSYIQSRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGtiGIPPAhmldqgK 229
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 148839316 227 PRDysPELAELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd14133  230 ADD--ELFVDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
13-259 1.58e-19

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


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 89.60  E-value: 1.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  13 GKGSYGEVtlVKHRRDGKQYVIKKLNLRNASSRER-------------------RAAEQEAQLLSQLKHPNIVTYKeswe 73
Cdd:cd14000    3 GDGGFGSV--YRASYKGEPVAVKIFNKHTSSNFANvpadtmlrhlratdamknfRLLRQELTVLSHLHHPSIVYLL---- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  74 gGDGL--LYIVMGFCEGGDLYRKLKEQKGQLLPENQVVEWFV--QIAMALQYLHEKHILHRDLKTQNVFLTRTN-----I 144
Cdd:cd14000   77 -GIGIhpLMLVLELAPLGSLDHLLQQDSRSFASLGRTLQQRIalQVADGLRYLHSAMIIYRDLKSHNVLVWTLYpnsaiI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 145 IKVGDLGIARvleNHCDM-ASTLIGTPYYMSPELFS-NKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGK 222
Cdd:cd14000  156 IKIADYGISR---QCCRMgAKGSEGTPGFRAPEIARgNVIYNEKVDVFSFGMLLYEILSGGAPMVGHLKFPNEFDIHGGL 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 148839316 223 LPPMPR---DYSPELAELIRTMLSKRPEERP---SVRSILRQP 259
Cdd:cd14000  233 RPPLKQyecAPWPEVEVLMKKCWKENPQQRPtavTVVSILNSP 275
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
5-218 1.62e-19

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: 90.14  E-value: 1.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   5 AYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAeQEAQLLSQLKHPNIVTYKESWEGGDGLLyIVMG 84
Cdd:cd07869    6 SYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTAI-REASLLKGLKHANIVLLHDIIHTKETLT-LVFE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGgDLYRKLKEQKGQLLPENqVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMAS 164
Cdd:cd07869   84 YVHT-DLCQYMDKHPGGLHPEN-VKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARAKSVPSHTYS 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 148839316 165 TLIGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAF-NAKDMNSLVYRI 218
Cdd:cd07869  162 NEVVTLWYRPPDvLLGSTEYSTCLDMWGVGCIFVEMIQGVAAFpGMKDIQDQLERI 217
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
6-261 1.71e-19

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: 89.86  E-value: 1.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKE---------SWEGGD 76
Cdd:cd07864    9 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLNHRSVVNLKEivtdkqdalDFKKDK 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  77 GLLYIVMGFCEGgDLYrKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVL 156
Cdd:cd07864   89 GAFYLVFEYMDH-DLM-GLLESGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADFGLARLY 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 157 ENHCDMAST-LIGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAFNA-KDMNSL--VYRIIEG---------- 221
Cdd:cd07864  167 NSEESRPYTnKVITLWYRPPElLLGEERYGPAIDVWSCGCILGELFTKKPIFQAnQELAQLelISRLCGSpcpavwpdvi 246
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 148839316 222 KLP-----PMPRDYSPELAE-----------LIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd07864  247 KLPyfntmKPKKQYRRRLREefsfiptpaldLLDHMLTLDPSKRCTAEQALNSPWL 302
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
9-217 2.27e-19

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: 89.01  E-value: 2.27e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEV--TLVKHRRDGKQYVIKKLNLRNASSRE-RRAAEQEAQLLSQLKHPNIVTykesweggdgLLYIVMG- 84
Cdd:cd05057   12 GKVLGSGAFGTVykGVWIPEGEKVKIPVAIKVLREETGPKaNEEILDEAYVMASVDHPHLVR----------LLGICLSs 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 -------FCEGGDLYRKLKEQKGQLLPEnQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLE 157
Cdd:cd05057   82 qvqlitqLMPLGCLLDYVRNHRDNIGSQ-LLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGLAKLLD 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148839316 158 N-----HCDMASTLIGtpyYMSPELFSNKPYNYKSDVWALGCCVYEMATLK----HAFNAKDMNSLVYR 217
Cdd:cd05057  161 VdekeyHAEGGKVPIK---WMALESIQYRIYTHKSDVWSYGVTVWELMTFGakpyEGIPAVEIPDLLEK 226
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
12-248 2.46e-19

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: 89.32  E-value: 2.46e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYV-IKKLNLRNASSRERRAAEQEAQLLSQLK---HPNIVTYKE----SWEGGDGLLYIVM 83
Cdd:cd07862    9 IGEGAYGKVFKARDLKNGGRFVaLKRVRVQTGEEGMPLSTIREVAVLRHLEtfeHPNVVRLFDvctvSRTDRETKLTLVF 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  84 GFCEGgDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMA 163
Cdd:cd07862   89 EHVDQ-DLTTYLDKVPEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLARIYSFQMALT 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 164 STLIgTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPRDYSPELAeLIRTMLS 243
Cdd:cd07862  168 SVVV-TLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFRGSSDVDQLGKILDVIGLPGEEDWPRDVA-LPRQAFH 245

                 ....*
gi 148839316 244 KRPEE 248
Cdd:cd07862  246 SKSAQ 250
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
11-261 2.48e-19

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


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 89.40  E-value: 2.48e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  11 VVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERraAEQEAQLLSQLK-HPNIVTYKESWEGgDGLLYIVMGFCEGG 89
Cdd:cd14090    9 LLGEGAYASVQTCINLYTGKEYAVKIIEKHPGHSRSR--VFREVETLHQCQgHPNILQLIEYFED-DERFYLVFEKMRGG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  90 DLYRKLkEQKGQL--LPENQVVEwfvQIAMALQYLHEKHILHRDLKTQNVFLTRTNII---KVGDLGIA---RVLENHCD 161
Cdd:cd14090   86 PLLSHI-EKRVHFteQEASLVVR---DIASALDFLHDKGIAHRDLKPENILCESMDKVspvKICDFDLGsgiKLSSTSMT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 162 MAST-----LIGTPYYMSPE---LFSNKPYNY--KSDVWALGCCVYEMATLKHAF--------------NAKD-MNSLVY 216
Cdd:cd14090  162 PVTTpelltPVGSAEYMAPEvvdAFVGEALSYdkRCDLWSLGVILYIMLCGYPPFygrcgedcgwdrgeACQDcQELLFH 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 148839316 217 RIIEGKLpPMPRD----YSPELAELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd14090  242 SIQEGEY-EFPEKewshISAEAKDLISHLLVRDASQRYTAEQVLQHPWV 289
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
12-261 2.56e-19

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: 89.30  E-value: 2.56e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNlrnassRERRAAEQEAQLLSQL-KHPNIVTYKESWEGGDgLLYIVMGFCEGGD 90
Cdd:cd14177   12 IGVGSYSVCKRCIHRATNMEFAVKIID------KSKRDPSEEIEILMRYgQHPNIITLKDVYDDGR-YVYLVTELMKGGE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  91 LYRKLKEQKgqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFL----TRTNIIKVGDLGIARVLENHCDMASTL 166
Cdd:cd14177   85 LLDRILRQK--FFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYmddsANADSIRICDFGFAKQLRGENGLLLTP 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 167 IGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFnAKDMN----SLVYRIIEGKLPPMPRDY---SPELAELIR 239
Cdd:cd14177  163 CYTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPF-ANGPNdtpeEILLRIGSGKFSLSGGNWdtvSDAAKDLLS 241
                        250       260
                 ....*....|....*....|..
gi 148839316 240 TMLSKRPEERPSVRSILRQPYI 261
Cdd:cd14177  242 HMLHVDPHQRYTAEQVLKHSWI 263
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
8-261 2.68e-19

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: 88.78  E-value: 2.68e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   8 YLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLrNASSRERRAAEQEAQLLSQLKHPNIVTYKESWeGGDGLLYIVMGFCE 87
Cdd:cd06619    5 YQEILGHGNGGTVYKAYHLLTRRILAVKVIPL-DITVELQKQIMSELEILYKCDSPYIIGFYGAF-FVENRISICTEFMD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  88 GG--DLYRKLkeqkgqllPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENhcDMAST 165
Cdd:cd06619   83 GGslDVYRKI--------PEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLVN--SIAKT 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMN-------SLVYRIIEGKLPPMP-RDYSPELAEL 237
Cdd:cd06619  153 YVGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGRFPYPQIQKNqgslmplQLLQCIVDEDPPVLPvGQFSEKFVHF 232
                        250       260
                 ....*....|....*....|....
gi 148839316 238 IRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd06619  233 ITQCMRKQPKERPAPENLMDHPFI 256
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
12-255 2.72e-19

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: 88.85  E-value: 2.72e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQ--YVIKKLNLRNASSrERRAAEQEAQLLSQLKHPNIVTYKESWEGGDglLYIVMGFCEGG 89
Cdd:cd05115   12 LGSGNFGCVKKGVYKMRKKQidVAIKVLKQGNEKA-VRDEMMREAQIMHQLDNPYIVRMIGVCEAEA--LMLVMEMASGG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  90 DLYRKLKEQKGQLLPENqVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVL--ENHCDMASTLI 167
Cdd:cd05115   89 PLNKFLSGKKDEITVSN-VVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLSKALgaDDSYYKARSAG 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 168 GTPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIE-GKLPPMPRDYSPELAELIRTMLSKR 245
Cdd:cd05115  168 KWPLkWYAPECINFRKFSSRSDVWSYGVTMWEAFSYGQKPYKKMKGPEVMSFIEqGKRMDCPAECPPEMYALMSDCWIYK 247
                        250
                 ....*....|
gi 148839316 246 PEERPSVRSI 255
Cdd:cd05115  248 WEDRPNFLTV 257
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
12-226 2.88e-19

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: 89.47  E-value: 2.88e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLN----LRNASSRERraaeqEAQLLSQLKHPNIV---TYKESWEGGDGLlyIVMG 84
Cdd:cd13988    1 LGQGATANVFRGRHKKTGDLYAVKVFNnlsfMRPLDVQMR-----EFEVLKKLNHKNIVklfAIEEELTTRHKV--LVME 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGGDLYRKLKEQKGQL-LPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLT----RTNIIKVGDLGIARVLENH 159
Cdd:cd13988   74 LCPCGSLYTVLEEPSNAYgLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMRVigedGQSVYKLTDFGAARELEDD 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148839316 160 CDMAStLIGTPYYMSPELF--------SNKPYNYKSDVWALGCCVYEMATLKHAF----NAKDMNSLVYRIIEGKLPPM 226
Cdd:cd13988  154 EQFVS-LYGTEEYLHPDMYeravlrkdHQKKYGATVDLWSIGVTFYHAATGSLPFrpfeGPRRNKEVMYKIITGKPSGA 231
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
12-255 3.22e-19

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


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 88.59  E-value: 3.22e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKqYVIKKLNlrnASSRERRAAEQEAQLLSQLKHPNIVTYKESWEggDGLLYIVMGFCEGGDL 91
Cdd:cd05069   20 LGQGCFGEVWMGTWNGTTK-VAIKTLK---PGTMMPEAFLQEAQIMKKLRHDKLVPLYAVVS--EEPIYIVTEFMGKGSL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  92 YRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTLIGTPY 171
Cdd:cd05069   94 LDFLKEGDGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQGAKFPI 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 172 -YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIE-GKLPPMPRDYSPELAELIRTMLSKRPEER 249
Cdd:cd05069  174 kWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMVNREVLEQVErGYRMPCPQGCPESLHELMKLCWKKDPDER 253

                 ....*.
gi 148839316 250 PSVRSI 255
Cdd:cd05069  254 PTFEYI 259
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
12-258 3.50e-19

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: 88.14  E-value: 3.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRnassrERRAAEQEAQllSQLKHPNIVTYKES--WeggDGLLYIVMGFCEGG 89
Cdd:cd13995   12 IPRGAFGKVYLAQDTKTKKRMACKLIPVE-----QFKPSDVEIQ--ACFRHENIAELYGAllW---EETVHLFMEAGEGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  90 DLYRKLkEQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVgDLGIARVLENHCDMASTLIGT 169
Cdd:cd13995   82 SVLEKL-ESCGPM-REFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAVLV-DFGLSVQMTEDVYVPKDLRGT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 170 PYYMSPELFSNKPYNYKSDVWALGCCVYEMAT----LKHAFNAKDMNSLVYrIIEGKLPPM---PRDYSPELAELIRTML 242
Cdd:cd13995  159 EIYMSPEVILCRGHNTKADIYSLGATIIHMQTgsppWVRRYPRSAYPSYLY-IIHKQAPPLediAQDCSPAMRELLEAAL 237
                        250
                 ....*....|....*.
gi 148839316 243 SKRPEERPSVRSILRQ 258
Cdd:cd13995  238 ERNPNHRSSAAELLKH 253
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
9-251 3.72e-19

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: 88.23  E-value: 3.72e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEV--------TLVkhrrdgkqyVIKKLNLRNASSRERRAaeqEAQLLSQLKHPNIV------TYKESweg 74
Cdd:cd05068   13 LRKLGSGQFGEVweglwnntTPV---------AVKTLKPGTMDPEDFLR---EAQIMKKLRHPKLIqlyavcTLEEP--- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  75 gdglLYIVMGFCEGGDLYRKLKEQKGQL-LPenQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIA 153
Cdd:cd05068   78 ----IYIITELMKHGSLLEYLQGKGRSLqLP--QLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFGLA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 154 RVLENHcDMASTLIGTPY---YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIE-GKLPPMPRD 229
Cdd:cd05068  152 RVIKVE-DEYEAREGAKFpikWTAPEAANYNRFSIKSDVWSFGILLTEIVTYGRIPYPGMTNAEVLQQVErGYRMPCPPN 230
                        250       260
                 ....*....|....*....|..
gi 148839316 230 YSPELAELIRTMLSKRPEERPS 251
Cdd:cd05068  231 CPPQLYDIMLECWKADPMERPT 252
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
8-256 4.41e-19

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: 87.63  E-value: 4.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   8 YLRVVGKGSYGEVTLVKHRrdGKQYVIKKLnLRNASSRERRAAEqEAQLLSQLKHPNIVTY-----KESweggdgLLYIV 82
Cdd:cd05113    8 FLKELGTGQFGVVKYGKWR--GQYDVAIKM-IKEGSMSEDEFIE-EAKVMMNLSHEKLVQLygvctKQR------PIFII 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  83 MGFCEGGDLYRKLKEQKGQLLPEnQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIAR-VLEnhcD 161
Cdd:cd05113   78 TEYMANGCLLNYLREMRKRFQTQ-QLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRyVLD---D 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 162 MASTLIGTPY---YMSPELFSNKPYNYKSDVWALGCCVYEMATL-KHAFNAKDMNSLVYRIIEGKlppmpRDYSPELA-- 235
Cdd:cd05113  154 EYTSSVGSKFpvrWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSLgKMPYERFTNSETVEHVSQGL-----RLYRPHLAse 228
                        250       260
                 ....*....|....*....|....
gi 148839316 236 ELIRTMLS---KRPEERPSVRSIL 256
Cdd:cd05113  229 KVYTIMYScwhEKADERPTFKILL 252
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
9-263 5.39e-19

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: 89.36  E-value: 5.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAA-EQEAQLLSQLKHPNIVTYKESWEgGDGLLYIVMGFCE 87
Cdd:cd05596   31 IKVIGRGAFGEVQLVRHKSTKKVYAMKLLSKFEMIKRSDSAFfWEERDIMAHANSEWIVQLHYAFQ-DDKYLYMVMDYMP 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  88 GGDLYRKLKEQKgqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIA-RVLEN---HCDMA 163
Cdd:cd05596  110 GGDLVNLMSNYD---VPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFGTCmKMDKDglvRSDTA 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 164 stlIGTPYYMSPELFSNKP----YNYKSDVWALGCCVYEMATLKHAFNA--------KDM---NSLVYriiegklpPMPR 228
Cdd:cd05596  187 ---VGTPDYISPEVLKSQGgdgvYGRECDWWSVGVFLYEMLVGDTPFYAdslvgtygKIMnhkNSLQF--------PDDV 255
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 148839316 229 DYSPELAELIRTMLSKRPEE--RPSVRSILRQPYIKR 263
Cdd:cd05596  256 EISKDAKSLICAFLTDREVRlgRNGIEEIKAHPFFKN 292
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
9-249 6.30e-19

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: 89.52  E-value: 6.30e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRA-AEQEAQLLSQLKHPNIVTYKESWEGGDgLLYIVMGFCE 87
Cdd:cd05629    6 VKVIGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMFKKDQLAhVKAERDVLAESDSPWVVSLYYSFQDAQ-YLYLIMEFLP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  88 GGDLYRKLKeqKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIA-------------R 154
Cdd:cd05629   85 GGDLMTMLI--KYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGLStgfhkqhdsayyqK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 155 VLE----------------------------------NHCDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMA 200
Cdd:cd05629  163 LLQgksnknridnrnsvavdsinltmsskdqiatwkkNRRLMAYSTVGTPDYIAPEIFLQQGYGQECDWWSLGAIMFECL 242
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 148839316 201 TLKHAFNAKDMNSLVYRIIEGKLP-PMPRD--YSPELAELIRTMLSKrPEER 249
Cdd:cd05629  243 IGWPPFCSENSHETYRKIINWRETlYFPDDihLSVEAEDLIRRLITN-AENR 293
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
11-262 6.66e-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: 88.16  E-value: 6.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  11 VVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERraAEQEAQLLSQLK-HPNIVTYKESWEGgDGLLYIVMGFCEGG 89
Cdd:cd14174    9 LLGEGAYAKVQGCVSLQNGKEYAVKIIEKNAGHSRSR--VFREVETLYQCQgNKNILELIEFFED-DTRFYLVFEKLRGG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  90 DLYRKLKEQKgqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNV---FLTRTNIIKVG--DLGIARVLENHCDMA- 163
Cdd:cd14174   86 SILAHIQKRK--HFNEREASRVVRDIASALDFLHTKGIAHRDLKPENIlceSPDKVSPVKICdfDLGSGVKLNSACTPIt 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 164 ----STLIGTPYYMSP---ELFSNKP--YNYKSDVWALGCCVYEMATLKHAFNAK---------------DMNSLVYRII 219
Cdd:cd14174  164 tpelTTPCGSAEYMAPevvEVFTDEAtfYDKRCDLWSLGVILYIMLSGYPPFVGHcgtdcgwdrgevcrvCQNKLFESIQ 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 148839316 220 EGKLPPMPRDY---SPELAELIRTMLSKRPEERPSVRSILRQPYIK 262
Cdd:cd14174  244 EGKYEFPDKDWshiSSEAKDLISKLLVRDAKERLSAAQVLQHPWVQ 289
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
12-199 7.12e-19

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK2 activation is induced by transforming growth factor-beta l (TGFb-l) and shares the same subcellular location as the cofilin family member twinfilin, which may be its biological substrate. LIMK2 plays a role in spermatogenesis, and may contribute to tumor progression and metastasis formation in some cancer cells. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 87.69  E-value: 7.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLnLRnASSRERRAAEQEAQLLSQLKHPNI-----VTYKesweggDGLLYIVMGFC 86
Cdd:cd14222    1 LGKGFFGQAIKVTHKATGKVMVMKEL-IR-CDEETQKTFLTEVKVMRSLDHPNVlkfigVLYK------DKRLNLLTEFI 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  87 EGGDLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVL---------- 156
Cdd:cd14222   73 EGGTLKDFLRADDP--FPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveekkkpppd 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 148839316 157 ----------ENHCDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEM 199
Cdd:cd14222  151 kpttkkrtlrKNDRKKRYTVVGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCEI 203
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
11-251 8.90e-19

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: 87.51  E-value: 8.90e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  11 VVGKGSYGEV---TLVKHRRDGKQYVIKKLnLRNASSRERRAAEQEAQLLSQLKHPNIVT-YKESWEGGDG--LLYIVMG 84
Cdd:cd05043   13 LLQEGTFGRIfhgILRDEKGKEEEVLVKTV-KDHASEIQVTMLLQESSLLYGLSHQNLLPiLHVCIEDGEKpmVLYPYMN 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FcegGDLYRKLK------EQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVL-- 156
Cdd:cd05043   92 W---GNLKLFLQqcrlseANNPQALSTQQLVHMALQIACGMSYLHRRGVIHKDIAARNCVIDDELQVKITDNALSRDLfp 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 157 -ENHC--DMASTLIGtpyYMSPELFSNKPYNYKSDVWALGCCVYEMATL-KHAFNAKDMNSLVYRIIEGKLPPMPRDYSP 232
Cdd:cd05043  169 mDYHClgDNENRPIK---WMSLESLVNKEYSSASDVWSFGVLLWELMTLgQTPYVEIDPFEMAAYLKDGYRLAQPINCPD 245
                        250
                 ....*....|....*....
gi 148839316 233 ELAELIRTMLSKRPEERPS 251
Cdd:cd05043  246 ELFAVMACCWALDPEERPS 264
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
12-251 9.52e-19

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


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 87.44  E-value: 9.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLvKHRRDGKQYVIKKLNLRNASSRerrAAEQEAQLLSQLKHPNIVTYKESWEggDGLLYIVMGFCEGGDL 91
Cdd:cd05071   17 LGQGCFGEVWM-GTWNGTTRVAIKTLKPGTMSPE---AFLQEAQVMKKLRHEKLVQLYAVVS--EEPIYIVTEYMSKGSL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  92 YRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTLIGTPY 171
Cdd:cd05071   91 LDFLKGEMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAKFPI 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 172 -YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIE-GKLPPMPRDYSPELAELIRTMLSKRPEER 249
Cdd:cd05071  171 kWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVErGYRMPCPPECPESLHDLMCQCWRKEPEER 250

                 ..
gi 148839316 250 PS 251
Cdd:cd05071  251 PT 252
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
11-249 9.69e-19

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: 87.11  E-value: 9.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  11 VVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRA-AEQEAQLLSQLKH----PNIVTYKESWEGGDGLLYIvMGF 85
Cdd:cd05606    1 IIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETlALNERIMLSLVSTggdcPFIVCMTYAFQTPDKLCFI-LDL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGGDLYRKLKeQKGqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIArvlenhCDMAST 165
Cdd:cd05606   80 MNGGDLHYHLS-QHG-VFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLA------CDFSKK 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 L----IGTPYYMSPELFSN-KPYNYKSDVWALGCCVYEMATLKHAF---NAKDMNSlVYRIIEGKLPPMPRDYSPELAEL 237
Cdd:cd05606  152 KphasVGTHGYMAPEVLQKgVAYDSSADWFSLGCMLYKLLKGHSPFrqhKTKDKHE-IDRMTLTMNVELPDSFSPELKSL 230
                        250
                 ....*....|..
gi 148839316 238 IRTMLSKRPEER 249
Cdd:cd05606  231 LEGLLQRDVSKR 242
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
12-279 9.95e-19

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: 87.22  E-value: 9.95e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRNAssrERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLYIvMGFCEGGDL 91
Cdd:cd14104    8 LGRGQFGIVHRCVETSSKKTYMAKFVKVKGA---DQVLVKKEISILNIARHRNILRLHESFESHEELVMI-FEFISGVDI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  92 YRKLKEQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLT--RTNIIKVGDLGIARVLENHcDMASTLIGT 169
Cdd:cd14104   84 FERITTARFEL-NEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCtrRGSYIKIIEFGQSRQLKPG-DKFRLQYTS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 170 PYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLP---PMPRDYSPELAELIRTMLSKRP 246
Cdd:cd14104  162 AEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAEYAfddEAFKNISIEALDFVDRLLVKER 241
                        250       260       270
                 ....*....|....*....|....*....|...
gi 148839316 247 EERPSVRSILRQPYIKRQISfFLEATKIKTSKN 279
Cdd:cd14104  242 KSRMTAQEALNHPWLKQGME-TVSSKDIKTTRH 273
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
12-197 9.97e-19

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: 86.88  E-value: 9.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRnasSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLyIVMGFCEGGDL 91
Cdd:cd14108   10 IGRGAFSYLRRVKEKSSDLSFAAKFIPVR---AKKKTSARRELALLAELDHKSIVRFHDAFEKRRVVI-IVTELCHEELL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  92 YRKLKEQKgqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFL--TRTNIIKVGDLGIARVL----ENHCDMast 165
Cdd:cd14108   86 ERITKRPT---VCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMadQKTDQVRICDFGNAQELtpnePQYCKY--- 159
                        170       180       190
                 ....*....|....*....|....*....|..
gi 148839316 166 liGTPYYMSPELFSNKPYNYKSDVWALGCCVY 197
Cdd:cd14108  160 --GTPEFVAPEIVNQSPVSKVTDIWPVGVIAY 189
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
12-255 1.30e-18

Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The FGFR subfamily consists of FGFR1, FGFR2, FGFR3, FGFR4, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, and to heparin/heparan sulfate (HS) results in the formation of a ternary complex, which leads to receptor dimerization and activation, and intracellular signaling. There are at least 23 FGFs and four types of FGFRs. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. FGF/FGFR signaling is important in the regulation of embryonic development, homeostasis, and regenerative processes. Depending on the cell type and stage, FGFR signaling produces diverse cellular responses including proliferation, growth arrest, differentiation, and apoptosis. Aberrant signaling leads to many human diseases such as skeletal, olfactory, and metabolic disorders, as well as cancer. The FGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 87.09  E-value: 1.30e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTL-----VKHRRDGKQYVIKKLNLRNASSRERraaeqeAQLLSQL-------KHPNIV------Tykeswe 73
Cdd:cd05053   20 LGEGAFGQVVKaeavgLDNKPNEVVTVAVKMLKDDATEKDL------SDLVSEMemmkmigKHKNIInllgacT------ 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  74 gGDGLLYIVMGFCEGGDLYRKLKEQK---------GQLLPENQ-----VVEWFVQIAMALQYLHEKHILHRDLKTQNVFL 139
Cdd:cd05053   88 -QDGPLYVVVEYASKGNLREFLRARRppgeeaspdDPRVPEEQltqkdLVSFAYQVARGMEYLASKKCIHRDLAARNVLV 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 140 TRTNIIKVGDLGIARVLeNHCDM--ASTLIGTPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLV 215
Cdd:cd05053  167 TEDNVMKIADFGLARDI-HHIDYyrKTTNGRLPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSpYPGIPVEELF 245
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 148839316 216 YRIIEGKLPPMPRDYSPELAELIRTMLSKRPEERPSVRSI 255
Cdd:cd05053  246 KLLKEGHRMEKPQNCTQELYMLMRDCWHEVPSQRPTFKQL 285
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
10-255 1.33e-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: 87.33  E-value: 1.33e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVtlVK------HRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVM 83
Cdd:cd05045    6 KTLGEGEFGKV--VKatafrlKGRAGYTTVAVKMLKENASSSELRDLLSEFNLLKQVNHPHVIKLYGACSQ-DGPLLLIV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  84 GFCEGGDLYRKLKEQKG----------------------QLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTR 141
Cdd:cd05045   83 EYAKYGSLRSFLRESRKvgpsylgsdgnrnssyldnpdeRALTMGDLISFAWQISRGMQYLAEMKLVHRDLAARNVLVAE 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 142 TNIIKVGDLGIAR-VLENHCDMASTLIGTPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATL-KHAFNAKDMNSLVYRI 218
Cdd:cd05045  163 GRKMKISDFGLSRdVYEEDSYVKRSKGRIPVkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLgGNPYPGIAPERLFNLL 242
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 148839316 219 IEGKLPPMPRDYSPELAELIRTMLSKRPEERPSVRSI 255
Cdd:cd05045  243 KTGYRMERPENCSEEMYNLMLTCWKQEPDKRPTFADI 279
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
9-256 1.54e-18

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: 86.75  E-value: 1.54e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRR----DGKQYV-IKKLNLR---NASSRERRaaeqEAQLLSQLKHPNIVTYKesweggdGLL- 79
Cdd:cd05046   10 ITTLGRGEFGEVFLAKAKGieeeGGETLVlVKALQKTkdeNLQSEFRR----ELDMFRKLSHKNVVRLL-------GLCr 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  80 -----YIVMGFCEGGDLYR-------KLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKV 147
Cdd:cd05046   79 eaephYMILEYTDLGDLKQflratksKDEKLKPPPLSTKQKVALCTQIALGMDHLSNARFVHRDLAARNCLVSSQREVKV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 148 GDLGIARVLEN--HCDMASTLIgtPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATL-KHAFNAKDMNSLVYRIIEGKL 223
Cdd:cd05046  159 SLLSLSKDVYNseYYKLRNALI--PLrWLAPEAVQEDDFSTKSDVWSFGVLMWEVFTQgELPFYGLSDEEVLNRLQAGKL 236
                        250       260       270
                 ....*....|....*....|....*....|....
gi 148839316 224 PPMPRDYSPE-LAELIRTMLSKRPEERPSVRSIL 256
Cdd:cd05046  237 ELPVPEGCPSrLYKLMTRCWAVNPKDRPSFSELV 270
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
11-256 1.84e-18

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: 86.08  E-value: 1.84e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  11 VVGKGSYGEVTLVKHRRDGK--QYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVtYKESWEGGDGLLYIVMGFCEG 88
Cdd:cd05065   11 VIGAGEFGEVCRGRLKLPGKreIFVAIKTLKSGYTEKQRRDFLSEASIMGQFDHPNII-HLEGVVTKSRPVMIITEFMEN 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  89 GDLYRKLKEQKGQLLPeNQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCD---MAST 165
Cdd:cd05065   90 GALDSFLRQNDGQFTV-IQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLEDDTSdptYTSS 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 LIGT-PY-YMSPELFSNKPYNYKSDVWALGCCVYEMATlkhaFNAK---DM-NSLVYRIIEG--KLPPmPRDYSPELAEL 237
Cdd:cd05065  169 LGGKiPIrWTAPEAIAYRKFTSASDVWSYGIVMWEVMS----YGERpywDMsNQDVINAIEQdyRLPP-PMDCPTALHQL 243
                        250
                 ....*....|....*....
gi 148839316 238 IRTMLSKRPEERPSVRSIL 256
Cdd:cd05065  244 MLDCWQKDRNLRPKFGQIV 262
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
12-256 2.28e-18

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


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 86.99  E-value: 2.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLV------KHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQL-KHPNIVTYKESWEGgDGLLYIVMG 84
Cdd:cd05101   32 LGEGCFGQVVMAeavgidKDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIgKHKNIINLLGACTQ-DGPLYVIVE 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGGDLYRKLKEQKG---------QLLPENQ-----VVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDL 150
Cdd:cd05101  111 YASKGNLREYLRARRPpgmeysydiNRVPEEQmtfkdLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMKIADF 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 151 GIARVLENHCDMASTLIGT-PY-YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLVYRIIEGKLPPMP 227
Cdd:cd05101  191 GLARDINNIDYYKKTTNGRlPVkWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSpYPGIPVEELFKLLKEGHRMDKP 270
                        250       260
                 ....*....|....*....|....*....
gi 148839316 228 RDYSPELAELIRTMLSKRPEERPSVRSIL 256
Cdd:cd05101  271 ANCTNELYMMMRDCWHAVPSQRPTFKQLV 299
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
89-260 2.79e-18

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: 85.09  E-value: 2.79e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  89 GDLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLT---RTnIIKVGDLGIARVLENHCDMAST 165
Cdd:cd14022   69 GDMHSFVRTCKK--LREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKdeeRT-RVKLESLEDAYILRGHDDSLSD 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 LIGTPYYMSPELF-SNKPYNYKS-DVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPpMPRDYSPELAELIRTMLS 243
Cdd:cd14022  146 KHGCPAYVSPEILnTSGSYSGKAaDVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFN-IPETLSPKAKCLIRSILR 224
                        170
                 ....*....|....*..
gi 148839316 244 KRPEERPSVRSILRQPY 260
Cdd:cd14022  225 REPSERLTSQEILDHPW 241
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
12-256 3.18e-18

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: 87.00  E-value: 3.18e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLV------KHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQL-KHPNIVTYKESWEGgDGLLYIVMG 84
Cdd:cd05100   20 LGEGCFGQVVMAeaigidKDKPNKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQ-DGPLYVLVE 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGGDLYRKLKEQKGQ---------LLPENQV-----VEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDL 150
Cdd:cd05100   99 YASKGNLREYLRARRPPgmdysfdtcKLPEEQLtfkdlVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADF 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 151 GIARVLENHCDMASTLIGT-PY-YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLVYRIIEGKLPPMP 227
Cdd:cd05100  179 GLARDVHNIDYYKKTTNGRlPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSpYPGIPVEELFKLLKEGHRMDKP 258
                        250       260
                 ....*....|....*....|....*....
gi 148839316 228 RDYSPELAELIRTMLSKRPEERPSVRSIL 256
Cdd:cd05100  259 ANCTHELYMIMRECWHAVPSQRPTFKQLV 287
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
52-251 4.57e-18

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: 85.12  E-value: 4.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  52 QEAQLLSQLKHPNIVTYKESWEggDGLLYIVMGFCEGGDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRD 131
Cdd:cd05070   53 EEAQIMKKLKHDKLVQLYAVVS--EEPIYIVTEYMSKGSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRD 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 132 LKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTLIGTPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATlKHAFNAKD 210
Cdd:cd05070  131 LRSANILVGNGLICKIADFGLARLIEDNEYTARQGAKFPIkWTAPEAALYGRFTIKSDVWSFGILLTELVT-KGRVPYPG 209
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 148839316 211 MNS--LVYRIIEGKLPPMPRDYSPELAELIRTMLSKRPEERPS 251
Cdd:cd05070  210 MNNreVLEQVERGYRMPCPQDCPISLHELMIHCWKKDPEERPT 252
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
12-199 4.76e-18

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: 87.01  E-value: 4.76e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSR-ERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLlYIVMGFCEGGD 90
Cdd:cd05600   19 VGQGGYGSVFLARKKDTGEICALKIMKKKVLFKLnEVNHVLTERDILTTTNSPWLVKLLYAFQDPENV-YLAMEYVPGGD 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  91 lYRKLKEQKGqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIAR---------------- 154
Cdd:cd05600   98 -FRTLLNNSG-ILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGLASgtlspkkiesmkirle 175
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148839316 155 ---------------------VLENHCDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEM 199
Cdd:cd05600  176 evkntafleltakerrniyraMRKEDQNYANSVVGSPDYMAPEVLRGEGYDLTVDYWSLGCILFEC 241
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
12-258 5.19e-18

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: 84.49  E-value: 5.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNlrnaSSRERRAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGFCEGGDL 91
Cdd:cd14156    1 IGSGFFSKVYKVTHGATGKVMVVKIYK----NDVDQHKIVREISLLQKLSHPNIVRYLGICVK-DEKLHPILEYVSGGCL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  92 YRKLKEQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIK---VGDLGIARVL----ENHCDMAS 164
Cdd:cd14156   76 EELLAREELPL-SWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGReavVTDFGLAREVgempANDPERKL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 TLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAfNAKDMN-----SLVYRIIEGKLPPMPrdysPELAELIR 239
Cdd:cd14156  155 SLVGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEILARIPA-DPEVLPrtgdfGLDVQAFKEMVPGCP----EPFLDLAA 229
                        250
                 ....*....|....*....
gi 148839316 240 TMLSKRPEERPSVRSILRQ 258
Cdd:cd14156  230 SCCRMDAFKRPSFAELLDE 248
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
10-256 6.77e-18

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: 84.64  E-value: 6.77e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYV---IKKLNlRNASSRERRAAEQEAQLLSQLKHPNIV-------TYKEsweggdglL 79
Cdd:cd05063   11 KVIGAGEFGEVFRGILKMPGRKEVavaIKTLK-PGYTEKQRQDFLSEASIMGQFSHHNIIrlegvvtKFKP--------A 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  80 YIVMGFCEGGDLYRKLKEQKGQLLPEnQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENH 159
Cdd:cd05063   82 MIITEYMENGALDKYLRDHDGEFSSY-QLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRVLEDD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 160 CDMASTLIGTPY---YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRII-EGKLPPMPRDYSPELA 235
Cdd:cd05063  161 PEGTYTTSGGKIpirWTAPEAIAYRKFTSASDVWSFGIVMWEVMSFGERPYWDMSNHEVMKAInDGFRLPAPMDCPSAVY 240
                        250       260
                 ....*....|....*....|.
gi 148839316 236 ELIRTMLSKRPEERPSVRSIL 256
Cdd:cd05063  241 QLMLQCWQQDRARRPRFVDIV 261
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
12-262 8.06e-18

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 84.87  E-value: 8.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGgDGLLYIVMGFCEGgDL 91
Cdd:PLN00009  10 IGEGTYGVVYKARDRVTNETIALKKIRLEQEDEGVPSTAIREISLLKEMQHGNIVRLQDVVHS-EKRLYLVFEYLDL-DL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  92 yRKLKEQKGQLLPENQVVEWFV-QIAMALQYLHEKHILHRDLKTQNVFLTR-TNIIKVGDLGIARVLENHCDMASTLIGT 169
Cdd:PLN00009  88 -KKHMDSSPDFAKNPRLIKTYLyQILRGIAYCHSHRVLHRDLKPQNLLIDRrTNALKLADFGLARAFGIPVRTFTHEVVT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 170 PYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAFNA-KDMNSL--VYRII----EGKLP---PMPrDY-------- 230
Cdd:PLN00009 167 LWYRAPEiLLGSRHYSTPVDIWSVGCIFAEMVNQKPLFPGdSEIDELfkIFRILgtpnEETWPgvtSLP-DYksafpkwp 245
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 148839316 231 -----------SPELAELIRTMLSKRPEERPSVRSILRQPYIK 262
Cdd:PLN00009 246 pkdlatvvptlEPAGVDLLSKMLRLDPSKRITARAALEHEYFK 288
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
5-260 1.07e-17

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: 84.50  E-value: 1.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   5 AYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPN----IVTYKESWEGGDGLLY 80
Cdd:cd07837    2 AYEKLEKIGEGTYGKVYKARDKNTGKLVALKKTRLEMEEEGVPSTALREVSLLQMLSQSIyivrLLDVEHVEENGKPLLY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  81 IVMGFCEGG-----DLYRKlkeQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRT-NIIKVGDLGIAR 154
Cdd:cd07837   82 LVFEYLDTDlkkfiDSYGR---GPHNPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQkGLLKIADLGLGR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 155 VLENHCDMASTLIGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAFNA-KDMNSL--VYRII----EGKLPPM 226
Cdd:cd07837  159 AFTIPIKSYTHEIVTLWYRAPEvLLGSTHYSTPVDMWSVGCIFAEMSRKQPLFPGdSELQQLlhIFRLLgtpnEEVWPGV 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 148839316 227 -------------PRDYS-------PELAELIRTMLSKRPEERPSVRSILRQPY 260
Cdd:cd07837  239 sklrdwheypqwkPQDLSravpdlePEGVDLLTKMLAYDPAKRISAKAALQHPY 292
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
10-258 1.21e-17

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


Pssm-ID: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 84.20  E-value: 1.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEV--TLVKHRRDGKQYV-IKKLNLRNASSRERRAAEQEAQLLSQLKHPNI-----VTYKESWEGGDGLLYI 81
Cdd:cd05074   15 RMLGKGEFGSVreAQLKSEDGSFQKVaVKMLKADIFSSSDIEEFLREAACMKEFDHPNVikligVSLRSRAKGRLPIPMV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  82 VMGFCEGGDLYRKLKEQK-GQ---LLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVL- 156
Cdd:cd05074   95 ILPFMKHGDLHTFLLMSRiGEepfTLPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCMLNENMTVCVADFGLSKKIy 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 157 -----ENHCdmASTLigtPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYR-IIEGKLPPMPRD 229
Cdd:cd05074  175 sgdyyRQGC--ASKL---PVkWLALESLADNVYTTHSDVWAFGVTMWEIMTRGQTPYAGVENSEIYNyLIKGNRLKQPPD 249
                        250       260
                 ....*....|....*....|....*....
gi 148839316 230 YSPELAELIRTMLSKRPEERPSVRSILRQ 258
Cdd:cd05074  250 CLEDVYELMCQCWSPEPKCRPSFQHLRDQ 278
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
3-206 1.66e-17

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: 83.90  E-value: 1.66e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   3 LAAYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAeQEAQLLSQLKHPNIVTYKESWEGgDGLLYIV 82
Cdd:cd07873    1 LETYIKLDKLGEGTYATVYKGRSKLTDNLVALKEIRLEHEEGAPCTAI-REVSLLKDLKHANIVTLHDIIHT-EKSLTLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  83 MGFCEGgDLYRKLkEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDM 162
Cdd:cd07873   79 FEYLDK-DLKQYL-DDCGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSIPTKT 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 148839316 163 ASTLIGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAF 206
Cdd:cd07873  157 YSNEVVTLWYRPPDiLLGSTDYSTQIDMWGVGCIFYEMSTGRPLF 201
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
10-251 1.70e-17

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: 84.08  E-value: 1.70e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVK----HRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQL-KHPNIVTYKESWEGGDGLLYIVMG 84
Cdd:cd05054   13 KPLGRGAFGKVIQASafgiDKSATCRTVAVKMLKEGATASEHKALMTELKILIHIgHHLNVVNLLGACTKPGGPLMVIVE 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGGDLYRKLKEQKGQLLPE------------------------NQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLT 140
Cdd:cd05054   93 FCKFGNLSNYLRSKREEFVPYrdkgardveeeedddelykepltlEDLICYSFQVARGMEFLASRKCIHRDLAARNILLS 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 141 RTNIIKVGDLGIARVLENHCD-MASTLIGTPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLVYR 217
Cdd:cd05054  173 ENNVVKICDFGLARDIYKDPDyVRKGDARLPLkWMAPESIFDKVYTTQSDVWSFGVLLWEIFSLGASpYPGVQMDEEFCR 252
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 148839316 218 iiegKLPPMPRDYSPELA--ELIRTMLS---KRPEERPS 251
Cdd:cd05054  253 ----RLKEGTRMRAPEYTtpEIYQIMLDcwhGEPKERPT 287
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
11-263 2.27e-17

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: 83.04  E-value: 2.27e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  11 VVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNA---SSRE----RRAAEQEAQLLSQLK-HPNIVTYKESWEGgDGLLYIV 82
Cdd:cd14182   10 ILGRGVSSVVRRCIHKPTRQEYAVKIIDITGGgsfSPEEvqelREATLKEIDILRKVSgHPNIIQLKDTYET-NTFFFLV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  83 MGFCEGGDLYRKLKEQkgQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHcDM 162
Cdd:cd14182   89 FDLMKKGELFDYLTEK--VTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQLDPG-EK 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 163 ASTLIGTPYYMSPELFS-----NKP-YNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKL---PPMPRDYSPE 233
Cdd:cd14182  166 LREVCGTPGYLAPEIIEcsmddNHPgYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGNYqfgSPEWDDRSDT 245
                        250       260       270
                 ....*....|....*....|....*....|
gi 148839316 234 LAELIRTMLSKRPEERPSVRSILRQPYIKR 263
Cdd:cd14182  246 VKDLISRFLVVQPQKRYTAEEALAHPFFQQ 275
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
10-257 2.85e-17

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


Pssm-ID: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 83.14  E-value: 2.85e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVK-----HRRDGKQYVIKKLNLRNASSRerRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLyIVMG 84
Cdd:cd05094   11 RELGEGAFGKVFLAEcynlsPTKDKMLVAVKTLKDPTLAAR--KDFQREAELLTNLQHDHIVKFYGVCGDGDPLI-MVFE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGGDLYRKLKEQ--------KGQLLPEN------QVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDL 150
Cdd:cd05094   88 YMKHGDLNKFLRAHgpdamilvDGQPRQAKgelglsQMLHIATQIASGMVYLASQHFVHRDLATRNCLVGANLLVKIGDF 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 151 GIARVL--ENHCDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYR-IIEGKLPPMP 227
Cdd:cd05094  168 GMSRDVysTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLSNTEVIEcITQGRVLERP 247
                        250       260       270
                 ....*....|....*....|....*....|
gi 148839316 228 RDYSPELAELIRTMLSKRPEERPSVRSILR 257
Cdd:cd05094  248 RVCPKEVYDIMLGCWQREPQQRLNIKEIYK 277
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
12-260 2.88e-17

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: 82.32  E-value: 2.88e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHRRDGKQYVIKKLNLRnasSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLyIVMGFCEGGDL 91
Cdd:cd14115    1 IGRGRFSIVKKCLHKATRKDVAVKFVSKK---MKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYI-LVLELMDDGRL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  92 YRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTN---IIKVGDLGIARVLENHCDMaSTLIG 168
Cdd:cd14115   77 LDYLMNHDE--LMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIpvpRVKLIDLEDAVQISGHRHV-HHLLG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 169 TPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAF--NAKDMNSLVYRIIEGKLPP-MPRDYSPELAELIRTMLSKR 245
Cdd:cd14115  154 NPEFAAPEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFldESKEETCINVCRVDFSFPDeYFGDVSQAARDFINVILQED 233
                        250
                 ....*....|....*
gi 148839316 246 PEERPSVRSILRQPY 260
Cdd:cd14115  234 PRRRPTAATCLQHPW 248
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
45-255 3.03e-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: 82.44  E-value: 3.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  45 RERRAAEQEAQLLSQLK---HPNIVT-YKESWEGGDglLYIVMGFCEGGDLyrklkeqKGQLLPENQVVEWFVQIAMA-- 118
Cdd:cd13992   35 FSRTEKRTILQELNQLKelvHDNLNKfIGICINPPN--IAVVTEYCTRGSL-------QDVLLNREIKMDWMFKSSFIkd 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 119 ----LQYLHEKHI-LHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTLIGTPY---YMSPELFSNKPYNY----K 186
Cdd:cd13992  106 ivkgMNYLHSSSIgYHGRLKSSNCLVDSRWVVKLTDFGLRNLLEEQTNHQLDEDAQHKkllWTAPELLRGSLLEVrgtqK 185
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148839316 187 SDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIE-GKLPPMPRDY------SPELAELIRTMLSKRPEERPSVRSI 255
Cdd:cd13992  186 GDVYSFAIILYEILFRSDPFALEREVAIVEKVISgGNKPFRPELAvlldefPPRLVLLVKQCWAENPEKRPSFKQI 261
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
12-209 4.26e-17

Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L6 is also called CDK8-like and was previously referred to as CDK11. However, this is a confusing nomenclature as CDC2L6 is distinct from CDC2L1, which is represented by the two protein products from its gene, called CDK11(p110) and CDK11(p58), as well as the caspase-processed CDK11(p46). CDK11(p110), CDK11(p58), and CDK11(p46)do not belong to this subfamily. CDC2L6 is an associated protein of Mediator, a multiprotein complex that provides a platform to connect transcriptional and chromatin regulators and cofactors, in order to activate and mediate RNA polymerase II transcription. CDC2L6 is localized mainly in the nucleus amd exerts an opposing effect to CDK8 in VP16-dependent transcriptional activation by being a negative regulator. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 83.19  E-value: 4.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHR--RDGKQYVIKKLNLRNASsrerRAAEQEAQLLSQLKHPNIVTYKESW-EGGDGLLYIVMGFCEG 88
Cdd:cd07867   10 VGRGTYGHVYKAKRKdgKDEKEYALKQIEGTGIS----MSACREIALLRELKHPNVIALQKVFlSHSDRKVWLLFDYAEH 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  89 gDLYRKLK-------EQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLT----RTNIIKVGDLGIARVLE 157
Cdd:cd07867   86 -DLWHIIKfhraskaNKKPMQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMgegpERGRVKIADMGFARLFN 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 148839316 158 NHCDMASTL---IGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAFNAK 209
Cdd:cd07867  165 SPLKPLADLdpvVVTFWYRAPElLLGARHYTKAIDIWAIGCIFAELLTSEPIFHCR 220
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
8-255 4.28e-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: 82.77  E-value: 4.28e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   8 YLRVVGKGSYGEVTLVK---------------HRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIV------ 66
Cdd:cd05051    9 FVEKLGEGQFGEVHLCEanglsdltsddfignDNKDEPVLVAVKMLRPDASKNAREDFLKEVKIMSQLKDPNIVrllgvc 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  67 TYKESWeggdgllYIVMGFCEGGDLYRKLKEQ----------KGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQN 136
Cdd:cd05051   89 TRDEPL-------CMIVEYMENGDLNQFLQKHeaetqgasatNSKTLSYGTLLYMATQIASGMKYLESLNFVHRDLATRN 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 137 VFLTRTNIIKVGDLGIARVLENhCDmastligtpYY------------MSPELFSNKPYNYKSDVWALGCCVYEMATL-- 202
Cdd:cd05051  162 CLVGPNYTIKIADFGMSRNLYS-GD---------YYriegravlpirwMAWESILLGKFTTKSDVWAFGVTLWEILTLck 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 203 KHAFNAKDMNSLVYRIIEGK-------LPPMPRDYSPELAELIRTMLSKRPEERPSVRSI 255
Cdd:cd05051  232 EQPYEHLTDEQVIENAGEFFrddgmevYLSRPPNCPKEIYELMLECWRRDEEDRPTFREI 291
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
12-275 4.37e-17

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK8 can act as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II (RNAP II)-dependent transcription. CDK8 phosphorylates cyclin H, a subunit of the general transcription factor TFIIH, which results in the inhibition of TFIIH-dependent phosphorylation of the C-terminal domain of RNAP II, facilitating the inhibition of transcription. It has also been shown to promote transcription by a mechanism that is likely to involve RNAP II phosphorylation. CDK8 also functions as a stimulus-specific positive coregulator of p53 transcriptional responses. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 83.57  E-value: 4.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVKHR--RDGKQYVIKKLNLRNASsrerRAAEQEAQLLSQLKHPNIVTYKESW-EGGDGLLYIVMGFCEG 88
Cdd:cd07868   25 VGRGTYGHVYKAKRKdgKDDKDYALKQIEGTGIS----MSACREIALLRELKHPNVISLQKVFlSHADRKVWLLFDYAEH 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  89 gDLYRKLK-------EQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLT----RTNIIKVGDLGIARVLE 157
Cdd:cd07868  101 -DLWHIIKfhraskaNKKPVQLPRGMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMgegpERGRVKIADMGFARLFN 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 158 NHCDMASTL---IGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMN---------SLVYRIIEGKLP 224
Cdd:cd07868  180 SPLKPLADLdpvVVTFWYRAPElLLGARHYTKAIDIWAIGCIFAELLTSEPIFHCRQEDiktsnpyhhDQLDRIFNVMGF 259
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 148839316 225 PMPRDYSPelaelirtmLSKRPEERPSVRSILRQPYIKRQISFFLEATKIK 275
Cdd:cd07868  260 PADKDWED---------IKKMPEHSTLMKDFRRNTYTNCSLIKYMEKHKVK 301
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
3-219 4.78e-17

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: 82.73  E-value: 4.78e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   3 LAAYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAeQEAQLLSQLKHPNIVTYKESWEGgDGLLYIV 82
Cdd:cd07872    5 METYIKLEKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTAI-REVSLLKDLKHANIVTLHDIVHT-DKSLTLV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  83 MGFCEGgDLyRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDM 162
Cdd:cd07872   83 FEYLDK-DL-KQYMDDCGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSVPTKT 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148839316 163 ASTLIGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAF---NAKDMNSLVYRII 219
Cdd:cd07872  161 YSNEVVTLWYRPPDvLLGSSEYSTQIDMWGVGCIFFEMASGRPLFpgsTVEDELHLIFRLL 221
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
11-261 5.55e-17

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


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 82.38  E-value: 5.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  11 VVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERraAEQEAQLLSQLK-HPNIVTYKESWEGGDGLLYIVMGFCEGG 89
Cdd:cd14173    9 VLGEGAYARVQTCINLITNKEYAVKIIEKRPGHSRSR--VFREVEMLYQCQgHRNVLELIEFFEEEDKFYLVFEKMRGGS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  90 DLYRKLKEQKGQLLPENQVVEwfvQIAMALQYLHEKHILHRDLKTQNVFLTRTNII---KVG--DLGIARVLENHCDMAS 164
Cdd:cd14173   87 ILSHIHRRRHFNELEASVVVQ---DIASALDFLHNKGIAHRDLKPENILCEHPNQVspvKICdfDLGSGIKLNSDCSPIS 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 T--LI---GTPYYMSPEL---FSNKP--YNYKSDVWALGCCVYEMATLKHAFNAK---------------DMNSLVYRII 219
Cdd:cd14173  164 TpeLLtpcGSAEYMAPEVveaFNEEAsiYDKRCDLWSLGVILYIMLSGYPPFVGRcgsdcgwdrgeacpaCQNMLFESIQ 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 148839316 220 EGKLPPMPRDY---SPELAELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd14173  244 EGKYEFPEKDWahiSCAAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
10-249 5.88e-17

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: 82.79  E-value: 5.88e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRA-AEQEAQLLSQLKH---PNIVTYKESWEGGDGLLYIvMGF 85
Cdd:cd14223    6 RIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETlALNERIMLSLVSTgdcPFIVCMSYAFHTPDKLSFI-LDL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGGDLYRKLKEQKgqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIArvlenhCDMAS- 164
Cdd:cd14223   85 MNGGDLHYHLSQHG--VFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLA------CDFSKk 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 ---TLIGTPYYMSPELFSNK-PYNYKSDVWALGCCVYEMATLKHAF---NAKDMNSlVYRIIEGKLPPMPRDYSPELAEL 237
Cdd:cd14223  157 kphASVGTHGYMAPEVLQKGvAYDSSADWFSLGCMLFKLLRGHSPFrqhKTKDKHE-IDRMTLTMAVELPDSFSPELRSL 235
                        250
                 ....*....|..
gi 148839316 238 IRTMLSKRPEER 249
Cdd:cd14223  236 LEGLLQRDVNRR 247
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
10-220 6.17e-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: 82.16  E-value: 6.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVtlVKHRRDGKQYVIKKLNLRNASSRE--RRAAEQEAQLLSQLKHPNIVTYKESWEGGDG--LLYIVMgf 85
Cdd:cd14158   21 NKLGEGGFGVV--FKGYINDKNVAVKKLAAMVDISTEdlTKQFEQEIQVMAKCQHENLVELLGYSCDGPQlcLVYTYM-- 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 cEGGDLYRKLKEQKGQL-LPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCD--M 162
Cdd:cd14158   97 -PNGSLLDRLACLNDTPpLSWHMRCKIAQGTANGINYLHENNHIHRDIKSANILLDETFVPKISDFGLARASEKFSQtiM 175
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 148839316 163 ASTLIGTPYYMSPELFSNKpYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIE 220
Cdd:cd14158  176 TERIVGTTAYMAPEALRGE-ITPKSDIFSFGVVLLEIITGLPPVDENRDPQLLLDIKE 232
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
10-251 6.22e-17

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


Pssm-ID: 271106 [Multi-domain]  Cd Length: 284  Bit Score: 81.90  E-value: 6.22e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRR-DG--KQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYK----ESWEGGDGLLYIV 82
Cdd:cd14204   13 KVLGEGEFGSVMEGELQQpDGtnHKVAVKTMKLDNFSQREIEEFLSEAACMKDFNHPNVIRLLgvclEVGSQRIPKPMVI 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  83 MGFCEGGDLY----RKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIA-RVLE 157
Cdd:cd14204   93 LPFMKYGDLHsfllRSRLGSGPQHVPLQTLLKFMIDIALGMEYLSSRNFLHRDLAARNCMLRDDMTVCVADFGLSkKIYS 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 158 NHCDMASTLIGTPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYR-IIEGKLPPMPRDYSPELA 235
Cdd:cd14204  173 GDYYRQGRIAKMPVkWIAVESLADRVYTVKSDVWAFGVTMWEIATRGMTPYPGVQNHEIYDyLLHGHRLKQPEDCLDELY 252
                        250
                 ....*....|....*.
gi 148839316 236 ELIRTMLSKRPEERPS 251
Cdd:cd14204  253 DIMYSCWRSDPTDRPT 268
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
10-258 6.36e-17

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


Pssm-ID: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 81.37  E-value: 6.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEV---TLVKHRRDGKQYVIKKLNlRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLYIVMGFC 86
Cdd:cd05058    1 EVIGKGHFGCVyhgTLIDSDGQKIHCAVKSLN-RITDIEEVEQFLKEGIIMKDFSHPNVLSLLGICLPSEGSPLVVLPYM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  87 EGGDLYRKLKEQKgqllpENQVVEWFV----QIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIAR-VLENHCD 161
Cdd:cd05058   80 KHGDLRNFIRSET-----HNPTVKDLIgfglQVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVADFGLARdIYDKEYY 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 162 MASTLIGTPY---YMSPELFSNKPYNYKSDVWALGCCVYEMATlKHAFNAKDMNS--LVYRIIEGKLPPMPrDYSPE-LA 235
Cdd:cd05058  155 SVHNHTGAKLpvkWMALESLQTQKFTTKSDVWSFGVLLWELMT-RGAPPYPDVDSfdITVYLLQGRRLLQP-EYCPDpLY 232
                        250       260
                 ....*....|....*....|...
gi 148839316 236 ELIRTMLSKRPEERPSVRSILRQ 258
Cdd:cd05058  233 EVMLSCWHPKPEMRPTFSELVSR 255
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
29-261 9.82e-17

Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Tribbles Homolog (TRB) proteins interact with many proteins involved in signaling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, differentiation, and gene expression. TRB proteins bind to the middle kinase in mitogen activated protein kinase (MAPK) signaling cascades, MAPK kinases. They regulate the activity of MAPK kinases, and thus, affect MAPK signaling. In Drosophila, Tribbles regulates String, the ortholog of mammalian Cdc25, during morphogenesis. String is implicated in the progression of mitosis during embryonic development. Vertebrates contain three TRB proteins encoded by three separate genes: Tribbles-1 (TRB1 or TRIB1), Tribbles-2 (TRB2 or TRIB2), and Tribbles-3 (TRB3 or TRIB3). The TRB subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 80.55  E-value: 9.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  29 GKQYVIKKLNLRNASSRERRAAEQEAqllsqlkHPNIVTYKESWEGGdGLLYIvmgFCEG--GDLYRKLKEQKGqlLPEN 106
Cdd:cd13976   18 GEELVCKVVPVPECHAVLRAYFRLPS-------HPNISGVHEVIAGE-TKAYV---FFERdhGDLHSYVRSRKR--LREP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 107 QVVEWFVQIAMALQYLHEKHILHRDLKTQN-VFLT--RTNIiKVGDLGIARVLENHCDMASTLIGTPYYMSPELF-SNKP 182
Cdd:cd13976   85 EAARLFRQIASAVAHCHRNGIVLRDLKLRKfVFADeeRTKL-RLESLEDAVILEGEDDSLSDKHGCPAYVSPEILnSGAT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 183 YNYK-SDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPpMPRDYSPELAELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd13976  164 YSGKaADVWSLGVILYTMLVGRYPFHDSEPASLFAKIRRGQFA-IPETLSPRARCLIRSLLRREPSERLTAEDILLHPWL 242
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
9-199 9.85e-17

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: 82.80  E-value: 9.85e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRA-AEQEAQLLSQLKHPNIVTYKESWEGGDGlLYIVMGFCE 87
Cdd:cd05627    7 LKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQVAhIRAERDILVEADGAWVVKMFYSFQDKRN-LYLIMEFLP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  88 GGDLYRKLkeQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVL----------- 156
Cdd:cd05627   86 GGDMMTLL--MKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLCTGLkkahrtefyrn 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148839316 157 ------------------------ENHCDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEM 199
Cdd:cd05627  164 lthnppsdfsfqnmnskrkaetwkKNRRQLAYSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEM 230
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
10-249 9.96e-17

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: 82.42  E-value: 9.96e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRA-AEQEAQLLSQLKH---PNIVTYKESWEGGDGLLYIvMGF 85
Cdd:cd05633   11 RIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETlALNERIMLSLVSTgdcPFIVCMTYAFHTPDKLCFI-LDL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGGDLYRKLKEQKgqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIArvlenhCDMAS- 164
Cdd:cd05633   90 MNGGDLHYHLSQHG--VFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLA------CDFSKk 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 ---TLIGTPYYMSPELFSN-KPYNYKSDVWALGCCVYEMATLKHAF---NAKDMNSlVYRIIEGKLPPMPRDYSPELAEL 237
Cdd:cd05633  162 kphASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFrqhKTKDKHE-IDRMTLTVNVELPDSFSPELKSL 240
                        250
                 ....*....|..
gi 148839316 238 IRTMLSKRPEER 249
Cdd:cd05633  241 LEGLLQRDVSKR 252
PK_NRBP1_like cd13984
Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The ...
57-259 1.01e-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: 80.66  E-value: 1.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  57 LSQLKHPNIVTYKESW---EGGDGLLYIVMGFCEGGDLYRKLKEQK--GQLLPENQVVEWFVQIAMALQYLH--EKHILH 129
Cdd:cd13984   49 LIQLDHPNIVKFHRYWtdvQEEKARVIFITEYMSSGSLKQFLKKTKknHKTMNEKSWKRWCTQILSALSYLHscDPPIIH 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 130 RDLKTQNVFLTRTNIIKVGDLgIARVLENHCDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKhafnAK 209
Cdd:cd13984  129 GNLTCDTIFIQHNGLIKIGSV-APDAIHNHVKTCREEHRNLHFFAPEYGYLEDVTTAVDIYSFGMCALEMAALE----IQ 203
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 148839316 210 DMNSLVYRIIEGKLPPMPRDYSPELAELIRTMLSKRPEERPSVRSILRQP 259
Cdd:cd13984  204 SNGEKVSANEEAIIRAIFSLEDPLQKDFIRKCLSVAPQDRPSARDLLFHP 253
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
2-255 1.03e-16

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


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 81.27  E-value: 1.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   2 PLAAYCYLRVVGKGSYGEV----TLVKHRRDGKQYV-IKKLNlRNASSRERRAAEQEAQLLSQLKHPNIVTYK------- 69
Cdd:cd05048    3 PLSAVRFLEELGEGAFGKVykgeLLGPSSEESAISVaIKTLK-ENASPKTQQDFRREAELMSDLQHPNIVCLLgvctkeq 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  70 ------ESWEGGDGLLYIVM-------GFCEGGDLYRKLKEQKGQLlpenQVVewfVQIAMALQYLHEKHILHRDLKTQN 136
Cdd:cd05048   82 pqcmlfEYMAHGDLHEFLVRhsphsdvGVSSDDDGTASSLDQSDFL----HIA---IQIAAGMEYLSSHHYVHRDLAARN 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 137 VFLTRTNIIKVGDLGIARvlenhcDMAStligTPYY------------MSPELFSNKPYNYKSDVWALGCCVYEMATLK- 203
Cdd:cd05048  155 CLVGDGLTVKISDFGLSR------DIYS----SDYYrvqsksllpvrwMPPEAILYGKFTTESDVWSFGVVLWEIFSYGl 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 148839316 204 ---HAFNAKDmnsLVYRIIEGKLPPMPRDYSPELAELIRTMLSKRPEERPSVRSI 255
Cdd:cd05048  225 qpyYGYSNQE---VIEMIRSRQLLPCPEDCPARVYSLMVECWHEIPSRRPRFKEI 276
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
11-256 1.04e-16

Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR2 interacts with the protein phosphatase calcineurin and functions in calcium-mediated ERK signaling. It also functions in energy metabolism by regulating AMP kinase and AMPK-dependent processes such as glucose uptake and fatty acid oxidation. KSR proteins act as scaffold proteins that function downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases. The KSR2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 81.21  E-value: 1.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  11 VVGKGSYGEVTlvkHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLyIVMGFCEGGD 90
Cdd:cd14153    7 LIGKGRFGQVY---HGRWHGEVAIRLIDIERDNEEQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLA-IITSLCKGRT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  91 LYRKLKEQKgQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIkVGDLG---IARVLENH-------- 159
Cdd:cd14153   83 LYSVVRDAK-VVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGlftISGVLQAGrredklri 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 160 -----CDMASTLIgtpYYMSPELFSNK-PYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPR-DYSP 232
Cdd:cd14153  161 qsgwlCHLAPEII---RQLSPETEEDKlPFSKHSDVFAFGTIWYELHAREWPFKTQPAEAIIWQVGSGMKPNLSQiGMGK 237
                        250       260
                 ....*....|....*....|....
gi 148839316 233 ELAELIRTMLSKRPEERPSVRSIL 256
Cdd:cd14153  238 EISDILLFCWAYEQEERPTFSKLM 261
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
15-255 1.53e-16

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: 80.62  E-value: 1.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  15 GSYGEVTLVKHRRDGkqYVIKKLNLRNASSRERRAAE-QEAQLLSQLKHPNIVTYKeswegG----DGLLYIVMGFCEGG 89
Cdd:cd14027    4 GGFGKVSLCFHRTQG--LVVLKTVYTGPNCIEHNEALlEEGKMMNRLRHSRVVKLL-----GvileEGKYSLVMEYMEKG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  90 DLYRKLKEQKGQLLPENQVVewfVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIAR-------VLENHCDM 162
Cdd:cd14027   77 NLMHVLKKVSVPLSVKGRII---LEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASfkmwsklTKEEHNEQ 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 163 ------ASTLIGTPYYMSPELFSN---KPYNyKSDVWALGCCVYEMATLKHAF-NAKDMNSLVYRIIEGKLPP---MPRD 229
Cdd:cd14027  154 revdgtAKKNAGTLYYMAPEHLNDvnaKPTE-KSDVYSFAIVLWAIFANKEPYeNAINEDQIIMCIKSGNRPDvddITEY 232
                        250       260
                 ....*....|....*....|....*.
gi 148839316 230 YSPELAELIRTMLSKRPEERPSVRSI 255
Cdd:cd14027  233 CPREIIDLMKLCWEANPEARPTFPGI 258
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
2-220 1.61e-16

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 83.16  E-value: 1.61e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   2 PLAAYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLnLRNASSRERraaeqEAQLLSQLKHPNIV-----TYKESWEGGD 76
Cdd:PTZ00036  64 PNKSYKLGNIIGNGSFGVVYEAICIDTSEKVAIKKV-LQDPQYKNR-----ELLIMKNLNHINIIflkdyYYTECFKKNE 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  77 G--LLYIVMGFC-EGGDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLT-RTNIIKVGDLGI 152
Cdd:PTZ00036 138 KniFLNVVMEFIpQTVHKYMKHYARNNHALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDpNTHTLKLCDFGS 217
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148839316 153 ARVLENHcDMASTLIGTPYYMSPEL-FSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIE 220
Cdd:PTZ00036 218 AKNLLAG-QRSVSYICSRFYRAPELmLGATNYTTHIDLWSLGCIIAEMILGYPIFSGQSSVDQLVRIIQ 285
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
10-251 2.39e-16

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


Pssm-ID: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 80.27  E-value: 2.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYV---IKKLNLRNASSRERRAAEQEAQLLSQLKHPNI-----VTYKESWEGGDGLLYI 81
Cdd:cd05035    5 KILGEGEFGSVMEAQLKQDDGSQLkvaVKTMKVDIHTYSEIEEFLSEAACMKDFDHPNVmrligVCFTASDLNKPPSPMV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  82 VMGFCEGGDLYRKLKEQKGQLLPEN----QVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLE 157
Cdd:cd05035   85 ILPFMKHGDLHSYLLYSRLGGLPEKlplqTLLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVCVADFGLSRKIY 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 158 NHCDMASTLIGT-PY-YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYR-IIEGKLPPMPRDYSPEL 234
Cdd:cd05035  165 SGDYYRQGRISKmPVkWIALESLADNVYTSKSDVWSFGVTMWEIATRGQTPYPGVENHEIYDyLRNGNRLKQPEDCLDEV 244
                        250
                 ....*....|....*..
gi 148839316 235 AELIRTMLSKRPEERPS 251
Cdd:cd05035  245 YFLMYFCWTVDPKDRPT 261
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
8-257 2.99e-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: 80.26  E-value: 2.99e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   8 YLRVVGKGSYGEVtlVKHRRDG------KQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDG--LL 79
Cdd:cd05050    9 YVRDIGQGAFGRV--FQARAPGllpyepFTMVAVKMLKEEASADMQADFQREAALMAEFDHPNIVKLLGVCAVGKPmcLL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  80 YIVMGFcegGDLYRKLKEQKGQLLPENQVVEWFV--------------QIAMALQ------YLHEKHILHRDLKTQNVFL 139
Cdd:cd05050   87 FEYMAY---GDLNEFLRHRSPRAQCSLSHSTSSArkcglnplplscteQLCIAKQvaagmaYLSERKFVHRDLATRNCLV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 140 TRTNIIKVGDLGIAR--VLENHCDMASTLIGTPYYMSPE-LFSNKpYNYKSDVWALGCCVYEMATLK-HAFNAKDMNSLV 215
Cdd:cd05050  164 GENMVVKIADFGLSRniYSADYYKASENDAIPIRWMPPEsIFYNR-YTTESDVWAYGVVLWEIFSYGmQPYYGMAHEEVI 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 148839316 216 YRIIEGKLPPMPRDYSPELAELIRTMLSKRPEERPSVRSILR 257
Cdd:cd05050  243 YYVRDGNVLSCPDNCPLELYNLMRLCWSKLPSDRPSFASINR 284
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
9-256 3.04e-16

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: 80.45  E-value: 3.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQ----YVIKKLnlRNASS-RERRAAEQEAQLLSQLKHPNI-----VTYKESWEggdgL 78
Cdd:cd05108   12 IKVLGSGAFGTVYKGLWIPEGEKvkipVAIKEL--REATSpKANKEILDEAYVMASVDNPHVcrllgICLTSTVQ----L 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  79 LYIVMGFCEGGDLYRKLKEQKGQllpeNQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVL-- 156
Cdd:cd05108   86 ITQLMPFGCLLDYVREHKDNIGS----QYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLga 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 157 ---ENHCDMASTLIGtpyYMSPELFSNKPYNYKSDVWALGCCVYEMATlkhaFNAKDMNSL----VYRIIE-GKLPPMPR 228
Cdd:cd05108  162 eekEYHAEGGKVPIK---WMALESILHRIYTHQSDVWSYGVTVWELMT----FGSKPYDGIpaseISSILEkGERLPQPP 234
                        250       260
                 ....*....|....*....|....*...
gi 148839316 229 DYSPELAELIRTMLSKRPEERPSVRSIL 256
Cdd:cd05108  235 ICTIDVYMIMVKCWMIDADSRPKFRELI 262
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
6-262 3.29e-16

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: 80.92  E-value: 3.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLN--LRNASSRERraAEQEAQLLSQLKHPNIV----------TYKESWE 73
Cdd:cd07850    2 YQNLKPIGSGAQGIVCAAYDTVTGQNVAIKKLSrpFQNVTHAKR--AYRELVLMKLVNHKNIIgllnvftpqkSLEEFQD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  74 ggdglLYIVMGFCEGgDLYrklkeQKGQLLPENQVVEWFV-QIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGI 152
Cdd:cd07850   80 -----VYLVMELMDA-NLC-----QVIQMDLDHERMSYLLyQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 153 ARVLENHCDMASTLIgTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIE----------GK 222
Cdd:cd07850  149 ARTAGTSFMMTPYVV-TRYYRAPEVILGMGYKENVDIWSVGCIMGEMIRGTVLFPGTDHIDQWNKIIEqlgtpsdefmSR 227
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148839316 223 LPPMPRDYS-----------PEL-----------------AELIRTMLSKR----PEERPSVRSILRQPYIK 262
Cdd:cd07850  228 LQPTVRNYVenrpkyagysfEELfpdvlfppdseehnklkASQARDLLSKMlvidPEKRISVDDALQHPYIN 299
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
53-262 3.33e-16

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 81.08  E-value: 3.33e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  53 EAQLLSQLKHPNIVTYKESWEGGDGLLYIVMGFceGGDLYRKLKEQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDL 132
Cdd:PHA03209 107 EAMLLQNVNHPSVIRMKDTLVSGAITCMVLPHY--SSDLYTYLTKRSRPL-PIDQALIIEKQILEGLRYLHAQRIIHRDV 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 133 KTQNVFLTRTNIIKVGDLGIARVLENHCDMAStLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAfnakdmn 212
Cdd:PHA03209 184 KTENIFINDVDQVCIGDLGAAQFPVVAPAFLG-LAGTVETNAPEVLARDKYNSKADIWSAGIVLFEMLAYPST------- 255
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148839316 213 slvyriIEGKLPPMPRDYS----PELAELIRTmLSKRPEERPS------------VRSILRQPYIK 262
Cdd:PHA03209 256 ------IFEDPPSTPEEYVkschSHLLKIIST-LKVHPEEFPRdpgsrlvrgfieYASLERQPYTR 314
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
11-256 3.77e-16

Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie2 is a receptor PTK (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie2 is expressed mainly in endothelial cells and hematopoietic stem cells. It is also found in a subset of tumor-associated monocytes and eosinophils. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. Tie2 signaling plays key regulatory roles in vascular integrity and quiescence, and in inflammation. The Tie2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133219 [Multi-domain]  Cd Length: 303  Bit Score: 80.04  E-value: 3.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  11 VVGKGSYGEVTLVKHRRDGKQY--VIKKLNlRNASSRERRAAEQEAQLLSQL-KHPNIVTYKESWEGgDGLLYIVMGFCE 87
Cdd:cd05088   14 VIGEGNFGQVLKARIKKDGLRMdaAIKRMK-EYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEH-RGYLYLAIEYAP 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  88 GGDLYRKLKEQK--------------GQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIA 153
Cdd:cd05088   92 HGNLLDFLRKSRvletdpafaianstASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 154 RVLENHcdMASTLIGTPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLVYRIIEGKLPPMPRDYS 231
Cdd:cd05088  172 RGQEVY--VKKTMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTpYCGMTCAELYEKLPQGYRLEKPLNCD 249
                        250       260
                 ....*....|....*....|....*
gi 148839316 232 PELAELIRTMLSKRPEERPSVRSIL 256
Cdd:cd05088  250 DEVYDLMRQCWREKPYERPSFAQIL 274
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
9-258 4.03e-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: 79.68  E-value: 4.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIK---KLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKeswegGDGL---LYIV 82
Cdd:cd05109   12 VKVLGSGAFGTVYKGIWIPDGENVKIPvaiKVLRENTSPKANKEILDEAYVMAGVGSPYVCRLL-----GICLtstVQLV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  83 MGFCEGGDLYRKLKEQKGQLLPENqVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVL-----E 157
Cdd:cd05109   87 TQLMPYGCLLDYVRENKDRIGSQD-LLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFGLARLLdidetE 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 158 NHCDMASTLIGtpyYMSPELFSNKPYNYKSDVWALGCCVYEMATlkhaFNAKDMNSLVYRII-----EGKLPPMPRDYSP 232
Cdd:cd05109  166 YHADGGKVPIK---WMALESILHRRFTHQSDVWSYGVTVWELMT----FGAKPYDGIPAREIpdlleKGERLPQPPICTI 238
                        250       260
                 ....*....|....*....|....*.
gi 148839316 233 ELAELIRTMLSKRPEERPSVRSILRQ 258
Cdd:cd05109  239 DVYMIMVKCWMIDSECRPRFRELVDE 264
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
9-199 4.33e-16

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: 80.85  E-value: 4.33e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRA-AEQEAQLLSQLKHPNIVTYKESWEggDGL-LYIVMGFC 86
Cdd:cd05628    6 LKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQVGhIRAERDILVEADSLWVVKMFYSFQ--DKLnLYLIMEFL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  87 EGGDLYRKLkeQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLE--------- 157
Cdd:cd05628   84 PGGDMMTLL--MKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCTGLKkahrtefyr 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148839316 158 --NHC------------------------DMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEM 199
Cdd:cd05628  162 nlNHSlpsdftfqnmnskrkaetwkrnrrQLAFSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEM 229
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
10-261 4.73e-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: 78.91  E-value: 4.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLnLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLlYIVMGFCEGG 89
Cdd:cd14088    7 QVIKTEEFCEIFRAKDKTTGKLYTCKKF-LKRDGRKVRKAAKNEINILKMVKHPNILQLVDVFETRKEY-FIFLELATGR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  90 DLYRKLKEQKgqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQN-VFLTR--TNIIKVGDLGIARvLENhcDMASTL 166
Cdd:cd14088   85 EVFDWILDQG--YYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENlVYYNRlkNSKIVISDFHLAK-LEN--GLIKEP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 167 IGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAF---------NAKDMNsLVYRIIEGKL---PPMPRDYSPEL 234
Cdd:cd14088  160 CGTPEYLAPEVVGRQRYGRPVDCWAIGVIMYILLSGNPPFydeaeeddyENHDKN-LFRKILAGDYefdSPYWDDISQAA 238
                        250       260
                 ....*....|....*....|....*..
gi 148839316 235 AELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd14088  239 KDLVTRLMEVEQDQRITAEEAISHEWI 265
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
12-258 8.18e-16

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


Pssm-ID: 270638 [Multi-domain]  Cd Length: 269  Bit Score: 78.40  E-value: 8.18e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTL--VKHRRDGKQYVIKKLNlRNASSRERRAAEQEAQLLSQLKHPNIVT-YKESWEGGDGLLyiVMGFCEG 88
Cdd:cd05042    3 IGNGWFGKVLLgeIYSGTSVAQVVVKELK-ASANPKEQDTFLKEGQPYRILQHPNILQcLGQCVEAIPYLL--VMEFCDL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  89 GDLYRKLKEQKGQLLPENQVV---EWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIA--RVLENHCDMA 163
Cdd:cd05042   80 GDLKAYLRSEREHERGDSDTRtlqRMACEVAAGLAHLHKLNFVHSDLALRNCLLTSDLTVKIGDYGLAhsRYKEDYIETD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 164 STLIGTPYYMSPELFSNKPYNY-------KSDVWALGCCVYEMATL--KHAFNAKDMNSLVYRIIEGKL----PPMPRDY 230
Cdd:cd05042  160 DKLWFPLRWTAPELVTEFHDRLlvvdqtkYSNIWSLGVTLWELFENgaQPYSNLSDLDVLAQVVREQDTklpkPQLELPY 239
                        250       260
                 ....*....|....*....|....*...
gi 148839316 231 SPELAELIRTMLsKRPEERPSVRSILRQ 258
Cdd:cd05042  240 SDRWYEVLQFCW-LSPEQRPAAEDVHLL 266
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
8-258 8.54e-16

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


Pssm-ID: 271108 [Multi-domain]  Cd Length: 276  Bit Score: 78.46  E-value: 8.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   8 YLRVVGKGSYGEVTLVKHRRD--GKQYVIKKLNLrNASSRERRAAEQEAQLLSQLKHPNIVT-YKESWEGGDGLLyiVMG 84
Cdd:cd14206    1 YLQEIGNGWFGKVILGEIFSDytPAQVVVKELRV-SAGPLEQRKFISEAQPYRSLQHPNILQcLGLCTETIPFLL--IME 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGGDLYRKLKEQKG------QLLPEN--QVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIArvl 156
Cdd:cd14206   78 FCQLGDLKRYLRAQRKadgmtpDLPTRDlrTLQRMAYEITLGLLHLHKNNYIHSDLALRNCLLTSDLTVRIGDYGLS--- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 157 enHCDMASTLIGTP-------YYMSPELFSNKPYNY-------KSDVWALGCCVYEM----ATLKHAFNAKDMNSLVYRI 218
Cdd:cd14206  155 --HNNYKEDYYLTPdrlwiplRWVAPELLDELHGNLivvdqskESNVWSLGVTIWELfefgAQPYRHLSDEEVLTFVVRE 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 148839316 219 IEGKL--PPMPRDYSPELAELIRTmLSKRPEERPSVRSILRQ 258
Cdd:cd14206  233 QQMKLakPRLKLPYADYWYEIMQS-CWLPPSQRPSVEELHLQ 273
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
6-272 1.20e-15

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 79.89  E-value: 1.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTL-VKHRRDGKQYVIKKLNLRNassrerRAAEQEAQLLSQLKHPNIVTYKESWEGGDgLLYIVMG 84
Cdd:PHA03207  94 YNILSSLTPGSEGEVFVcTKHGDEQRKKVIVKAVTGG------KTPGREIDILKTISHRAIINLIHAYRWKS-TVCMVMP 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGgDLYRKLkEQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMAS 164
Cdd:PHA03207 167 KYKC-DLFTYV-DRSGPL-PLEQAITIQRRLLEALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGAACKLDAHPDTPQ 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 165 TL--IGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNS--------------------------LV- 215
Cdd:PHA03207 244 CYgwSGTLETNSPELLALDPYCAKTDIWSAGLVLFEMSVKNVTLFGKQVKSsssqlrsiircmqvhplefpqngstnLCk 323
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148839316 216 ----YRIIEGK---LPPMPRDYSP--ELAELIRTMLSKRPEERPSVRSILRQPYIKRQISFFLEAT 272
Cdd:PHA03207 324 hfkqYAIVLRPpytIPPVIRKYGMhmDVEYLIAKMLTFDQEFRPSAQDILSLPLFTKEPINLLNIT 389
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
95-257 1.44e-15

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: 78.22  E-value: 1.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  95 LKEQKgqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLT-RTNIIKVGDLGIARVLENHCDMASTLIGTPYYM 173
Cdd:cd13974  124 IREKR---LSEREALVIFYDVVRVVEALHKKNIVHRDLKLGNMVLNkRTRKITITNFCLGKHLVSEDDLLKDQRGSPAYI 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 174 SPELFSNKPYNYK-SDVWALGCCVYEMATLKHAFnAKDMNSLVYRIIEGKLPPMPRD--YSPELAELIRTMLSKRPEERP 250
Cdd:cd13974  201 SPDVLSGKPYLGKpSDMWALGVVLFTMLYGQFPF-YDSIPQELFRKIKAAEYTIPEDgrVSENTVCLIRKLLVLNPQKRL 279

                 ....*..
gi 148839316 251 SVRSILR 257
Cdd:cd13974  280 TASEVLD 286
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
89-260 1.45e-15

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


Pssm-ID: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 77.01  E-value: 1.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  89 GDLYRKLKEQKgqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQN-VFLT--RTNIiKVGDLGIARVLENHCDMAST 165
Cdd:cd14023   69 GDMHSYVRSCK--RLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKfVFSDeeRTQL-RLESLEDTHIMKGEDDALSD 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 LIGTPYYMSPELFSNK-PYNYKS-DVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPpMPRDYSPELAELIRTMLS 243
Cdd:cd14023  146 KHGCPAYVSPEILNTTgTYSGKSaDVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFC-IPDHVSPKARCLIRSLLR 224
                        170
                 ....*....|....*..
gi 148839316 244 KRPEERPSVRSILRQPY 260
Cdd:cd14023  225 REPSERLTAPEILLHPW 241
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
9-256 1.77e-15

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: 77.43  E-value: 1.77e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEV--TLVKHRRDGK---QYVIKKLNlRNASSRERRAAEQEAQLLSQLKHPNIV-----TYKESWEggdgl 78
Cdd:cd05036   11 IRALGQGAFGEVyeGTVSGMPGDPsplQVAVKTLP-ELCSEQDEMDFLMEALIMSKFNHPNIVrcigvCFQRLPR----- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  79 lYIVMGFCEGGDLYRKLKE-----QKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRT---NIIKVGDL 150
Cdd:cd05036   85 -FILLELMAGGDLKSFLREnrprpEQPSSLTMLDLLQLAQDVAKGCRYLEENHFIHRDIAARNCLLTCKgpgRVAKIGDF 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 151 GIARvlenhcDM--AStligtpYY------------MSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVY 216
Cdd:cd05036  164 GMAR------DIyrAD------YYrkggkamlpvkwMPPEAFLDGIFTSKTDVWSFGVLLWEIFSLGYMPYPGKSNQEVM 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 148839316 217 RIIE--GKLPPmPRDYSPELAELIRTMLSKRPEERPSVRSIL 256
Cdd:cd05036  232 EFVTsgGRMDP-PKNCPGPVYRIMTQCWQHIPEDRPNFSTIL 272
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
9-249 2.03e-15

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: 78.90  E-value: 2.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRA-AEQEAQLLSQLKHPNIVTYKESWEGGDGLlYIVMGFCE 87
Cdd:cd05626    6 IKTLGIGAFGEVCLACKVDTHALYAMKTLRKKDVLNRNQVAhVKAERDILAEADNEWVVKLYYSFQDKDNL-YFVMDYIP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  88 GGDLYRKLKEQkgQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGI--------------- 152
Cdd:cd05626   85 GGDMMSLLIRM--EVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLctgfrwthnskyyqk 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 153 ---------------------------------ARVLENHCdMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEM 199
Cdd:cd05626  163 gshirqdsmepsdlwddvsncrcgdrlktleqrATKQHQRC-LAHSLVGTPNYIAPEVLLRKGYTQLCDWWSVGVILFEM 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 148839316 200 ATLKHAFNAKDMNSLVYRIIEGK----LPPMPRdYSPELAELIrTMLSKRPEER 249
Cdd:cd05626  242 LVGQPPFLAPTPTETQLKVINWEntlhIPPQVK-LSPEAVDLI-TKLCCSAEER 293
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
10-258 2.40e-15

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: 77.36  E-value: 2.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGK--QYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNI-----VTYKESWEGGDGLLYIV 82
Cdd:cd05075    6 KTLGEGEFGSVMEGQLNQDDSvlKVAVKTMKIAICTRSEMEDFLSEAVCMKEFDHPNVmrligVCLQNTESEGYPSPVVI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  83 MGFCEGGDL-----YRKLKEQKgQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLE 157
Cdd:cd05075   86 LPFMKHGDLhsfllYSRLGDCP-VYLPTQMLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADFGLSKKIY 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 158 NHCDMASTLIG-TPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRII-EGKLPPMPRDYSPEL 234
Cdd:cd05075  165 NGDYYRQGRISkMPVkWIAIESLADRVYTTKSDVWSFGVTMWEIATRGQTPYPGVENSEIYDYLrQGNRLKQPPDCLDGL 244
                        250       260
                 ....*....|....*....|....
gi 148839316 235 AELIRTMLSKRPEERPSVRSILRQ 258
Cdd:cd05075  245 YELMSSCWLLNPKDRPSFETLRCE 268
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
79-255 3.39e-15

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: 76.45  E-value: 3.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  79 LYIVMGFCEGGDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLEN 158
Cdd:cd05083   73 LYIVMELMSKGNLVNFLRSRGRALVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAKVGSM 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 159 HCDMASTLIGtpyYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAK-DMNSLVYRIIEGKLPPMPRDYSPELAEL 237
Cdd:cd05083  153 GVDNSRLPVK---WTAPEALKNKKFSSKSDVWSYGVLLWEVFSYGRAPYPKmSVKEVKEAVEKGYRMEPPEGCPPDVYSI 229
                        170
                 ....*....|....*...
gi 148839316 238 IRTMLSKRPEERPSVRSI 255
Cdd:cd05083  230 MTSCWEAEPGKRPSFKKL 247
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
8-257 3.51e-15

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


Pssm-ID: 270669 [Multi-domain]  Cd Length: 271  Bit Score: 76.44  E-value: 3.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   8 YLRVVGKGSYGEVTLVKHRRD--GKQYVIKKLNlRNASSRERRAAEQEAQLLSQLKHPNIVT-YKESWEGGDGLLyiVMG 84
Cdd:cd05086    1 YIQEIGNGWFGKVLLGEIYTGtsVARVVVKELK-ASANPKEQDDFLQQGEPYYILQHPNILQcVGQCVEAIPYLL--VFE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGGDLYRKLKEQKGQLLPENQVVE---WFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGI--ARVLENH 159
Cdd:cd05086   78 FCDLGDLKTYLANQQEKLRGDSQIMLlqrMACEIAAGLAHMHKHNFLHSDLALRNCYLTSDLTVKVGDYGIgfSRYKEDY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 160 CDMASTLIGTPYYMSPELFSNK-------PYNYKSDVWALGCCVYEM----ATLKHAFNAKDMNSLVYRIIEGKL--PPM 226
Cdd:cd05086  158 IETDDKKYAPLRWTAPELVTSFqdgllaaEQTKYSNIWSLGVTLWELfenaAQPYSDLSDREVLNHVIKERQVKLfkPHL 237
                        250       260       270
                 ....*....|....*....|....*....|..
gi 148839316 227 PRDYSPELAELIR-TMLSkrPEERPSVRSILR 257
Cdd:cd05086  238 EQPYSDRWYEVLQfCWLS--PEKRPTAEEVHR 267
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
4-261 4.09e-15

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: 76.17  E-value: 4.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   4 AAYCYLRVVGKGSYGEVTLVKHRRDGK----QYVIKKLnlrnassRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLL 79
Cdd:cd14113    7 SFYSEVAELGRGRFSVVKKCDQRGTKRavatKFVNKKL-------MKRDQVTHELGVLQSLQHPQLVGLLDTFETPTSYI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  80 yIVMGFCEGGDLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTN---IIKVGDLGIARVL 156
Cdd:cd14113   80 -LVLEMADQGRLLDYVVRWGN--LTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLskpTIKLADFGDAVQL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 157 eNHCDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLpPMPRDY----SP 232
Cdd:cd14113  157 -NTTYYIHQLLGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLDF-SFPDDYfkgvSQ 234
                        250       260
                 ....*....|....*....|....*....
gi 148839316 233 ELAELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd14113  235 KAKDFVCFLLQMDPAKRPSAALCLQEQWL 263
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
12-257 5.60e-15

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: 75.99  E-value: 5.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGevTLVKHRRDGKQYV-IKKLNlRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDG--LLYIVMGFCEG 88
Cdd:cd14664    1 IGRGGAG--TVYKGVMPNGTLVaVKRLK-GEGTQGGDHGFQAEIQTLGMIRHRNIVRLRGYCSNPTTnlLVYEYMPNGSL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  89 GDLYRKLKEQKGQL-LPENQVVEwfVQIAMALQYLHEK---HILHRDLKTQNVFLTRTNIIKVGDLGIARVL---ENHCd 161
Cdd:cd14664   78 GELLHSRPESQPPLdWETRQRIA--LGSARGLAYLHHDcspLIIHRDVKSNNILLDEEFEAHVADFGLAKLMddkDSHV- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 162 mASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNA---KDMNSLVY--------RIIEGKLPPMPRDY 230
Cdd:cd14664  155 -MSSVAGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRPFDEaflDDGVDIVDwvrglleeKKVEALVDPDLQGV 233
                        250       260       270
                 ....*....|....*....|....*....|..
gi 148839316 231 SP--ELAELIRTML---SKRPEERPSVRSILR 257
Cdd:cd14664  234 YKleEVEQVFQVALlctQSSPMERPTMREVVR 265
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
4-262 6.77e-15

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: 77.39  E-value: 6.77e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   4 AAYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRA-AEQEAQLLSQLKHPNIVTYKESWEGGDGLlYIV 82
Cdd:cd05625    1 SMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAhVKAERDILAEADNEWVVRLYYSFQDKDNL-YFV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  83 MGFCEGGDLYRKLKEQKgqLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIA--------- 153
Cdd:cd05625   80 MDYIPGGDMMSLLIRMG--VFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthds 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 154 -------------------------------------RVLENH--CdMASTLIGTPYYMSPELFSNKPYNYKSDVWALGC 194
Cdd:cd05625  158 kyyqsgdhlrqdsmdfsnewgdpencrcgdrlkplerRAARQHqrC-LAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGV 236
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148839316 195 CVYEMATLKHAFNAKDMNSLVYRIIEGK----LPPMPRdYSPELAELIrTMLSKRPEER---PSVRSILRQPYIK 262
Cdd:cd05625  237 ILFEMLVGQPPFLAQTPLETQMKVINWQtslhIPPQAK-LSPEASDLI-IKLCRGPEDRlgkNGADEIKAHPFFK 309
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
8-255 8.13e-15

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


Pssm-ID: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 75.41  E-value: 8.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   8 YLRVVGKGSYGEVTL--VKHRRDGKQYVIKKLNlRNASSRERRAAEQEAQLLSQLKHPNIVT-YKESWEGGDGLLyiVMG 84
Cdd:cd05087    1 YLKEIGHGWFGKVFLgeVNSGLSSTQVVVKELK-ASASVQDQMQFLEEAQPYRALQHTNLLQcLAQCAEVTPYLL--VME 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGGDLYRKLKEQKG--QLLPENQVVEWFV-QIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIA--RVLENH 159
Cdd:cd05087   78 FCPLGDLKGYLRSCRAaeSMAPDPLTLQRMAcEVACGLLHLHRNNFVHSDLALRNCLLTADLTVKIGDYGLShcKYKEDY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 160 CDMASTLIGTPYYMSPELFSNKPYNY-------KSDVWALGCCVYEMATL--KHAFNAKDMNSLVYRIIEGKL----PPM 226
Cdd:cd05087  158 FVTADQLWVPLRWIAPELVDEVHGNLlvvdqtkQSNVWSLGVTIWELFELgnQPYRHYSDRQVLTYTVREQQLklpkPQL 237
                        250       260
                 ....*....|....*....|....*....
gi 148839316 227 PRDYSPELAELIRtMLSKRPEERPSVRSI 255
Cdd:cd05087  238 KLSLAERWYEVMQ-FCWLQPEQRPTAEEV 265
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
25-261 9.80e-15

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


Pssm-ID: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 74.53  E-value: 9.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  25 HRRDGKQYVIKKLNLRNASSrerrAAEQEAQLLSqlkHPNIVTYKESWEGGDgLLYIvmgFCEG--GDLYRKLKEQKGql 102
Cdd:cd14024   14 HYQTEKEYTCKVLSLRSYQE----CLAPYDRLGP---HEGVCSVLEVVIGQD-RAYA---FFSRhyGDMHSHVRRRRR-- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 103 LPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLT---RTNIIKVGdLGIARVLENHCDMASTLIGTPYYMSPELFS 179
Cdd:cd14024   81 LSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTdelRTKLVLVN-LEDSCPLNGDDDSLTDKHGCPAYVGPEILS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 180 NK-PYNYK-SDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLpPMPRDYSPELAELIRTMLSKRPEERPSVRSILR 257
Cdd:cd14024  160 SRrSYSGKaADVWSLGVCLYTMLLGRYPFQDTEPAALFAKIRRGAF-SLPAWLSPGARCLVSCMLRRSPAERLKASEILL 238

                 ....
gi 148839316 258 QPYI 261
Cdd:cd14024  239 HPWL 242
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
9-260 1.00e-14

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: 76.06  E-value: 1.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLnlRNASsRERRAAEQEAQLLSQLKH------PNIVTYKESWEGgDGLLYIV 82
Cdd:cd14134   17 LRLLGEGTFGKVLECWDRKRKRYVAVKII--RNVE-KYREAAKIEIDVLETLAEkdpngkSHCVQLRDWFDY-RGHMCIV 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  83 MGFCeGGDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFL----------TRTN--------- 143
Cdd:cd14134   93 FELL-GPSLYDFLKKNNYGPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLvdsdyvkvynPKKKrqirvpkst 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 144 IIKVGDLGIArVLENHCDmaSTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMAT----------LKH--------- 204
Cdd:cd14134  172 DIKLIDFGSA-TFDDEYH--SSIVSTRHYRAPEVILGLGWSYPCDVWSIGCILVELYTgellfqthdnLEHlammerilg 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 205 --------------AFNAKDMNSL-----------VYRIIEGKLPPMPRDYS--PELAELIRTMLSKRPEERPSVRSILR 257
Cdd:cd14134  249 plpkrmirrakkgaKYFYFYHGRLdwpegsssgrsIKRVCKPLKRLMLLVDPehRLLFDLIRKMLEYDPSKRITAKEALK 328

                 ...
gi 148839316 258 QPY 260
Cdd:cd14134  329 HPF 331
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
3-247 1.48e-14

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: 75.90  E-value: 1.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   3 LAAYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGL---- 78
Cdd:cd07874   16 LKRYQNLKPIGSGAQGIVCAAYDAVLDRNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIISLLNVFTPQKSLeefq 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  79 -LYIVMGFCEGgDLYRKLKEQkgqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLE 157
Cdd:cd07874   96 dVYLVMELMDA-NLCQVIQME----LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAG 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 158 NHCDMASTLIgTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPrDYSPELAEL 237
Cdd:cd07874  171 TSFMMTPYVV-TRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVIEQLGTPCP-EFMKKLQPT 248
                        250
                 ....*....|
gi 148839316 238 IRTMLSKRPE 247
Cdd:cd07874  249 VRNYVENRPK 258
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
72-261 1.66e-14

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: 74.22  E-value: 1.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  72 WEGGDGLLyIVMGFCE-GGDLYRKLKEqKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFL-TRTNIIKVGD 149
Cdd:cd14102   73 YERPDGFL-IVMERPEpVKDLFDFITE-KGAL-DEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVdLRTGELKLID 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 150 LGIARVLENhcDMASTLIGTPYYMSPELFSNKPYNYKS-DVWALGCCVYEMATLKHAFNAKDmnslvyRIIEGKLPpMPR 228
Cdd:cd14102  150 FGSGALLKD--TVYTDFDGTRVYSPPEWIRYHRYHGRSaTVWSLGVLLYDMVCGDIPFEQDE------EILRGRLY-FRR 220
                        170       180       190
                 ....*....|....*....|....*....|...
gi 148839316 229 DYSPELAELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd14102  221 RVSPECQQLIKWCLSLRPSDRPTLEQIFDHPWM 253
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
46-210 2.37e-14

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 75.80  E-value: 2.37e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  46 ERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLYIVMGFceGGDLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEK 125
Cdd:PHA03212 126 QRGGTATEAHILRAINHPSIIQLKGTFTYNKFTCLILPRY--KTDLYCYLAAKRN--IAICDILAIERSVLRAIQYLHEN 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 126 HILHRDLKTQNVFLTRTNIIKVGDLGIARV-LENHCDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKH 204
Cdd:PHA03212 202 RIIHRDIKAENIFINHPGDVCLGDFGAACFpVDINANKYYGWAGTIATNAPELLARDPYGPAVDIWSAGIVLFEMATCHD 281

                 ....*.
gi 148839316 205 AFNAKD 210
Cdd:PHA03212 282 SLFEKD 287
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
1-255 3.31e-14

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


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 73.89  E-value: 3.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   1 MPLAAYCYLRVVGKGSYGEVT---LVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIV------TYKES 71
Cdd:cd05090    2 LPLSAVRFMEELGECAFGKIYkghLYLPGMDHAQLVAIKTLKDYNNPQQWNEFQQEASLMTELHHPNIVcllgvvTQEQP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  72 weggdglLYIVMGFCEGGDLYRKL------------KEQKGQL---LPENQVVEWFVQIAMALQYLHEKHILHRDLKTQN 136
Cdd:cd05090   82 -------VCMLFEFMNQGDLHEFLimrsphsdvgcsSDEDGTVkssLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARN 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 137 VFLTRTNIIKVGDLGIARVL---ENHCDMASTLIGTpYYMSPELFSNKPYNYKSDVWALGCCVYEMATLK----HAFNAK 209
Cdd:cd05090  155 ILVGEQLHVKISDLGLSREIyssDYYRVQNKSLLPI-RWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGlqpyYGFSNQ 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 148839316 210 DMNSLVYRiieGKLPPMPRDYSPELAELIRTMLSKRPEERPSVRSI 255
Cdd:cd05090  234 EVIEMVRK---RQLLPCSEDCPPRMYSLMTECWQEIPSRRPRFKDI 276
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
6-261 3.68e-14

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: 74.54  E-value: 3.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKklnLRNASSRERRAAEQEAQLLSQL-----KHP---NIVTYKESWE--GG 75
Cdd:cd14136   12 YHVVRKLGWGHFSTVWLCWDLQNKRFVALK---VVKSAQHYTEAALDEIKLLKCVreadpKDPgreHVVQLLDDFKhtGP 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  76 DGLlYIVMGFCEGGDLYRKLKEQ---KGqlLPENQVVEWFVQIAMALQYLHEK-HILHRDLKTQNVFLTRTNI-IKVGDL 150
Cdd:cd14136   89 NGT-HVCMVFEVLGPNLLKLIKRynyRG--IPLPLVKKIARQVLQGLDYLHTKcGIIHTDIKPENVLLCISKIeVKIADL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 151 GIARVLENHcdmASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFN-------AKDMNSLVYrIIE--G 221
Cdd:cd14136  166 GNACWTDKH---FTEDIQTRQYRSPEVILGAGYGTPADIWSTACMAFELATGDYLFDphsgedySRDEDHLAL-IIEllG 241
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148839316 222 KLPP---------------------------------------MPRDYSPELAELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd14136  242 RIPRsiilsgkysreffnrkgelrhisklkpwpledvlvekykWSKEEAKEFASFLLPMLEYDPEKRATAAQCLQHPWL 320
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
11-200 4.16e-14

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: 73.63  E-value: 4.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  11 VVGKGSYGEVtlVKHRRDGKQYVIKKLnlrnaSSRERRAAEQEAQLLS--QLKHPNIVTYKESWEGGDGL---LYIVMGF 85
Cdd:cd13998    2 VIGKGRFGEV--WKASLKNEPVAVKIF-----SSRDKQSWFREKEIYRtpMLKHENILQFIAADERDTALrteLWLVTAF 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGGDLYRKLKeqkGQLLPENQVVEWFVQIAMALQYLHEKH---------ILHRDLKTQNVFLTRTNIIKVGDLGIARVL 156
Cdd:cd13998   75 HPNGSL*DYLS---LHTIDWVSLCRLALSVARGLAHLHSEIpgctqgkpaIAHRDLKSKNILVKNDGTCCIADFGLAVRL 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 148839316 157 E---NHCDMA-STLIGTPYYMSPEL------FSNKPYNYKSDVWALGCCVYEMA 200
Cdd:cd13998  152 SpstGEEDNAnNGQVGTKRYMAPEVlegainLRDFESFKRVDIYAMGLVLWEMA 205
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
10-255 4.56e-14

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphA10, which contains an inactive tyr kinase domain, may function to attenuate signals of co-clustered active receptors. EphA10 is mainly expressed in the testis. Ephrin/EphR interaction results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. EphRs comprise the largest subfamily of receptor tyr kinases (RTKs). In general, class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The EphA10 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133195 [Multi-domain]  Cd Length: 266  Bit Score: 73.03  E-value: 4.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRRDGKQYVIKKLN-LR-NASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLyIVMGFCE 87
Cdd:cd05064   11 RILGTGRFGELCRGCLKLPSKRELPVAIHtLRaGCSDKQRRGFLAEALTLGQFDHSNIVRLEGVITRGNTMM-IVTEYMS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  88 GGDLYRKLKEQKGQLLPeNQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGdlGIARVLENHCD-MASTL 166
Cdd:cd05064   90 NGALDSFLRKHEGQLVA-GQLMGMLPGLASGMKYLSEMGYVHKGLAAHKVLVNSDLVCKIS--GFRRLQEDKSEaIYTTM 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 167 IGTP--YYMSPELFSNKPYNYKSDVWALGCCVYEMAtlkhAFNAK---DM-NSLVYRIIEG--KLPPmPRDYSPELAELI 238
Cdd:cd05064  167 SGKSpvLWAAPEAIQYHHFSSASDVWSFGIVMWEVM----SYGERpywDMsGQDVIKAVEDgfRLPA-PRNCPNLLHQLM 241
                        250
                 ....*....|....*..
gi 148839316 239 RTMLSKRPEERPSVRSI 255
Cdd:cd05064  242 LDCWQKERGERPRFSQI 258
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
12-228 5.98e-14

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK3 is predominantly expressed in mature spermatozoa, and might play a role in the fertilization process. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271116 [Multi-domain]  Cd Length: 331  Bit Score: 73.89  E-value: 5.98e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVT-LVKHRRdGKQYVIKKLnLRNASsRERRAAEQEAQLLSQLK-----HPNIVTYKESWEGGDGLLYIVMGF 85
Cdd:cd14214   21 LGEGTFGKVVeCLDHAR-GKSQVALKI-IRNVG-KYREAARLEINVLKKIKekdkeNKFLCVLMSDWFNFHGHMCIAFEL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CeGGDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLT-------------------RTNIIK 146
Cdd:cd14214   98 L-GKNTFEFLKENNFQPYPLPHIRHMAYQLCHALKFLHENQLTHTDLKPENILFVnsefdtlynesksceeksvKNTSIR 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 147 VGDLGIARVLENHcdmASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDmNSLVYRIIEGKLPPM 226
Cdd:cd14214  177 VADFGSATFDHEH---HTTIVATRHYRPPEVILELGWAQPCDVWSLGCILFEYYRGFTLFQTHE-NREHLVMMEKILGPI 252

                 ..
gi 148839316 227 PR 228
Cdd:cd14214  253 PS 254
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
3-247 7.88e-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: 7.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   3 LAAYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGL---- 78
Cdd:cd07875   23 LKRYQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIIGLLNVFTPQKSLeefq 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  79 -LYIVMGFCEGgDLYRKLKEQkgqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLE 157
Cdd:cd07875  103 dVYIVMELMDA-NLCQVIQME----LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAG 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 158 NHCDMASTLIgTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPrDYSPELAEL 237
Cdd:cd07875  178 TSFMMTPYVV-TRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGVLFPGTDHIDQWNKVIEQLGTPCP-EFMKKLQPT 255
                        250
                 ....*....|
gi 148839316 238 IRTMLSKRPE 247
Cdd:cd07875  256 VRTYVENRPK 265
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
9-201 8.88e-14

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


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 72.68  E-value: 8.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKL--NLRNASSRERRAAEQEAQL-LSQLKHPNIVTYKESWEGGDglLYIVMGF 85
Cdd:cd05111   12 LKVLGSGVFGTVHKGIWIPEGDSIKIPVAikVIQDRSGRQSFQAVTDHMLaIGSLDHAYIVRLLGICPGAS--LQLVTQL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGGDLYRKLKEQKGQLLPEnQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVL-ENHCDMAS 164
Cdd:cd05111   90 LPLGSLLDHVRQHRGSLGPQ-LLLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLKSPSQVQVADFGVADLLyPDDKKYFY 168
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 148839316 165 TLIGTPY-YMSPELFSNKPYNYKSDVWALGCCVYEMAT 201
Cdd:cd05111  169 SEAKTPIkWMALESIHFGKYTHQSDVWSYGVTVWEMMT 206
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
9-266 9.12e-14

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: 73.10  E-value: 9.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKG--SYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESW-EGGDglLYIVMGF 85
Cdd:cd08216    3 LYEIGKCfkGGGVVHLAKHKPTNTLVAVKKINLESDSKEDLKFLQQEILTSRQLQHPNILPYVTSFvVDND--LYVVTPL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  86 CEGGDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMAST 165
Cdd:cd08216   81 MAYGSCRDLLKTHFPEGLPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYAYSMVKHGKRQRV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 LIGTP-------YYMSPELF--SNKPYNYKSDVWALG--CCvyEMATLKHAFnaKDM----------NSLVYRII----- 219
Cdd:cd08216  161 VHDFPksseknlPWLSPEVLqqNLLGYNEKSDIYSVGitAC--ELANGVVPF--SDMpatqmllekvRGTTPQLLdcsty 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148839316 220 ---EGKLPPMP------------------RDYSPELAELIRTMLSKRPEERPSVRSILRQPYIKrQIS 266
Cdd:cd08216  237 pleEDSMSQSEdsstehpnnrdtrdipyqRTFSEAFHQFVELCLQRDPELRPSASQLLAHSFFK-QCR 303
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
90-250 9.62e-14

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: 72.14  E-value: 9.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  90 DLYRKLKeqKGQLLPENQVVEwfVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARvleNHCDMASTLIGT 169
Cdd:cd13975   90 DLYTGIK--AGLSLEERLQIA--LDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFCK---PEAMMSGSIVGT 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 170 PYYMSPELFSNKpYNYKSDVWALGCCVYEM----ATLKHAFNAKDMNSLVYRIIEGKLPPMPR-DYSPELAELIRTMLSK 244
Cdd:cd13975  163 PIHMAPELFSGK-YDNSVDVYAFGILFWYLcaghVKLPEAFEQCASKDHLWNNVRKGVRPERLpVFDEECWNLMEACWSG 241

                 ....*.
gi 148839316 245 RPEERP 250
Cdd:cd13975  242 DPSQRP 247
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
3-261 9.67e-14

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: 73.52  E-value: 9.67e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   3 LAAYCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGL---- 78
Cdd:cd07876   20 LKRYQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRPFQNQTHAKRAYRELVLLKCVNHKNIISLLNVFTPQKSLeefq 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  79 -LYIVMGFCEGgdlyrKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLE 157
Cdd:cd07876  100 dVYLVMELMDA-----NLCQVIHMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAC 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 158 NHCDMASTLIgTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIE----------GKLPPMP 227
Cdd:cd07876  175 TNFMMTPYVV-TRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGSVIFQGTDHIDQWNKVIEqlgtpsaefmNRLQPTV 253
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148839316 228 RDY-------------------------------SPELAELIRTMLSKRPEERPSVRSILRQPYI 261
Cdd:cd07876  254 RNYvenrpqypgisfeelfpdwifpseserdklkTSQARDLLSKMLVIDPDKRISVDEALRHPYI 318
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
10-256 1.06e-13

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: 72.37  E-value: 1.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEV------TLVKHRRDGKqYVIKKLNlRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLyIVM 83
Cdd:cd05062   12 RELGQGSFGMVyegiakGVVKDEPETR-VAIKTVN-EAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQGQPTL-VIM 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  84 GFCEGGDLYRKLKEQK-------GQLLPE-NQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARV 155
Cdd:cd05062   89 ELMTRGDLKSYLRSLRpemennpVQAPPSlKKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVKIGDFGMTRD 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 156 L--ENHCDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYR-IIEGKLPPMPRDYSP 232
Cdd:cd05062  169 IyeTDYYRKGGKGLLPVRWMSPESLKDGVFTTYSDVWSFGVVLWEIATLAEQPYQGMSNEQVLRfVMEGGLLDKPDNCPD 248
                        250       260
                 ....*....|....*....|....
gi 148839316 233 ELAELIRTMLSKRPEERPSVRSIL 256
Cdd:cd05062  249 MLFELMRMCWQYNPKMRPSFLEII 272
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
108-250 1.15e-13

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR1 (or Flt1) binds VEGFA, VEGFB, and placenta growth factor (PLGF). It regulates monocyte and macrophage migration, vascular permeability, haematopoiesis, and the recruitment of haematopietic progenitor cells from the bone marrow. VEGFR1 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 73.11  E-value: 1.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 108 VVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTliGTPY----YMSPELFSNKPY 183
Cdd:cd14207  182 LISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARDIYKNPDYVRK--GDARlplkWMAPESIFDKIY 259
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148839316 184 NYKSDVWALGCCVYEMATLKHA-FNAKDMNS-LVYRIIEGKLPPMPRDYSPELAELIRTMLSKRPEERP 250
Cdd:cd14207  260 STKSDVWSYGVLLWEIFSLGASpYPGVQIDEdFCSKLKEGIRMRAPEFATSEIYQIMLDCWQGDPNERP 328
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
9-256 1.17e-13

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: 72.31  E-value: 1.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEV------TLVKHRRDGKqYVIKKLNlRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLyIV 82
Cdd:cd05061   11 LRELGQGSFGMVyegnarDIIKGEAETR-VAVKTVN-ESASLRERIEFLNEASVMKGFTCHHVVRLLGVVSKGQPTL-VV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  83 MGFCEGGDLYRKLKEQK-------GQLLPE-NQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIAR 154
Cdd:cd05061   88 MELMAHGDLKSYLRSLRpeaennpGRPPPTlQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKIGDFGMTR 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 155 vlenhcdmasTLIGTPYY------------MSPELFSNKPYNYKSDVWALGCCVYEMATL-KHAFNAKDMNSLVYRIIEG 221
Cdd:cd05061  168 ----------DIYETDYYrkggkgllpvrwMAPESLKDGVFTTSSDMWSFGVVLWEITSLaEQPYQGLSNEQVLKFVMDG 237
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 148839316 222 KLPPMPRDYSPELAELIRTMLSKRPEERPSVRSIL 256
Cdd:cd05061  238 GYLDQPDNCPERVTDLMRMCWQFNPKMRPTFLEIV 272
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
90-261 1.18e-13

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


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 71.92  E-value: 1.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  90 DLYRKLKEQKGqlLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLT-RTNIIKVGDLGIARVLENhcDMASTLIG 168
Cdd:cd14100   92 DLFDFITERGA--LPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDlNTGELKLIDFGSGALLKD--TVYTDFDG 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 169 TPYYMSPELFSNKPYNYKS-DVWALGCCVYEMATLKHAFNAKDmnslvyRIIEGKLpPMPRDYSPELAELIRTMLSKRPE 247
Cdd:cd14100  168 TRVYSPPEWIRFHRYHGRSaAVWSLGILLYDMVCGDIPFEHDE------EIIRGQV-FFRQRVSSECQHLIKWCLALRPS 240
                        170
                 ....*....|....
gi 148839316 248 ERPSVRSILRQPYI 261
Cdd:cd14100  241 DRPSFEDIQNHPWM 254
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
32-260 1.36e-13

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


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 71.97  E-value: 1.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  32 YVIKKLNLRNASSRER--------RAAEQeaqlLSQLKHPNIVTYKESWEGGDGLLYIVMG--FC-------EGGDLYRK 94
Cdd:cd14011   27 FVFEKKQLEEYSKRDReqilellkRGVKQ----LTRLRHPRILTVQHPLEESRESLAFATEpvFAslanvlgERDNMPSP 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  95 LKEQKGQLLPENQVVEWFVQIAMALQYLH-EKHILHRDLKTQNVFLTRTNIIKVGDLGIA-----------RVLENHCDM 162
Cdd:cd14011  103 PPELQDYKLYDVEIKYGLLQISEALSFLHnDVKLVHGNICPESVVINSNGEWKLAGFDFCisseqatdqfpYFREYDPNL 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 163 ASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEM-ATLKHAFNAKDmNSLVYRIIEGKLPPMPR----DYSPELAEL 237
Cdd:cd14011  183 PPLAQPNLNYLAPEYILSKTCDPASDMFSLGVLIYAIyNKGKPLFDCVN-NLLSYKKNSNQLRQLSLslleKVPEELRDH 261
                        250       260
                 ....*....|....*....|...
gi 148839316 238 IRTMLSKRPEERPSVRSILRQPY 260
Cdd:cd14011  262 VKTLLNVTPEVRPDAEQLSKIPF 284
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
114-265 1.39e-13

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


Pssm-ID: 270682 [Multi-domain]  Cd Length: 375  Bit Score: 73.40  E-value: 1.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 114 QIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENhcDMASTLIGTPY----YMSPELFSNKPYNYKSDV 189
Cdd:cd05104  222 QVAKGMEFLASKNCIHRDLAARNILLTHGRITKICDFGLARDIRN--DSNYVVKGNARlpvkWMAPESIFECVYTFESDV 299
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148839316 190 WALGCCVYEMATLKHA-FNAKDMNSLVYRII-EGKLPPMPRDYSPELAELIRTMLSKRPEERPSVRSILRQpyIKRQI 265
Cdd:cd05104  300 WSYGILLWEIFSLGSSpYPGMPVDSKFYKMIkEGYRMDSPEFAPSEMYDIMRSCWDADPLKRPTFKQIVQL--IEQQL 375
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
89-255 2.02e-13

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


Pssm-ID: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 73.13  E-value: 2.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  89 GDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVL---ENHCDMAST 165
Cdd:cd05105  220 SEVKNLLSDDGSEGLTTLDLLSFTYQVARGMEFLASKNCVHRDLAARNVLLAQGKIVKICDFGLARDImhdSNYVSKGST 299
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 166 LIGTPyYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLVY-RIIEGKLPPMPRDYSPELAELIRTMLS 243
Cdd:cd05105  300 FLPVK-WMAPESIFDNLYTTLSDVWSYGILLWEIFSLGGTpYPGMIVDSTFYnKIKSGYRMAKPDHATQEVYDIMVKCWN 378
                        170
                 ....*....|..
gi 148839316 244 KRPEERPSVRSI 255
Cdd:cd05105  379 SEPEKRPSFLHL 390
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
11-252 3.72e-13

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: 70.76  E-value: 3.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  11 VVGKGSYGEVTLVKHRrdgKQYV-IKKLNLRNASSRERraaEQEAQLLSQLKHPNIVTY--KESW-EGGDGLLYIVMGFC 86
Cdd:cd14056    2 TIGKGRYGEVWLGKYR---GEKVaVKIFSSRDEDSWFR---ETEIYQTVMLRHENILGFiaADIKsTGSWTQLWLITEYH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  87 EGGDLYRKLKEQKgqlLPENQVVEWFVQIAMALQYLH-EKH-------ILHRDLKTQNVFLTRTNIIKVGDLGIA-RVLE 157
Cdd:cd14056   76 EHGSLYDYLQRNT---LDTEEALRLAYSAASGLAHLHtEIVgtqgkpaIAHRDLKSKNILVKRDGTCCIADLGLAvRYDS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 158 NHCDMA---STLIGTPYYMSPELFSNK--PYN---YK-SDVWALGCCVYEMA------------------TLKHAFNAKD 210
Cdd:cd14056  153 DTNTIDippNPRVGTKRYMAPEVLDDSinPKSfesFKmADIYSFGLVLWEIArrceiggiaeeyqlpyfgMVPSDPSFEE 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 148839316 211 MNSLVyrIIEGKLPPMPRDYS-----PELAELIRTMLSKRPEERPSV 252
Cdd:cd14056  233 MRKVV--CVEKLRPPIPNRWKsdpvlRSMVKLMQECWSENPHARLTA 277
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
9-251 4.37e-13

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: 4.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   9 LRVVGKGSYGEVTLVKHRRDGKQYVIKKLNLRN-ASSRERRAAEQEAQLLSQLKHPNIVTykesweggdgllyiVMGFCE 87
Cdd:cd14026    2 LRYLSRGAFGTVSRARHADWRVTVAIKCLKLDSpVGDSERNCLLKEAEILHKARFSYILP--------------ILGICN 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  88 GGDLYRKLKE-----QKGQLLPENQV---VEW------FVQIAMALQYLHEKH--ILHRDLKTQNVFLTRTNIIKVGDLG 151
Cdd:cd14026   68 EPEFLGIVTEymtngSLNELLHEKDIypdVAWplrlriLYEIALGVNYLHNMSppLLHHDLKTQNILLDGEFHVKIADFG 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 152 IA--RVLENHCDMASTLI---GTPYYMSPELFS---NKPYNYKSDVWALGCCVYEMATLKHAF-NAKDMNSLVYRIIEGK 222
Cdd:cd14026  148 LSkwRQLSISQSRSSKSApegGTIIYMPPEEYEpsqKRRASVKHDIYSYAIIMWEVLSRKIPFeEVTNPLQIMYSVSQGH 227
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 148839316 223 LP-----PMPRDYsPELAELIRTMLS---KRPEERPS 251
Cdd:cd14026  228 RPdtgedSLPVDI-PHRATLINLIESgwaQNPDERPS 263
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
12-266 4.72e-13

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


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 70.38  E-value: 4.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVtlvkHR-RDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLyIVMGFCEGGD 90
Cdd:cd14152    8 IGQGRWGKV----HRgRWHGEVAIRLLEIDGNNQDHLKLFKKEVMNYRQTRHENVVLFMGACMHPPHLA-IITSFCKGRT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  91 LYRKLKEQKGQLlPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNII--KVGDLGIARVL-----ENHCDMA 163
Cdd:cd14152   83 LYSFVRDPKTSL-DINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVVitDFGLFGISGVVqegrrENELKLP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 164 STLIgtpYYMSPELFSNK---------PYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEG---KLPPMPRDYS 231
Cdd:cd14152  162 HDWL---CYLAPEIVREMtpgkdedclPFSKAADVYAFGTIWYELQARDWPLKNQPAEALIWQIGSGegmKQVLTTISLG 238
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 148839316 232 PELAELIRTMLSKRPEERPSVRSIL----RQPYIKRQIS 266
Cdd:cd14152  239 KEVTEILSACWAFDLEERPSFTLLMdmleKLPKLNRRLS 277
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
13-257 6.16e-13

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. In the case of Jak2, the presumed pseudokinase (repeat 1) domain exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270633 [Multi-domain]  Cd Length: 259  Bit Score: 69.82  E-value: 6.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  13 GKGSYGEVTLVKHRRDGKQYVIKK---LNLRNASSRERRAAEQE-AQLLSQLKHPNIVtykesweggdgLLY-------- 80
Cdd:cd05037    8 GQGTFTNIYDGILREVGDGRVQEVevlLKVLDSDHRDISESFFEtASLMSQISHKHLV-----------KLYgvcvaden 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  81 -IVMGFCEGGDLYRKLKEQKGqllpeNQVVEWFV----QIAMALQYLHEKHILHRDLKTQNVFLTRTNI------IKVGD 149
Cdd:cd05037   77 iMVQEYVRYGPLDKYLRRMGN-----NVPLSWKLqvakQLASALHYLEDKKLIHGNVRGRNILLAREGLdgyppfIKLSD 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 150 LGIARVLENHCDMASTLIGTPYYMSPELFSNkpYNYKSDVWALGCCVYEMAT-LKHAFNAKDMNSLVYRIIEGKLPPMPR 228
Cdd:cd05037  152 PGVPITVLSREERVDRIPWIAPECLRNLQAN--LTIAADKWSFGTTLWEICSgGEEPLSALSSQEKLQFYEDQHQLPAPD 229
                        250       260
                 ....*....|....*....|....*....
gi 148839316 229 dySPELAELIRTMLSKRPEERPSVRSILR 257
Cdd:cd05037  230 --CAELAELIMQCWTYEPTKRPSFRAILR 256
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
112-253 6.82e-13

Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PINK1 contains an N-terminal mitochondrial targeting sequence, a catalytic domain, and a C-terminal regulatory region. It plays an important role in maintaining mitochondrial homeostasis. It protects cells against oxidative stress-induced apoptosis by phosphorylating the chaperone TNFR-associated protein 1 (TRAP1), also called Hsp75. Phosphorylated TRAP1 prevents cytochrome c release and peroxide-induced apoptosis. PINK1 interacts with Omi/HtrA2, a serine protease, and Parkin, an E3 ubiquitin ligase, in different pathways to promote mitochondrial health. The parkin gene is the most commonly mutated gene in autosomal recessive familial parkinsonism. Mutations within the catalytic domain of PINK1 are also associated with Parkinson's disease. The PINK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270920 [Multi-domain]  Cd Length: 313  Bit Score: 70.60  E-value: 6.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 112 FVQIAMALQYLHEKHILHRDLKTQNVFLTRTN----IIKVGDLGIARVLENH---CDMASTLI---GTPYYMSPELFSNK 181
Cdd:cd14018  144 ILQLLEGVDHLVRHGIAHRDLKSDNILLELDFdgcpWLVIADFGCCLADDSIglqLPFSSWYVdrgGNACLMAPEVSTAV 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 182 P-----YNY-KSDVWALGCCVYEMATLKHAF---NAKDMNSLVYRiiEGKLPPMPRDYSPELAELIRTMLSKRPEERPSV 252
Cdd:cd14018  224 PgpgvvINYsKADAWAVGAIAYEIFGLSNPFyglGDTMLESRSYQ--ESQLPALPSAVPPDVRQVVKDLLQRDPNKRVSA 301

                 .
gi 148839316 253 R 253
Cdd:cd14018  302 R 302
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
114-224 7.56e-13

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: 70.33  E-value: 7.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 114 QIAMALQYLHEKHILHRDLKTQNVFLT-RTNIIKVGDLGIA-RVLENHCdmastligTPY-----YMSPELFSNKPYNYK 186
Cdd:cd14135  113 QLFLALKHLKKCNILHADIKPDNILVNeKKNTLKLCDFGSAsDIGENEI--------TPYlvsrfYRAPEIILGLPYDYP 184
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 148839316 187 SDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIE--GKLP 224
Cdd:cd14135  185 IDMWSVGCTLYELYTGKILFPGKTNNHMLKLMMDlkGKFP 224
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
102-251 8.74e-13

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


Pssm-ID: 133238 [Multi-domain]  Cd Length: 401  Bit Score: 71.20  E-value: 8.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 102 LLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVL---ENHCDMASTLIGTPyYMSPELF 178
Cdd:cd05107  235 ALSYMDLVGFSYQVANGMEFLASKNCVHRDLAARNVLICEGKLVKICDFGLARDImrdSNYISKGSTFLPLK-WMAPESI 313
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148839316 179 SNKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLVYRIIE-GKLPPMPRDYSPELAELIRTMLSKRPEERPS 251
Cdd:cd05107  314 FNNLYTTLSDVWSFGILLWEIFTLGGTpYPELPMNEQFYNAIKrGYRMAKPAHASDEIYEIMQKCWEEKFEIRPD 388
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
24-256 9.18e-13

Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. ILK contains N-terminal ankyrin repeats, a Pleckstrin Homology (PH) domain, and a C-terminal pseudokinase domain. It is a component of the IPP (ILK/PINCH/Parvin) complex that couples beta integrins to the actin cytoskeleton, and plays important roles in cell adhesion, spreading, invasion, and migration. ILK was initially thought to be an active kinase despite the lack of key conserved residues because of in vitro studies showing that it can phosphorylate certain protein substrates. However, in vivo experiments in Caenorhabditis elegans, Drosophila melanogaster, and mice (ILK-null and knock-in) proved that ILK is not an active kinase. In addition to actin cytoskeleton regulation, ILK also influences the microtubule network and mitotic spindle orientation. The pseudokinase domain of ILK binds several adaptor proteins including the parvins and paxillin. The ILK subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270959 [Multi-domain]  Cd Length: 251  Bit Score: 69.05  E-value: 9.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  24 KHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLyIVMGFCEGGDLYRKLKEQKGQLL 103
Cdd:cd14057   13 KGRWQGNDIVAKILKVRDVTTRISRDFNEEYPRLRIFSHPNVLPVLGACNSPPNLV-VISQYMPYGSLYNVLHEGTGVVV 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 104 PENQVVEWFVQIAMALQYLH--EKHILHRDLKTQNVFLTR--TNIIKVGDLGIArvLENHCDMAStligtPYYMSPELFS 179
Cdd:cd14057   92 DQSQAVKFALDIARGMAFLHtlEPLIPRHHLNSKHVMIDEdmTARINMADVKFS--FQEPGKMYN-----PAWMAPEALQ 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 180 NKP--YNYKS-DVWALGCCVYEMATLKHAF-NAKDMNSLVYRIIEGKLPPMPRDYSPELAELIRTMLSKRPEERPSVRSI 255
Cdd:cd14057  165 KKPedINRRSaDMWSFAILLWELVTREVPFaDLSNMEIGMKIALEGLRVTIPPGISPHMCKLMKICMNEDPGKRPKFDMI 244

                 .
gi 148839316 256 L 256
Cdd:cd14057  245 V 245
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
12-202 1.12e-12

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


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 69.62  E-value: 1.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  12 VGKGSYGEVTLVK------------HRRDGKQYVIKKLNLR-NASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGL 78
Cdd:cd05097   13 LGEGQFGEVHLCEaeglaeflgegaPEFDGQPVLVAVKMLRaDVTKTARNDFLKEIKIMSRLKNPNIIRLLGVCVSDDPL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  79 LyIVMGFCEGGDLYRKL--KEQKGQLLPENQV--------VEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVG 148
Cdd:cd05097   93 C-MITEYMENGDLNQFLsqREIESTFTHANNIpsvsianlLYMAVQIASGMKYLASLNFVHRDLATRNCLVGNHYTIKIA 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 148839316 149 DLGIARVL--ENHCDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATL 202
Cdd:cd05097  172 DFGMSRNLysGDYYRIQGRAVLPIRWMAWESILLGKFTTASDVWAFGVTLWEMFTL 227
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
6-192 1.20e-12

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


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 68.82  E-value: 1.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316   6 YCYLRVVGKGSYGEVTLVKHRRDGKQYVIKKlnlrNASSRERRAAEQEAQLLSQL---KH-PNIVTYKESweggDGLLYI 81
Cdd:cd14017    2 WKVVKKIGGGGFGEIYKVRDVVDGEEVAMKV----ESKSQPKQVLKMEVAVLKKLqgkPHfCRLIGCGRT----ERYNYI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  82 VMGFCeGGDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRT----NIIKVGDLGIARVLE 157
Cdd:cd14017   74 VMTLL-GPNLAELRRSQPRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIGRGpsdeRTVYILDFGLARQYT 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 148839316 158 NHCD-------MASTLIGTPYYMSPELFSNKPYNYKSDVWAL 192
Cdd:cd14017  153 NKDGeverpprNAAGFRGTVRYASVNAHRNKEQGRRDDLWSW 194
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
47-255 1.22e-12

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: 69.28  E-value: 1.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  47 RRAAEQEAQLLSQLKHPNIV-----TYKESweggdgLLYIVMGFCEGGDLYRKL---------------KEQKGQLLPEN 106
Cdd:cd05091   53 REEFRHEAMLRSRLQHPNIVcllgvVTKEQ------PMSMIFSYCSHGDLHEFLvmrsphsdvgstdddKTVKSTLEPAD 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 107 qVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARvlENHCDMASTLIGTPY----YMSPELFSNKP 182
Cdd:cd05091  127 -FLHIVTQIAAGMEYLSSHHVVHKDLATRNVLVFDKLNVKISDLGLFR--EVYAADYYKLMGNSLlpirWMSPEAIMYGK 203
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148839316 183 YNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGK-LPPMPRDYSPELAELIRTMLSKRPEERPSVRSI 255
Cdd:cd05091  204 FSIDSDIWSYGVVLWEVFSYGLQPYCGYSNQDVIEMIRNRqVLPCPDDCPAWVYTLMLECWNEFPSRRPRFKDI 277
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
14-201 1.43e-12

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: 69.28  E-value: 1.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  14 KGSYGEVTlvKHRRDGKQYVIKKLNLRNASSRErraAEQEAQLLSQLKHPNIVTYKESWEGGDGL---LYIVMGFCEGGD 90
Cdd:cd14053    5 RGRFGAVW--KAQYLNRLVAVKIFPLQEKQSWL---TEREIYSLPGMKHENILQFIGAEKHGESLeaeYWLITEFHERGS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  91 LYRKLKeqkgqllpeNQVVEW--FVQIAMA----LQYLHE----------KHILHRDLKTQNVFLTRTNIIKVGDLGIAR 154
Cdd:cd14053   80 LCDYLK---------GNVISWneLCKIAESmargLAYLHEdipatngghkPSIAHRDFKSKNVLLKSDLTACIADFGLAL 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 148839316 155 VLENHCDMASTL--IGTPYYMSPEL------FSNKPYnYKSDVWALGCCVYEMAT 201
Cdd:cd14053  151 KFEPGKSCGDTHgqVGTRRYMAPEVlegainFTRDAF-LRIDMYAMGLVLWELLS 204
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
10-200 1.53e-12

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: 68.91  E-value: 1.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVKHRrdGKQYVIKKLNLRNASSRERraaEQEAQLLSQLKHPNIVTYKESWEGGDGL---LYIVMGFC 86
Cdd:cd14220    1 RQIGKGRYGEVWMGKWR--GEKVAVKVFFTTEEASWFR---ETEIYQTVLMRHENILGFIAADIKGTGSwtqLYLITDYH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  87 EGGDLYRKLKeqkGQLLPENQVVEWFVQIAMALQYLHEK--------HILHRDLKTQNVFLTRTNIIKVGDLGIARVLE- 157
Cdd:cd14220   76 ENGSLYDFLK---CTTLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGTCCIADLGLAVKFNs 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 148839316 158 --NHCDMA-STLIGTPYYMSPELFSN-------KPYnYKSDVWALGCCVYEMA 200
Cdd:cd14220  153 dtNEVDVPlNTRVGTKRYMAPEVLDEslnknhfQAY-IMADIYSFGLIIWEMA 204
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
10-251 1.63e-12

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


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 69.62  E-value: 1.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  10 RVVGKGSYGEVTLVK----HRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQL-KHPNIVTYKESWEGGDGLLYIVMG 84
Cdd:cd05102   13 KVLGHGAFGKVVEASafgiDKSSSCETVAVKMLKEGATASEHKALMSELKILIHIgNHLNVVNLLGACTKPNGPLMVIVE 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  85 FCEGGDLYRKLKEQKGQLLPENQ-----------VVE------------------------------------------- 110
Cdd:cd05102   93 FCKYGNLSNFLRAKREGFSPYRErsprtrsqvrsMVEavradrrsrqgsdrvasftestsstnqprqevddlwqspltme 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316 111 ----WFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHCDMASTliGTPY----YMSPELFSNKP 182
Cdd:cd05102  173 dlicYSFQVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKDPDYVRK--GSARlplkWMAPESIFDKV 250
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148839316 183 YNYKSDVWALGCCVYEMATLKHA-FNAKDMNS-LVYRIIEGKLPPMPRDYSPELAELIRTMLSKRPEERPS 251
Cdd:cd05102  251 YTTQSDVWSFGVLLWEIFSLGASpYPGVQINEeFCQRLKDGTRMRAPEYATPEIYRIMLSCWHGDPKERPT 321
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
88-224 2.11e-12

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: 69.20  E-value: 2.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148839316  88 GGDLYRKLKEQKGQLLPENQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTN--IIKVGDLGIArvlenhCDMAST 165
Cdd:cd14212   85 GVNLYELLKQNQFRGLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNLDspEIKLIDFGSA------CFENYT 158
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148839316 166 L---IGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIE--GKLP 224
Cdd:cd14212  159 LytyIQSRFYRSPEVLLGLPYSTAIDMWSLGCIAAELFLGLPLFPGNSEYNQLSRIIEmlGMPP 222
 
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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