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Conserved domains on  [gi|41055987|ref|NP_957306|]
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serine/threonine-protein kinase Nek4 [Danio rerio]

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 ...
3-259 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: 543.18  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   3 GYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDCQLYIVMG 82
Cdd:cd08223   1 EYQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKAAEQEAKLLSKLKHPNIVSYKESFEGEDGFLYIVMG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FCEGGDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMAS 162
Cdd:cd08223  81 FCEGGDLYTRLKEQKGVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLESSSDMAT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 163 TLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPSKYDPQLGELIKRMLCK 242
Cdd:cd08223 161 TLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEGKLPPMPKQYSPELGELIKAMLHQ 240
                       250
                ....*....|....*..
gi 41055987 243 KPEDRPDVKHILRQPYI 259
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 ...
3-259 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: 543.18  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   3 GYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDCQLYIVMG 82
Cdd:cd08223   1 EYQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKAAEQEAKLLSKLKHPNIVSYKESFEGEDGFLYIVMG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FCEGGDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMAS 162
Cdd:cd08223  81 FCEGGDLYTRLKEQKGVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLESSSDMAT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 163 TLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPSKYDPQLGELIKRMLCK 242
Cdd:cd08223 161 TLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEGKLPPMPKQYSPELGELIKAMLHQ 240
                       250
                ....*....|....*..
gi 41055987 243 KPEDRPDVKHILRQPYI 259
Cdd:cd08223 241 DPEKRPSVKRILRQPYI 257
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
4-259 3.24e-92

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 290.59  E-value: 3.24e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987      4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRtSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDCqLYIVMGF 83
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKK-KIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDK-LYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987     84 CEGGDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENqNDMAST 163
Cdd:smart00220  79 CEGGDLFDLLKKRGR--LSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDP-GEKLTT 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987    164 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPS---KYDPQLGELIKRML 240
Cdd:smart00220 156 FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPpewDISPEAKDLIRKLL 235
                          250
                   ....*....|....*....
gi 41055987    241 CKKPEDRPDVKHILRQPYI 259
Cdd:smart00220 236 VKDPEKRLTAEEALQHPFF 254
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
2-248 2.05e-69

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 237.60  E-value: 2.05e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLR-TSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIV 80
Cdd:COG0515   7 GRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPElAADPEARERFRREARALARLNHPNIVRVYDVGEEDG-RPYLV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MGFCEGGDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQN-D 159
Cdd:COG0515  86 MEYVEGESLADLLRRRGP--LPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATlT 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 160 MASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLP---QMPSKYDPQLGELI 236
Cdd:COG0515 164 QTGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPppsELRPDLPPALDAIV 243
                       250
                ....*....|..
gi 41055987 237 KRMLCKKPEDRP 248
Cdd:COG0515 244 LRALAKDPEERY 255
Pkinase pfam00069
Protein kinase domain;
4-259 4.61e-50

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 175.51  E-value: 4.61e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987     4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGF 83
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKD-NLYLVLEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987    84 CEGGDLYHRLKQQKGelLPERQVVEWFVQiamalqylhekhilhrdlktqnifltktniikvgdlgIARVLENQNDMaST 163
Cdd:pfam00069  80 VEGGSLFDLLSEKGA--FSEREAKFIMKQ-------------------------------------ILEGLESGSSL-TT 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   164 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQM--PSKYDPQLGELIKRMLC 241
Cdd:pfam00069 120 FVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPelPSNLSEEAKDLLKKLLK 199
                         250
                  ....*....|....*...
gi 41055987   242 KKPEDRPDVKHILRQPYI 259
Cdd:pfam00069 200 KDPSKRLTATQALQHPWF 217
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
4-309 4.80e-44

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 166.35  E-value: 4.80e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987    4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLnLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGF 83
Cdd:PTZ00267  69 YVLTTLVGRNPTTAAFVATRGSDPKEKVVAKF-VMLNDERQAAYARSELHCLAACDHFGIVKHFDDFKSDD-KLLLIMEY 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   84 CEGGDLYHRLKQQKGELLP--ERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQN--D 159
Cdd:PTZ00267 147 GSGGDLNKQIKQRLKEHLPfqEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQYSDSVslD 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  160 MASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPSKYDPQLGELIKRM 239
Cdd:PTZ00267 227 VASSFCGTPYYLAPELWERKRYSKKADMWSLGVILYELLTLHRPFKGPSQREIMQQVLYGKYDPFPCPVSSGMKALLDPL 306
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  240 LCKKPEDRPDVKHILRQPYIKHQISMFLEATKEKTAKSRKNAANGKLNSAGSDASTKPNQVVQPQCLNSE 309
Cdd:PTZ00267 307 LSKNPALRPTTQQLLHTEFLKYVANLFQDIVRHSETISPHDREEILRQLQESGERAPPPSSIRYGVVTSD 376
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
42-249 1.27e-34

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 139.93  E-value: 1.27e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   42 RRERRaaeqEAQLLSQLKHPNIV-MYrESWEGEDCQlYIVMGFCEGGDLyHRLKQQKGELLPERqVVEWFVQIAMALQYL 120
Cdd:NF033483  52 ARFRR----EAQSAASLSHPNIVsVY-DVGEDGGIP-YIVMEYVDGRTL-KDYIREHGPLSPEE-AVEIMIQILSALEHA 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  121 HEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLeNQNDMAST--LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMA 198
Cdd:NF033483 124 HRNGIVHRDIKPQNILITKDGRVKVTDFGIARAL-SSTTMTQTnsVLGTVHYLSPEQARGGTVDARSDIYSLGIVLYEML 202
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41055987  199 T--------------LKHaFNaKDMNSlvyrivegklpqmPSKYDP----QLGELIKRMLCKKPEDRPD 249
Cdd:NF033483 203 TgrppfdgdspvsvaYKH-VQ-EDPPP-------------PSELNPgipqSLDAVVLKATAKDPDDRYQ 256
 
Name Accession Description Interval E-value
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
3-259 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: 543.18  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   3 GYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDCQLYIVMG 82
Cdd:cd08223   1 EYQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKAAEQEAKLLSKLKHPNIVSYKESFEGEDGFLYIVMG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FCEGGDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMAS 162
Cdd:cd08223  81 FCEGGDLYTRLKEQKGVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLESSSDMAT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 163 TLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPSKYDPQLGELIKRMLCK 242
Cdd:cd08223 161 TLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEGKLPPMPKQYSPELGELIKAMLHQ 240
                       250
                ....*....|....*..
gi 41055987 243 KPEDRPDVKHILRQPYI 259
Cdd:cd08223 241 DPEKRPSVKRILRQPYI 257
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
3-259 3.15e-152

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: 446.52  E-value: 3.15e-152
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   3 GYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDCqLYIVMG 82
Cdd:cd08215   1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMSEKEREEALNEVKLLSKLKHPNIVKYYESFEENGK-LCIVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FCEGGDLYHRLKQQK--GELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDM 160
Cdd:cd08215  80 YADGGDLAQKIKKQKkkGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISKVLESTTDL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 161 ASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPSKYDPQLGELIKRML 240
Cdd:cd08215 160 AKTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYPPIPSQYSSELRDLVNSML 239
                       250
                ....*....|....*....
gi 41055987 241 CKKPEDRPDVKHILRQPYI 259
Cdd:cd08215 240 QKDPEKRPSANEILSSPFI 258
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
4-259 3.39e-110

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: 337.94  E-value: 3.39e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEgEDCQLYIVMGF 83
Cdd:cd08218   2 YVRIKKIGEGSFGKALLVKSKEDGKQYVIKEINISKMSPKEREESRKEVAVLSKMKHPNIVQYQESFE-ENGNLYIVMDY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGGDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMAST 163
Cdd:cd08218  81 CDGGDLYKRINAQRGVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVLNSTVELART 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 164 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPSKYDPQLGELIKRMLCKK 243
Cdd:cd08218 161 CIGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKIIRGSYPPVPSRYSYDLRSLVSQLFKRN 240
                       250
                ....*....|....*.
gi 41055987 244 PEDRPDVKHILRQPYI 259
Cdd:cd08218 241 PRDRPSINSILEKPFI 256
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
10-257 1.22e-97

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: 305.10  E-value: 1.22e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEgEDCQLYIVMGFCEGGDL 89
Cdd:cd08529   8 LGKGSFGVVYKVVRKVDGRVYALKQIDISRMSRKMREEAIDEARVLSKLNSPYVIKYYDSFV-DKGKLNIVMEYAENGDL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  90 YHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLIGTPY 169
Cdd:cd08529  87 HSLIKSQRGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAKILSDTTNFAQTIVGTPY 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 170 YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPSKYDPQLGELIKRMLCKKPEDRPD 249
Cdd:cd08529 167 YLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKYPPISASYSQDLSQLIDSCLTKDYRQRPD 246

                ....*...
gi 41055987 250 VKHILRQP 257
Cdd:cd08529 247 TTELLRNP 254
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
4-259 3.24e-92

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 290.59  E-value: 3.24e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987      4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRtSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDCqLYIVMGF 83
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKK-KIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDK-LYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987     84 CEGGDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENqNDMAST 163
Cdd:smart00220  79 CEGGDLFDLLKKRGR--LSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDP-GEKLTT 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987    164 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPS---KYDPQLGELIKRML 240
Cdd:smart00220 156 FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPpewDISPEAKDLIRKLL 235
                          250
                   ....*....|....*....
gi 41055987    241 CKKPEDRPDVKHILRQPYI 259
Cdd:smart00220 236 VKDPEKRLTAEEALQHPFF 254
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
4-259 1.13e-91

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: 289.44  E-value: 1.13e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMY------RESwegedCQL 77
Cdd:cd08217   2 YEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDYGKMSEKEKQQLVSEVNILRELKHPNIVRYydrivdRAN-----TTL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  78 YIVMGFCEGGDLYHRLKQQK--GELLPERQVVEWFVQIAMALQYLHEKH-----ILHRDLKTQNIFLTKTNIIKVGDLGI 150
Cdd:cd08217  77 YIVMEYCEGGDLAQLIKKCKkeNQYIPEEFIWKIFTQLLLALYECHNRSvgggkILHRDLKPANIFLDSDNNVKLGDFGL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 151 ARVLENQNDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPSKYDP 230
Cdd:cd08217 157 ARVLSHDSSFAKTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAANQLELAKKIKEGKFPRIPSRYSS 236
                       250       260
                ....*....|....*....|....*....
gi 41055987 231 QLGELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd08217 237 ELNEVIKSMLNVDPDKRPSVEELLQLPLI 265
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
4-259 1.13e-89

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: 284.32  E-value: 1.13e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLV---RHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGED--Cqly 78
Cdd:cd08222   2 YRVVRKLGSGNFGTVYLVsdlKATADEELKVLKEISVGELQPDETVDANREAKLLSKLDHPAIVKFHDSFVEKEsfC--- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  79 IVMGFCEGGDLYHRLKQ--QKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLtKTNIIKVGDLGIARVLEN 156
Cdd:cd08222  79 IVTEYCEGGDLDDKISEykKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFL-KNNVIKVGDFGISRILMG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 157 QNDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPSKYDPQLGELI 236
Cdd:cd08222 158 TSDLATTFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVEGETPSLPDKYSKELNAIY 237
                       250       260
                ....*....|....*....|...
gi 41055987 237 KRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd08222 238 SRMLNKDPALRPSAAEILKIPFI 260
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
4-254 9.39e-88

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: 279.17  E-value: 9.39e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRrERRAAEQEAQLLSQLKHPNIVMYRESWEGeDCQLYIVMGF 83
Cdd:cd08219   2 YNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIRLPKSSS-AVEDSRKEAVLLAKMKHPNIVAFKESFEA-DGHLYIVMEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGGDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMAST 163
Cdd:cd08219  80 CDGGDLMQKIKLQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSPGAYACT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 164 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPSKYDPQLGELIKRMLCKK 243
Cdd:cd08219 160 YVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGSYKPLPSHYSYELRSLIKQMFKRN 239
                       250
                ....*....|.
gi 41055987 244 PEDRPDVKHIL 254
Cdd:cd08219 240 PRSRPSATTIL 250
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
4-259 2.33e-86

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: 275.30  E-value: 2.33e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEgEDCQLYIVMGF 83
Cdd:cd08225   2 YEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKEKEASKKEVILLAKMKHPNIVTFFASFQ-ENGRLFIVMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGGDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNII-KVGDLGIARVLENQNDMAS 162
Cdd:cd08225  81 CDGGDLMKRINRQRGVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVaKLGDFGIARQLNDSMELAY 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 163 TLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPSKYDPQLGELIKRMLCK 242
Cdd:cd08225 161 TCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNNLHQLVLKICQGYFAPISPNFSRDLRSLISQLFKV 240
                       250
                ....*....|....*..
gi 41055987 243 KPEDRPDVKHILRQPYI 259
Cdd:cd08225 241 SPRDRPSITSILKRPFL 257
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
4-259 1.10e-84

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: 270.84  E-value: 1.10e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEgEDCQLYIVMGF 83
Cdd:cd08221   2 YIPVRVLGRGAFGEAVLYRKTEDNSLVVWKEVNLSRLSEKERRDALNEIDILSLLNHDNIITYYNHFL-DGESLFIEMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGGDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMAST 163
Cdd:cd08221  81 CNGGNLHDKIAQQKNQLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVLDSESSMAES 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 164 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPSKYDPQLGELIKRMLCKK 243
Cdd:cd08221 161 IVGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFDATNPLRLAVKIVQGEYEDIDEQYSEEIIQLVHDCLHQD 240
                       250
                ....*....|....*.
gi 41055987 244 PEDRPDVKHILRQPYI 259
Cdd:cd08221 241 PEDRPTAEELLERPLL 256
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
3-257 1.50e-84

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: 270.42  E-value: 1.50e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   3 GYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEgEDCQLYIVMG 82
Cdd:cd08530   1 DFKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLGSLSQKEREDSVNEIRLLASVNHPNIIRYKEAFL-DGNRLCIVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FCEGGDLYHRLK--QQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQndM 160
Cdd:cd08530  80 YAPFGDLSKLISkrKKKRRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISKVLKKN--L 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 161 ASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPSKYDPQLGELIKRML 240
Cdd:cd08530 158 AKTQIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQELRYKVCRGKFPPIPPVYSQDLQQIIRSLL 237
                       250
                ....*....|....*..
gi 41055987 241 CKKPEDRPDVKHILRQP 257
Cdd:cd08530 238 QVNPKKRPSCDKLLQSP 254
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
4-259 2.43e-81

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: 261.98  E-value: 2.43e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEgEDCQLYIVMGF 83
Cdd:cd08220   2 YEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIPVEQMTKEERQAALNEVKVLSMLHHPNIIEYYESFL-EDKALMIVMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGGDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTK-TNIIKVGDLGIARVLeNQNDMAS 162
Cdd:cd08220  81 APGGTLFEYIQQRKGSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKkRTVVKIGDFGISKIL-SSKSKAY 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 163 TLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPSKYDPQLGELIKRMLCK 242
Cdd:cd08220 160 TVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMRGTFAPISDRYSEELRHLILSMLHL 239
                       250
                ....*....|....*..
gi 41055987 243 KPEDRPDVKHILRQPYI 259
Cdd:cd08220 240 DPNKRPTLSEIMAQPII 256
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
10-256 8.12e-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: 239.48  E-value: 8.12e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNL-RTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEgEDCQLYIVMGFCEGGD 88
Cdd:cd08224   8 IGKGQFSVVYRARCLLDGRLVALKKVQIfEMMDAKARQDCLKEIDLLQQLNHPNIIKYLASFI-ENNELNIVLELADAGD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  89 LYHRLK--QQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLIG 166
Cdd:cd08224  87 LSRLIKhfKKQKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGLGRFFSSKTTAAHSLVG 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 167 TPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMN--SLVYRIVEGKLPQMPSK-YDPQLGELIKRMLCKK 243
Cdd:cd08224 167 TPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYGEKMNlySLCKKIEKCEYPPLPADlYSQELRDLVAACIQPD 246
                       250
                ....*....|...
gi 41055987 244 PEDRPDVKHILRQ 256
Cdd:cd08224 247 PEKRPDISYVLDV 259
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
3-248 8.92e-72

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: 236.33  E-value: 8.92e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   3 GYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRE-RRAAEQEAQLLSQLKHPNIVMYRESWEgEDCQLYIVM 81
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEfRERFLREARALARLSHPNIVRVYDVGE-DDGRPYIVM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  82 GFCEGGDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVL-ENQNDM 160
Cdd:cd14014  80 EYVEGGSLADLLRERGP--LPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALgDSGLTQ 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 161 ASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGK---LPQMPSKYDPQLGELIK 237
Cdd:cd14014 158 TGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEApppPSPLNPDVPPALDAIIL 237
                       250
                ....*....|.
gi 41055987 238 RMLCKKPEDRP 248
Cdd:cd14014 238 RALAKDPEERP 248
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
2-248 2.05e-69

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 237.60  E-value: 2.05e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLR-TSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIV 80
Cdd:COG0515   7 GRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPElAADPEARERFRREARALARLNHPNIVRVYDVGEEDG-RPYLV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MGFCEGGDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQN-D 159
Cdd:COG0515  86 MEYVEGESLADLLRRRGP--LPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATlT 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 160 MASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLP---QMPSKYDPQLGELI 236
Cdd:COG0515 164 QTGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPppsELRPDLPPALDAIV 243
                       250
                ....*....|..
gi 41055987 237 KRMLCKKPEDRP 248
Cdd:COG0515 244 LRALAKDPEERY 255
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
11-257 1.27e-68

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: 226.38  E-value: 1.27e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  11 GKGSYGEVNLVRHKSDRKQYVIKKLNLRtSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDCqLYIVMGFCEGGDLY 90
Cdd:cd00180   2 GKGSFGKVYKARDKETGKKVAVKVIPKE-KLKKLLEELLREIEILKKLNHPNIVKLYDVFETENF-LYLVMEYCEGGSLK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  91 HRLKQQKGELlPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLIG--TP 168
Cdd:cd00180  80 DLLKENKGPL-SEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKTTGGttPP 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 169 YYMSPELFSNKPYNYKSDVWALGCCVYEMATLKhafnakdmnslvyrivegklpqmpskydpqlgELIKRMLCKKPEDRP 248
Cdd:cd00180 159 YYAPPELLGGRYYGPKVDIWSLGVILYELEELK--------------------------------DLIRRMLQYDPKKRP 206

                ....*....
gi 41055987 249 DVKHILRQP 257
Cdd:cd00180 207 SAKELLEHL 215
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
4-257 2.17e-67

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 224.66  E-value: 2.17e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGF 83
Cdd:cd05117   2 YELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDK-NLYLVMEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGGDLYHRLKQQKgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNI---IKVGDLGIARVLENQNDM 160
Cdd:cd05117  81 CTGGELFDRIVKKG--SFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPdspIKIIDFGLAKIFEEGEKL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 161 aSTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLpQMPSKY----DPQLGELI 236
Cdd:cd05117 159 -KTVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKY-SFDSPEwknvSEEAKDLI 236
                       250       260
                ....*....|....*....|.
gi 41055987 237 KRMLCKKPEDRPDVKHILRQP 257
Cdd:cd05117 237 KRLLVVDPKKRLTAAEALNHP 257
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
8-259 2.41e-65

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: 218.93  E-value: 2.41e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESwEGEDCQLYIVMGFCEGG 87
Cdd:cd06606   6 ELLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEELEALEREIRILSSLKHPNIVRYLGT-ERTENTLNIFLEYVPGG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  88 DLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLE--NQNDMASTLI 165
Cdd:cd06606  85 SLASLLKKFGK--LPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKRLAeiATGEGTKSLR 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 166 GTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAF-NAKDMNSLVYRIVEGK-LPQMPSKYDPQLGELIKRMLCKK 243
Cdd:cd06606 163 GTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWsELGNPVAALFKIGSSGePPPIPEHLSEEAKDFLRKCLQRD 242
                       250
                ....*....|....*.
gi 41055987 244 PEDRPDVKHILRQPYI 259
Cdd:cd06606 243 PKKRPTADELLQHPFL 258
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
10-254 4.22e-64

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: 215.09  E-value: 4.22e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSdrKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYResweG---EDCQLYIVMGFCEG 86
Cdd:cd13999   1 IGSGSFGEVYKGKWRG--TDVAIKKLKVEDDNDELLKEFRREVSILSKLRHPNIVQFI----GaclSPPPLCIVTEYMPG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  87 GDLYHRLKQQKGELlPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLIG 166
Cdd:cd13999  75 GSLYDLLHKKKIPL-SWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKMTGVVG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 167 TPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAF-NAKDMNSLVYRIVEGKLPQMPSKYDPQLGELIKRMLCKKPE 245
Cdd:cd13999 154 TPRWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFkELSPIQIAAAVVQKGLRPPIPPDCPPELSKLIKRCWNEDPE 233

                ....*....
gi 41055987 246 DRPDVKHIL 254
Cdd:cd13999 234 KRPSFSEIV 242
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
4-259 7.32e-62

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: 209.37  E-value: 7.32e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAaeQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGF 83
Cdd:cd05122   2 FEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEKKESIL--NEIAILKKCKHPNIVKYYGSYLKKD-ELWIVMEF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGGDLYHRLKQqKGELLPERQVVewFV--QIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDmA 161
Cdd:cd05122  79 CSGGSLKDLLKN-TNKTLTEQQIA--YVckEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQLSDGKT-R 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 162 STLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLP--QMPSKYDPQLGELIKRM 239
Cdd:cd05122 155 NTFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIATNGPPglRNPKKWSKEFKDFLKKC 234
                       250       260
                ....*....|....*....|
gi 41055987 240 LCKKPEDRPDVKHILRQPYI 259
Cdd:cd05122 235 LQKDPEKRPTAEQLLKHPFI 254
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
6-260 4.22e-61

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: 207.33  E-value: 4.22e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   6 FVRVVGKGSYGEVNLVRHKSDRKQYVIKKLnlrtsSRRERRAAEQEAQLL------SQLKHPNIV-MYreSWEGEDCQLY 78
Cdd:cd14007   4 IGKPLGKGKFGNVYLAREKKSGFIVALKVI-----SKSQLQKSGLEHQLRreieiqSHLRHPNILrLY--GYFEDKKRIY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  79 IVMGFCEGGDLYHRLKQQKgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARvlENQN 158
Cdd:cd14007  77 LILEYAPNGELYKELKKQK--RFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWSV--HAPS 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 159 DMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLpQMPSKYDPQLGELIKR 238
Cdd:cd14007 153 NRRKTFCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDI-KFPSSVSPEAKDLISK 231
                       250       260
                ....*....|....*....|..
gi 41055987 239 MLCKKPEDRPDVKHILRQPYIK 260
Cdd:cd14007 232 LLQKDPSKRLSLEQVLNHPWIK 253
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
4-258 7.07e-61

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: 206.60  E-value: 7.07e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGF 83
Cdd:cd14003   2 YELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETEN-KIYLVMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGGDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENqNDMAST 163
Cdd:cd14003  81 ASGGELFDYIVNNGR--LSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNEFRG-GSLLKT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 164 LIGTPYYMSPELFSNKPYN-YKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPqMPSKYDPQLGELIKRMLCK 242
Cdd:cd14003 158 FCGTPAYAAPEVLLGRKYDgPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYP-IPSHLSPDARDLIRRMLVV 236
                       250
                ....*....|....*.
gi 41055987 243 KPEDRPDVKHILRQPY 258
Cdd:cd14003 237 DPSKRITIEEILNHPW 252
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
7-261 1.49e-59

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: 203.59  E-value: 1.49e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   7 VRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLrTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEgEDCQLYIVMGFCEG 86
Cdd:cd06623   6 VKVLGQGSSGVVYKVRHKPTGKIYALKKIHV-DGDEEFRKQLLRELKTLRSCESPYVVKCYGAFY-KEGEISIVLEYMDG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  87 GDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLH-EKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLI 165
Cdd:cd06623  84 GSLADLLKKVGK--IPEPVLAYIARQILKGLDYLHtKRHIIHRDIKPSNLLINSKGEVKIADFGISKVLENTLDQCNTFV 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 166 GTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNS---LVYRIVEGKLPQMPSK-YDPQLGELIKRMLC 241
Cdd:cd06623 162 GTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPGQPSffeLMQAICDGPPPSLPAEeFSPEFRDFISACLQ 241
                       250       260
                ....*....|....*....|
gi 41055987 242 KKPEDRPDVKHILRQPYIKH 261
Cdd:cd06623 242 KDPKKRPSAAELLQHPFIKK 261
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
11-259 2.97e-59

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: 202.78  E-value: 2.97e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  11 GKGSYGEVNLVRHKSDRKQYVIKKLN---LRTSSRRERRAAEQEAQL---------LSQLKHPNIVMYRESWEGEDCQ-L 77
Cdd:cd14008   2 GRGSFGKVKLALDTETGQLYAIKIFNksrLRKRREGKNDRGKIKNALddvrreiaiMKKLDHPNIVRLYEVIDDPESDkL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  78 YIVMGFCEGGDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQ 157
Cdd:cd14008  82 YLVLEYCEGGPVMELDSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGVSEMFEDG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 158 NDMASTLIGTPYYMSPELF--SNKPYN-YKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPSKY-DPQLG 233
Cdd:cd14008 162 NDTLQKTAGTPAFLAPELCdgDSKTYSgKAADIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQNDEFPIPPElSPELK 241
                       250       260
                ....*....|....*....|....*.
gi 41055987 234 ELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd14008 242 DLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
10-247 7.67e-59

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: 200.82  E-value: 7.67e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRT-SSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEGGD 88
Cdd:cd05123   1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEiIKRKEVEHTLNERNILERVNHPFIVKLHYAFQTEE-KLYLVLDYVPGGE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  89 LYHRLKQQKgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLIGTP 168
Cdd:cd05123  80 LFSHLSKEG--RFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSDGDRTYTFCGTP 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41055987 169 YYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLpQMPSKYDPQLGELIKRMLCKKPEDR 247
Cdd:cd05123 158 EYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPL-KFPEYVSPEAKSLISGLLQKDPTKR 235
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
4-255 1.65e-58

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 is required for the transition from metaphase to anaphase. It also plays important roles in mitotic spindle formation and cytokinesis. Activated by Nek9 during mitosis, Nek6 phosphorylates Eg5, a kinesin that is important for spindle bipolarity. Nek6 localizes to spindle microtubules during metaphase and anaphase, and to the midbody during cytokinesis. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 200.64  E-value: 1.65e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNL-RTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEgEDCQLYIVMG 82
Cdd:cd08228   4 FQIEKKIGRGQFSEVYRATCLLDRKPVALKKVQIfEMMDAKARQDCVKEIDLLKQLNHPNVIKYLDSFI-EDNELNIVLE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FCEGGDLYHRLK--QQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDM 160
Cdd:cd08228  83 LADAGDLSQMIKyfKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTA 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 161 ASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMN--SLVYRIVEGKLPQMPSK-YDPQLGELIK 237
Cdd:cd08228 163 AHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNlfSLCQKIEQCDYPPLPTEhYSEKLRELVS 242
                       250
                ....*....|....*...
gi 41055987 238 RMLCKKPEDRPDVKHILR 255
Cdd:cd08228 243 MCIYPDPDQRPDIGYVHQ 260
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
7-256 7.78e-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: 190.97  E-value: 7.78e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   7 VRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAaEQEAQLLSQLKHPNIVMYRESWEGEDCqLYIVMGFCEG 86
Cdd:cd13996  11 IELLGSGGFGSVYKVRNKVDGVTYAIKKIRLTEKSSASEKV-LREVKALAKLNHPNIVRYYTAWVEEPP-LYIQMELCEG 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  87 GDLYHRL-KQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTK-TNIIKVGDLGIARVLENQ------- 157
Cdd:cd13996  89 GTLRDWIdRRNSSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNdDLQVKIGDFGLATSIGNQkrelnnl 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 158 -------NDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMAtlkHAFN-----AKDMNSLvyriVEGKLPQMP 225
Cdd:cd13996 169 nnnnngnTSNNSVGIGTPLYASPEQLDGENYNEKADIYSLGIILFEML---HPFKtamerSTILTDL----RNGILPESF 241
                       250       260       270
                ....*....|....*....|....*....|.
gi 41055987 226 SKYDPQLGELIKRMLCKKPEDRPDVKHILRQ 256
Cdd:cd13996 242 KAKHPKEADLIQSLLSKNPEERPSAEQLLRS 272
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
4-259 2.29e-54

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: 188.92  E-value: 2.29e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQY---VIKKLNLRTSSRRERraAEQEAQLLSQLKHPNIVMYRESWEGEDCqLYIV 80
Cdd:cd14099   3 YRRGKFLGKGGFAKCYEVTDMSTGKVYagkVVPKSSLTKPKQREK--LKSEIKIHRSLKHPNIVKFHDCFEDEEN-VYIL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MGFCEGGDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDM 160
Cdd:cd14099  80 LELCSNGSLMELLKRRKA--LTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAARLEYDGER 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 161 ASTLIGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLpQMPSK--YDPQLGELIK 237
Cdd:cd14099 158 KKTLCGTPNYIAPEvLEKKKGHSFEVDIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNEY-SFPSHlsISDEAKDLIR 236
                       250       260
                ....*....|....*....|..
gi 41055987 238 RMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd14099 237 SMLQPDPTKRPSLDEILSHPFF 258
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
4-250 2.70e-53

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: 186.55  E-value: 2.70e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQ-YVIKKLNL------RTSSRRERRAAEQEAQLL---SQLKHPNIVMYRESWEGE 73
Cdd:cd08528   2 YAVLELLGSGAFGCVYKVRKKSNGQTlLALKEINMtnpafgRTEQERDKSVGDIISEVNiikEQLRHPNIVRYYKTFLEN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  74 DcQLYIVMGFCEG---GDLYHRLKQqKGELLPERQVVEWFVQIAMALQYLH-EKHILHRDLKTQNIFLTKTNIIKVGDLG 149
Cdd:cd08528  82 D-RLYIVMELIEGaplGEHFSSLKE-KNEHFTEDRIWNIFVQMVLALRYLHkEKQIVHRDLKPNNIMLGEDDKVTITDFG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 150 IARV-LENQNDMASTlIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPS-K 227
Cdd:cd08528 160 LAKQkGPESSKMTSV-VGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIVEAEYEPLPEgM 238
                       250       260
                ....*....|....*....|...
gi 41055987 228 YDPQLGELIKRMLCKKPEDRPDV 250
Cdd:cd08528 239 YSDDITFVIRSCLTPDPEARPDI 261
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
2-259 7.41e-52

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: 181.68  E-value: 7.41e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDCqLYIVM 81
Cdd:cd14002   1 ENYHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPKRGKSEKELRNLRQEIEILRKLNHPNIIEMLDSFETKKE-FVVVT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  82 GFCEGgDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLeNQNDMA 161
Cdd:cd14002  80 EYAQG-ELFQILEDDGT--LPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARAM-SCNTLV 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 162 STLI-GTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLpQMPSKYDPQLGELIKRML 240
Cdd:cd14002 156 LTSIkGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIVKDPV-KWPSNMSPEFKSFLQGLL 234
                       250
                ....*....|....*....
gi 41055987 241 CKKPEDRPDVKHILRQPYI 259
Cdd:cd14002 235 NKDPSKRLSWPDLLEHPFV 253
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
10-247 4.65e-51

Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes yeast ATG1 and metazoan homologs including vertebrate ULK1-3. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. It is involved in nutrient sensing and signaling, the assembly of autophagy factors and the execution of autophagy. In metazoans, ATG1 homologs display additional functions. Unc-51 and ULKs have been implicated in neuronal and axonal development. The ATG1/ULK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 179.34  E-value: 4.65e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEGGDL 89
Cdd:cd14009   1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNKKLQENLESEIAILKSIKHPNIVRLYDVQKTED-FIYLVLEYCAGGDL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  90 YHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTN---IIKVGDLGIARVLENQnDMASTLIG 166
Cdd:cd14009  80 SQYIRKRGR--LPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGddpVLKIADFGFARSLQPA-SMAETLCG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 167 TPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPqMPSKYDPQLG----ELIKRMLCK 242
Cdd:cd14009 157 SPLYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIERSDAV-IPFPIAAQLSpdckDLLRRLLRR 235

                ....*
gi 41055987 243 KPEDR 247
Cdd:cd14009 236 DPAER 240
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
8-259 1.47e-50

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: 178.36  E-value: 1.47e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAA---EQEAQLLSQLKHPNIVMYRESwEGEDCQLYIVMGFC 84
Cdd:cd06632   6 QLLGSGSFGSVYEGFNGDTGDFFAVKEVSLVDDDKKSRESVkqlEQEIALLSKLRHPNIVQYYGT-EREEDNLYIFLEYV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  85 EGGDLyHRLKQQKGELlPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQnDMASTL 164
Cdd:cd06632  85 PGGSI-HKLLQRYGAF-EEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHVEAF-SFAKSF 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 165 IGTPYYMSPELFS--NKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIV-EGKLPQMPSKYDPQLGELIKRMLC 241
Cdd:cd06632 162 KGSPYWMAPEVIMqkNSGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIGnSGELPPIPDHLSPDAKDFIRLCLQ 241
                       250
                ....*....|....*...
gi 41055987 242 KKPEDRPDVKHILRQPYI 259
Cdd:cd06632 242 RDPEDRPTASQLLEHPFV 259
Pkinase pfam00069
Protein kinase domain;
4-259 4.61e-50

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 175.51  E-value: 4.61e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987     4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGF 83
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKD-NLYLVLEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987    84 CEGGDLYHRLKQQKGelLPERQVVEWFVQiamalqylhekhilhrdlktqnifltktniikvgdlgIARVLENQNDMaST 163
Cdd:pfam00069  80 VEGGSLFDLLSEKGA--FSEREAKFIMKQ-------------------------------------ILEGLESGSSL-TT 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   164 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQM--PSKYDPQLGELIKRMLC 241
Cdd:pfam00069 120 FVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPelPSNLSEEAKDLLKKLLK 199
                         250
                  ....*....|....*...
gi 41055987   242 KKPEDRPDVKHILRQPYI 259
Cdd:pfam00069 200 KDPSKRLTATQALQHPWF 217
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
10-259 1.19e-49

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: 175.49  E-value: 1.19e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEV----NLvrhksDRKQYV-IKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFC 84
Cdd:cd06627   8 IGRGAFGSVykglNL-----NTGEFVaIKQISLEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKD-SLYIILEYV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  85 EGGDLYHRLKqqKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTL 164
Cdd:cd06627  82 ENGSLASIIK--KFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVATKLNEVEKDENSV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 165 IGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLvYRIVEGKLPQMPSKYDPQLGELIkrMLC-- 241
Cdd:cd06627 160 VGTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPyYDLQPMAAL-FRIVQDDHPPLPENISPELRDFL--LQCfq 236
                       250
                ....*....|....*...
gi 41055987 242 KKPEDRPDVKHILRQPYI 259
Cdd:cd06627 237 KDPTLRPSAKELLKHPWL 254
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
8-260 5.09e-49

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST3, MST4, STK25, Schizosaccharomyces pombe Nak1 and Sid1, Saccharomyces cerevisiae sporulation-specific protein 1 (SPS1), and related proteins. Nak1 is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Sid1 is a component in the septation initiation network (SIN) signaling pathway, and plays a role in cytokinesis. SPS1 plays a role in regulating proteins required for spore wall formation. MST4 plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. STK25 may play a role in the regulation of cell migration and polarization. The MST3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 174.74  E-value: 5.09e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRrERRAAEQEAQLLSQLKHPNIVMYRESWEgEDCQLYIVMGFCEGG 87
Cdd:cd06609   7 ERIGKGSFGEVYKGIDKRTNQVVAIKVIDLEEAED-EIEDIQQEIQFLSQCDSPYITKYYGSFL-KGSKLWIIMEYCGGG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  88 DLYHRLKQQKgelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLIGT 167
Cdd:cd06609  85 SVLDLLKPGP---LDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSGQLTSTMSKRNTFVGT 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 168 PYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMP-SKYDPQLGELIKRMLCKKPED 246
Cdd:cd06609 162 PFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLSDLHPMRVLFLIPKNNPPSLEgNKFSKPFKDFVELCLNKDPKE 241
                       250
                ....*....|....
gi 41055987 247 RPDVKHILRQPYIK 260
Cdd:cd06609 242 RPSAKELLKHKFIK 255
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
6-256 6.50e-49

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: 173.84  E-value: 6.50e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987     6 FVRVVGKGSYGEV---NLVRHKSDRKQYV-IKKLNlRTSSRRERRAAEQEAQLLSQLKHPNIVMYreswEG---EDCQLY 78
Cdd:pfam07714   3 LGEKLGEGAFGEVykgTLKGEGENTKIKVaVKTLK-EGADEEEREDFLEEASIMKKLDHPNIVKL----LGvctQGEPLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987    79 IVMGFCEGGDLYHRLKQQKGELLPErQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQN 158
Cdd:pfam07714  78 IVTEYMPGGDLLDFLRKHKRKLTLK-DLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDIYDDD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   159 DMASTLIG-TPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATL-KHAFNAKDMNSLVYRIVEGKLPQMPSKYDPQLGEL 235
Cdd:pfam07714 157 YYRKRGGGkLPIkWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLgEQPYPGMSNEEVLEFLEDGYRLPQPENCPDELYDL 236
                         250       260
                  ....*....|....*....|.
gi 41055987   236 IKRMLCKKPEDRPDVKHILRQ 256
Cdd:pfam07714 237 MKQCWAYDPEDRPTFSELVED 257
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
10-253 8.97e-49

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek7 is required for mitotic spindle formation and cytokinesis. It is enriched in the centrosome and is critical for microtubule nucleation. Nek7 is activated by Nek9 during mitosis, and may regulate the p70 ribosomal S6 kinase. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 174.45  E-value: 8.97e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNL-RTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEgEDCQLYIVMGFCEGGD 88
Cdd:cd08229  32 IGRGQFSEVYRATCLLDGVPVALKKVQIfDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFI-EDNELNIVLELADAGD 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  89 LYHRLKQQKGE--LLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLIG 166
Cdd:cd08229 111 LSRMIKHFKKQkrLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSLVG 190
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 167 TPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMN--SLVYRIVEGKLPQMPS-KYDPQLGELIKRMLCKK 243
Cdd:cd08229 191 TPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNlySLCKKIEQCDYPPLPSdHYSEELRQLVNMCINPD 270
                       250
                ....*....|
gi 41055987 244 PEDRPDVKHI 253
Cdd:cd08229 271 PEKRPDITYV 280
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
4-260 1.22e-48

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: 172.78  E-value: 1.22e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRtssRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDCqLYIVMGF 83
Cdd:cd06614   2 YKNLEKIGEGASGEVYKATDRATGKEVAIKKMRLR---KQNKELIINEILIMKECKHPNIVDYYDSYLVGDE-LWVVMEY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGGDLYHRLKQQKGELlPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMAST 163
Cdd:cd06614  78 MDGGSLTDIITQNPVRM-NESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAAQLTKEKSKRNS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 164 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMA--TLKHaFNAKDMNSLvYRIVEGKLPQM--PSKYDPQLGELIKRM 239
Cdd:cd06614 157 VVGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAegEPPY-LEEPPLRAL-FLITTKGIPPLknPEKWSPEFKDFLNKC 234
                       250       260
                ....*....|....*....|.
gi 41055987 240 LCKKPEDRPDVKHILRQPYIK 260
Cdd:cd06614 235 LVKDPEKRPSAEELLQHPFLK 255
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
3-259 1.47e-48

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: 172.83  E-value: 1.47e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   3 GYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLN-LRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVM 81
Cdd:cd05578   1 HFQILRVIGKGSFGKVCIVQKKDTKKMFAMKYMNkQKCIEKDSVRNVLNELEILQELEHPFLVNLWYSFQDEE-DMYMVV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  82 GFCEGGDL-YHRLKQQKgelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENqNDM 160
Cdd:cd05578  80 DLLLGGDLrYHLQQKVK---FSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATKLTD-GTL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 161 ASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKD--MNSLVYRIVEGKLPQMPSKYDPQLGELIKR 238
Cdd:cd05578 156 ATSTSGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEIHSrtSIEEIRAKFETASVLYPAGWSEEAIDLINK 235
                       250       260
                ....*....|....*....|..
gi 41055987 239 MLCKKPEDR-PDVKHILRQPYI 259
Cdd:cd05578 236 LLERDPQKRlGDLSDLKNHPYF 257
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
6-256 3.62e-48

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: 171.58  E-value: 3.62e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987      6 FVRVVGKGSYGEVN---LVRHKSDRKQYV-IKKLNlRTSSRRERRAAEQEAQLLSQLKHPNIV-MYresweG---EDCQL 77
Cdd:smart00221   3 LGKKLGEGAFGEVYkgtLKGKGDGKEVEVaVKTLK-EDASEQQIEEFLREARIMRKLDHPNIVkLL-----GvctEEEPL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987     78 YIVMGFCEGGDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQ 157
Cdd:smart00221  77 MIVMEYMPGGDLLDYLRKNRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDD 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987    158 NDMASTLIGTPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATL-KHAFNAKDMNSLVYRIVEGKLPQMPsKYDPQlgEL 235
Cdd:smart00221 157 DYYKVKGGKLPIrWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLgEEPYPGMSNAEVLEYLKKGYRLPKP-PNCPP--EL 233
                          250       260
                   ....*....|....*....|....
gi 41055987    236 IKRML-C--KKPEDRPDVKHILRQ 256
Cdd:smart00221 234 YKLMLqCwaEDPEDRPTFSELVEI 257
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
3-259 1.01e-47

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: 170.44  E-value: 1.01e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   3 GYLFVRVVGKGSYGEVNLV--RHKSDRKQYVIKKLNLRTSSR--RER---RaaeqEAQLLSQLKHPNIVMYRESWEGEDc 75
Cdd:cd14080   1 GYRLGKTIGEGSYSKVKLAeyTKSGLKEKVACKIIDKKKAPKdfLEKflpR----ELEILRKLRHPNIIQVYSIFERGS- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  76 QLYIVMGFCEGGDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLE 155
Cdd:cd14080  76 KVFIFMEYAEHGDLLEYIQKRGA--LSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFARLCP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 156 NQN--DMASTLIGTPYYMSPELFSNKPYNYK-SDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKL--PQMPSKYDP 230
Cdd:cd14080 154 DDDgdVLSKTFCGSAAYAAPEILQGIPYDPKkYDIWSLGVILYIMLCGSMPFDDSNIKKMLKDQQNRKVrfPSSVKKLSP 233
                       250       260
                ....*....|....*....|....*....
gi 41055987 231 QLGELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd14080 234 ECKDLIDQLLEPDPTKRATIEEILNHPWL 262
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
8-255 1.20e-47

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: 170.41  E-value: 1.20e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNL--VRHKSDRKQYV-IKKLNLRTSSRrERRAAEQEAQLLSQLKHPNIV-MYRESWEGEdcQLYIVMGF 83
Cdd:cd00192   1 KKLGEGAFGEVYKgkLKGGDGKTVDVaVKTLKEDASES-ERKDFLKEARVMKKLGHPNVVrLLGVCTEEE--PLYLVMEY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGGDLYHRLKQQKGEL-------LPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLEN 156
Cdd:cd00192  78 MEGGDLLDFLRKSRPVFpspepstLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSRDIYD 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 157 -QNDMASTLIGTP-YYMSPELFSNKPYNYKSDVWALGCCVYEMATL-KHAFNAKDMNSLVYRIVEGKLPQMPSKYDPQLG 233
Cdd:cd00192 158 dDYYRKKTGGKLPiRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTLgATPYPGLSNEEVLEYLRKGYRLPKPENCPDELY 237
                       250       260
                ....*....|....*....|....*
gi 41055987 234 ELIKRMLCKKPEDRP---DVKHILR 255
Cdd:cd00192 238 ELMLSCWQLDPEDRPtfsELVERLE 262
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
4-259 2.59e-47

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: 168.98  E-value: 2.59e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRrerrAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGF 83
Cdd:cd06612   5 FDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVEEDLQ----EIIKEISILKQCDSPYIVKYYGSYFKNT-DLWIVMEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGG---DLYHRLKQQkgelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDM 160
Cdd:cd06612  80 CGAGsvsDIMKITNKT----LTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLTDTMAK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 161 ASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLK------HAFNAKDMnslvyriVEGKLPQM---PSKYDPQ 231
Cdd:cd06612 156 RNTVIGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKppysdiHPMRAIFM-------IPNKPPPTlsdPEKWSPE 228
                       250       260
                ....*....|....*....|....*...
gi 41055987 232 LGELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd06612 229 FNDFVKKCLVKDPEERPSAIQLLQHPFI 256
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
4-259 2.75e-47

Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BRSK1, also called SAD-B or SAD1 (Synapses of Amphids Defective homolog 1), and BRSK2, also called SAD-A, are highly expressed in mammalian forebrain. They play important roles in establishing neuronal polarity. BRSK1/2 double knock-out mice die soon after birth, showing thin cerebral cortices due to disordered subplate layers and neurons that lack distinct axons and dendrites. BRSK1 regulates presynaptic neurotransmitter release. Its activity fluctuates during cell cysle progression and it acts as a regulator of centrosome duplication. BRSK2 is also abundant in pancreatic islets, where it is involved in the regulation of glucose-stimulated insulin secretion. The BRSK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270983 [Multi-domain]  Cd Length: 255  Bit Score: 168.97  E-value: 2.75e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRE-RRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMG 82
Cdd:cd14081   3 YRLGKTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKESvLMKVEREIAIMKLIEHPNVLKLYDVYENKK-YLYLVLE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FCEGGDLYHRLkQQKGELlPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARvLENQNDMAS 162
Cdd:cd14081  82 YVSGGELFDYL-VKKGRL-TEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMAS-LQPEGSLLE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 163 TLIGTPYYMSPELFSNKPYN-YKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKlPQMPSKYDPQLGELIKRMLC 241
Cdd:cd14081 159 TSCGSPHYACPEVIKGEKYDgRKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGV-FHIPHFISPDAQDLLRRMLE 237
                       250
                ....*....|....*...
gi 41055987 242 KKPEDRPDVKHILRQPYI 259
Cdd:cd14081 238 VNPEKRITIEEIKKHPWF 255
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
6-256 5.33e-47

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 168.09  E-value: 5.33e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987      6 FVRVVGKGSYGEVNL--VRHKSDRKQY--VIKKLNlRTSSRRERRAAEQEAQLLSQLKHPNIV-MYresweG---EDCQL 77
Cdd:smart00219   3 LGKKLGEGAFGEVYKgkLKGKGGKKKVevAVKTLK-EDASEQQIEEFLREARIMRKLDHPNVVkLL-----GvctEEEPL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987     78 YIVMGFCEGGDLYHRLKQQKGELlPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQ 157
Cdd:smart00219  77 YIVMEYMEGGDLLSYLRKNRPKL-SLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDD 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987    158 NDMASTLIGTPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATL-KHAFNAKDMNSLVYRIVEGKLPQMPSKYDPQLGEL 235
Cdd:smart00219 156 DYYRKRGGKLPIrWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLgEQPYPGMSNEEVLEYLKNGYRLPQPPNCPPELYDL 235
                          250       260
                   ....*....|....*....|.
gi 41055987    236 IKRMLCKKPEDRPDVKHILRQ 256
Cdd:smart00219 236 MLQCWAEDPEDRPTFSELVEI 256
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
2-259 1.20e-46

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: 167.95  E-value: 1.20e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAA------EQEAQLLSQLKHPNIVMYRESWEGEDc 75
Cdd:cd14084   6 KKYIMSRTLGSGACGEVKLAYDKSTCKKVAIKIINKRKFTIGSRREInkprniETEIEILKKLSHPCIIKIEDFFDAED- 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  76 QLYIVMGFCEGGDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTN---IIKVGDLGIAR 152
Cdd:cd14084  85 DYYIVLELMEGGELFDRVVSNKR--LKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEeecLIKITDFGLSK 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 153 VLENQNDMaSTLIGTPYYMSPELFSN---KPYNYKSDVWALGCCVYEMATLKHAFNA--KDMnSLVYRIVEGKL---PQM 224
Cdd:cd14084 163 ILGETSLM-KTLCGTPTYLAPEVLRSfgtEGYTRAVDCWSLGVILFICLSGYPPFSEeyTQM-SLKEQILSGKYtfiPKA 240
                       250       260       270
                ....*....|....*....|....*....|....*
gi 41055987 225 PSKYDPQLGELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd14084 241 WKNVSEEAKDLVKKMLVVDPSRRPSIEEALEHPWL 275
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
8-259 1.57e-46

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: 167.09  E-value: 1.57e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMY------REswegedcQLYIVM 81
Cdd:cd06626   6 NKIGEGTFGKVYTAVNLDTGELMAMKEIRFQDNDPKTIKEIADEMKVLEGLDHPNLVRYygvevhRE-------EVYIFM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  82 GFCEGGDLYHRLKQqkGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMA 161
Cdd:cd06626  79 EYCQEGTLEELLRH--GRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAVKLKNNTTTM 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 162 S-----TLIGTPYYMSPELF-SNKPYNYK--SDVWALGCCVYEMATLKHAFNAKDMN-SLVYRIVEGKLPQMP--SKYDP 230
Cdd:cd06626 157 ApgevnSLVGTPAYMAPEVItGNKGEGHGraADIWSLGCVVLEMATGKRPWSELDNEwAIMYHVGMGHKPPIPdsLQLSP 236
                       250       260
                ....*....|....*....|....*....
gi 41055987 231 QLGELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd06626 237 EGKDFLSRCLESDPKKRPTASELLDHPFI 265
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
4-247 3.29e-46

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: 166.99  E-value: 3.29e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSR-RERRAAEQEAQLLSQLKHPNIVMYRESWEgEDCQLYIVMG 82
Cdd:cd05580   3 FEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKIIKlKQVEHVLNEKRILSEVRHPFIVNLLGSFQ-DDRNLYMVME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FCEGGDLYHRLKqqKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLEnqnDMAS 162
Cdd:cd05580  82 YVPGGELFSLLR--RSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKRVK---DRTY 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 163 TLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLpQMPSKYDPQLGELIKRMLCK 242
Cdd:cd05580 157 TLCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGKI-RFPSFFDPDAKDLIKRLLVV 235

                ....*
gi 41055987 243 KPEDR 247
Cdd:cd05580 236 DLTKR 240
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
4-260 3.55e-46

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: 166.62  E-value: 3.55e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSR--------RERRAaeqeaqlLSQLKHPNIVMYRESWEGEDC 75
Cdd:cd05581   3 FKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLDKRHIIKekkvkyvtIEKEV-------LSRLAHPGIVKLYYTFQDESK 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  76 qLYIVMGFCEGGDLYHRLKQqKGELlpERQVVEWFV-QIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVL 154
Cdd:cd05581  76 -LYFVLEYAPNGDLLEYIRK-YGSL--DEKCTRFYTaEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGTAKVL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 155 -----------------ENQNDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIV 217
Cdd:cd05581 152 gpdsspestkgdadsqiAYNQARAASFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIV 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 41055987 218 EGKlPQMPSKYDPQLGELIKRMLCKKPEDRPDVKHILRQPYIK 260
Cdd:cd05581 232 KLE-YEFPENFPPDAKDLIQKLLVLDPSKRLGVNENGGYDELK 273
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
9-276 1.05e-45

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: 165.34  E-value: 1.05e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   9 VVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRrERRAAEQEAQLLSQLKH---PNIVMYRESWEgEDCQLYIVMGFCE 85
Cdd:cd06917   8 LVGRGSYGAVYRGYHVKTGRVVALKVLNLDTDDD-DVSDIQKEVALLSQLKLgqpKNIIKYYGSYL-KGPSLWIIMDYCE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  86 GGDLYHRLKQQKgelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLI 165
Cdd:cd06917  86 GGSIRTLMRAGP---IAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQNSSKRSTFV 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 166 GTPYYMSPELFSN-KPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPSK-YDPQLGELIKRMLCKK 243
Cdd:cd06917 163 GTPYWMAPEVITEgKYYDTKADIWSLGITTYEMATGNPPYSDVDALRAVMLIPKSKPPRLEGNgYSPLLKEFVAACLDEE 242
                       250       260       270
                ....*....|....*....|....*....|...
gi 41055987 244 PEDRPDVKHILRQPYIKHQISMFLEATKEKTAK 276
Cdd:cd06917 243 PKDRLSADELLKSKWIKQHSKTPTSVLKELISR 275
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
10-259 4.90e-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: 162.86  E-value: 4.90e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLrtSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEGG-- 87
Cdd:cd06613   8 IGSGTYGDVYKARNIATGELAAVKVIKL--EPGDDFEIIQQEISMLKECRHPNIVAYFGSYLRRD-KLWIVMEYCGGGsl 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  88 -DLYHRLKQqkgelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLIG 166
Cdd:cd06613  85 qDIYQVTGP-----LSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQLTATIAKRKSFIG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 167 TPYYMSPELFSNK---PYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLvYRIveGKLPQMP------SKYDPQLGELI 236
Cdd:cd06613 160 TPYWMAPEVAAVErkgGYDGKCDIWALGITAIELAELQPPmFDLHPMRAL-FLI--PKSNFDPpklkdkEKWSPDFHDFI 236
                       250       260
                ....*....|....*....|...
gi 41055987 237 KRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd06613 237 KKCLTKNPKKRPTATKLLQHPFV 259
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
6-257 5.86e-45

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


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 162.17  E-value: 5.86e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   6 FVRVVGKGSYGEVNLVRHKSDRKQYVIKKL--NLRTSSRRERRAAEQEAQ-LLSQlkHPNIVMYRESWEgEDCQLYIVMG 82
Cdd:cd13997   4 ELEQIGSGSFSEVFKVRSKVDGCLYAVKKSkkPFRGPKERARALREVEAHaALGQ--HPNIVRYYSSWE-EGGHLYIQME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FCEGGDLYHRLKQQKGE-LLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMA 161
Cdd:cd13997  81 LCENGSLQDALEELSPIsKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATRLETSGDVE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 162 StliGTPYYMSPELFSNKP-YNYKSDVWALGCCVYEMATlkhAFNAKDMNSLVYRIVEGKLPQMP-SKYDPQLGELIKRM 239
Cdd:cd13997 161 E---GDSRYLAPELLNENYtHLPKADIFSLGVTVYEAAT---GEPLPRNGQQWQQLRQGKLPLPPgLVLSQELTRLLKVM 234
                       250
                ....*....|....*...
gi 41055987 240 LCKKPEDRPDVKHILRQP 257
Cdd:cd13997 235 LDPDPTRRPTADQLLAHD 252
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
4-309 4.80e-44

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 166.35  E-value: 4.80e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987    4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLnLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGF 83
Cdd:PTZ00267  69 YVLTTLVGRNPTTAAFVATRGSDPKEKVVAKF-VMLNDERQAAYARSELHCLAACDHFGIVKHFDDFKSDD-KLLLIMEY 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   84 CEGGDLYHRLKQQKGELLP--ERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQN--D 159
Cdd:PTZ00267 147 GSGGDLNKQIKQRLKEHLPfqEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQYSDSVslD 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  160 MASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPSKYDPQLGELIKRM 239
Cdd:PTZ00267 227 VASSFCGTPYYLAPELWERKRYSKKADMWSLGVILYELLTLHRPFKGPSQREIMQQVLYGKYDPFPCPVSSGMKALLDPL 306
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  240 LCKKPEDRPDVKHILRQPYIKHQISMFLEATKEKTAKSRKNAANGKLNSAGSDASTKPNQVVQPQCLNSE 309
Cdd:PTZ00267 307 LSKNPALRPTTQQLLHTEFLKYVANLFQDIVRHSETISPHDREEILRQLQESGERAPPPSSIRYGVVTSD 376
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
2-260 5.33e-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: 160.20  E-value: 5.33e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLFVRVVGKGSYGEVNLVRHKSDrKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEdCQLYIVM 81
Cdd:cd06605   1 DDLEYLGELGEGNGGVVSKVRHRPS-GQIMAVKVIRLEIDEALQKQILRELDVLHKCNSPYIVGFYGAFYSE-GDISICM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  82 GFCEGGDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKH-ILHRDLKTQNIFLTKTNIIKVGDLGIARVLenQNDM 160
Cdd:cd06605  79 EYMDGGSLDKILKEVGR--IPERILGKIAVAVVKGLIYLHEKHkIIHRDVKPSNILVNSRGQVKLCDFGVSGQL--VDSL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 161 ASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAF---NAKDMNS---LVYRIVEGKLPQMPS-KYDPQLG 233
Cdd:cd06605 155 AKTFVGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPYpppNAKPSMMifeLLSYIVDEPPPLLPSgKFSPDFQ 234
                       250       260
                ....*....|....*....|....*..
gi 41055987 234 ELIKRMLCKKPEDRPDVKHILRQPYIK 260
Cdd:cd06605 235 DFVSQCLQKDPTERPSYKELMEHPFIK 261
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
10-255 6.31e-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: 159.96  E-value: 6.31e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSrrerraAEQEAQLLSQLKHPNIVMYRESWEGED--------------- 74
Cdd:cd14047  14 IGSGGFGQVFKAKHRIDGKTYAIKRVKLNNEK------AEREVKALAKLDHPNIVRYNGCWDGFDydpetsssnssrskt 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  75 -CqLYIVMGFCEGGDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARV 153
Cdd:cd14047  88 kC-LFIQMEFCEKGTLESWIEKRNGEKLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGKVKIGDFGLVTS 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 154 LENQNDMASTLiGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKdmNSLVYRIVEGKLPQMPSKYDPQLG 233
Cdd:cd14047 167 LKNDGKRTKSK-GTLSYMSPEQISSQDYGKEVDIYALGLILFELLHVCDSAFEK--SKFWTDLRNGILPDIFDKRYKIEK 243
                       250       260
                ....*....|....*....|..
gi 41055987 234 ELIKRMLCKKPEDRPDVKHILR 255
Cdd:cd14047 244 TIIKKMLSKKPEDRPNASEILR 265
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
10-247 6.54e-44

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


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 159.70  E-value: 6.54e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLR-TSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEGGD 88
Cdd:cd05572   1 LGVGGFGRVELVQLKSKGRTFALKCVKKRhIVQTRQQEHIFSEKEILEECNSPFIVKLYRTFKDKK-YLYMLMEYCLGGE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  89 LYHRLkQQKGeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDmASTLIGTP 168
Cdd:cd05572  80 LWTIL-RDRG-LFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKKLGSGRK-TWTFCGTP 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 169 YYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSL-VYR-IVEGKLP-QMPSKYDPQLGELIKRMLCKKPE 245
Cdd:cd05572 157 EYVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFGGDDEDPMkIYNiILKGIDKiEFPKYIDKNAKNLIKQLLRRNPE 236

                ..
gi 41055987 246 DR 247
Cdd:cd05572 237 ER 238
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
10-258 2.58e-43

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: 158.23  E-value: 2.58e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNlrtSSRRERRAaeQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEGGDL 89
Cdd:cd14010   8 IGRGKHSVVYKGRRKGTIEFVAIKCVD---KSKRPEVL--NEVRLTHELKHPNVLKFYEWYETSN-HLWLVVEYCTGGDL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  90 YHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVL--------------- 154
Cdd:cd14010  82 ETLLRQDGN--LPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLARREgeilkelfgqfsdeg 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 155 -ENQNDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPSKYD---- 229
Cdd:cd14010 160 nVNKVSKKQAKRGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFVAESFTELVEKILNEDPPPPPPKVSskps 239
                       250       260
                ....*....|....*....|....*....
gi 41055987 230 PQLGELIKRMLCKKPEDRPDVKHILRQPY 258
Cdd:cd14010 240 PDFKSLLKGLLEKDPAKRLSWDELVKHPF 268
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
12-260 4.32e-43

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: 157.76  E-value: 4.32e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  12 KGSYGEVNLVRHKSDRKQY---VIKKLNLRTSSRRERRAAEQEAqlLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEGGD 88
Cdd:cd05579   3 RGAYGRVYLAKKKSTGDLYaikVIKKRDMIRKNQVDSVLAERNI--LSQAQNPFVVKLYYSFQGKK-NLYLVMEYLPGGD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  89 LYHRLKQQkgELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARV-LENQNDMAS----- 162
Cdd:cd05579  80 LYSLLENV--GALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKVgLVRRQIKLSiqkks 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 163 ---------TLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKL--PQMPSKYDpQ 231
Cdd:cd05579 158 ngapekedrRIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNILNGKIewPEDPEVSD-E 236
                       250       260       270
                ....*....|....*....|....*....|..
gi 41055987 232 LGELIKRMLCKKPEDRPD---VKHILRQPYIK 260
Cdd:cd05579 237 AKDLISKLLTPDPEKRLGakgIEEIKNHPFFK 268
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
4-259 7.04e-43

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: 157.26  E-value: 7.04e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNL--------RTSSRrerraaeqEAQLLSQLKHPNIVMYRESWEGEDc 75
Cdd:cd07829   1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIRLdneeegipSTALR--------EISLLKELKHPNIVKLLDVIHTEN- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  76 QLYIVMGFCEGgDLYHRLKQQKGELlPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLE 155
Cdd:cd07829  72 KLYLVFEYCDQ-DLKKYLDKRPGPL-PPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLARAFG 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 156 NQNDMASTLIGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVE---------------- 218
Cdd:cd07829 150 IPLRTYTHEVVTLWYRAPEiLLGSKHYSTAVDIWSVGCIFAELITGKPLFPGDSEIDQLFKIFQilgtpteeswpgvtkl 229
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 41055987 219 ----GKLPQMPSK--------YDPQLGELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd07829 230 pdykPTFPKWPKNdlekvlprLDPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
2-240 1.07e-42

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: 157.18  E-value: 1.07e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSR-RERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIV 80
Cdd:cd14209   1 DDFDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVVKlKQVEHTLNEKRILQAINFPFLVKLEYSFKDNS-NLYMV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MGFCEGGDLYHRLkqQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLEnqnDM 160
Cdd:cd14209  80 MEYVPGGEMFSHL--RRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRVK---GR 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 161 ASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLpQMPSKYDPQLGELIKRML 240
Cdd:cd14209 155 TWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKV-RFPSHFSSDLKDLLRNLL 233
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
4-258 6.49e-42

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: 154.17  E-value: 6.49e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLR--TSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDCqLYIVM 81
Cdd:cd14098   2 YQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRkvAGNDKNLQLFQREINILKSLEHPGIVRLIDWYEDDQH-IYLVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  82 GFCEGGDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTN--IIKVGDLGIARVLENqND 159
Cdd:cd14098  81 EYVEGGDLMDFIMAWGA--IPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDpvIVKISDFGLAKVIHT-GT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 160 MASTLIGTPYYMSPELFSNKP------YNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPSK---YDP 230
Cdd:cd14098 158 FLVTFCGTMAYLAPEILMSKEqnlqggYSNLVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIRKGRYTQPPLVdfnISE 237
                       250       260
                ....*....|....*....|....*...
gi 41055987 231 QLGELIKRMLCKKPEDRPDVKHILRQPY 258
Cdd:cd14098 238 EAIDFILRLLDVDPEKRMTAAQALDHPW 265
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
7-254 7.48e-42

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


Pssm-ID: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 154.45  E-value: 7.48e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   7 VRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAeQEAQLLSQLKHPNIVMYRESWEgEDCQLYIVMGFCEG 86
Cdd:cd14046  11 LQVLGKGAFGQVVKVRNKLDGRYYAIKKIKLRSESKNNSRIL-REVMLLSRLNHQHVVRYYQAWI-ERANLYIQMEYCEK 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  87 GDLYHRLKQqkGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLI- 165
Cdd:cd14046  89 STLRDLIDS--GLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLATSNKLNVELATQDIn 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 166 -----------------GTPYYMSPELFSNKP--YNYKSDVWALGCCVYEMAtlkHAFNAKDMNSLVYRIVEGKLPQMPS 226
Cdd:cd14046 167 kstsaalgssgdltgnvGTALYVAPEVQSGTKstYNEKVDMYSLGIIFFEMC---YPFSTGMERVQILTALRSVSIEFPP 243
                       250       260       270
                ....*....|....*....|....*....|..
gi 41055987 227 KYD----PQLGELIKRMLCKKPEDRPDVKHIL 254
Cdd:cd14046 244 DFDdnkhSKQAKLIRWLLNHDPAKRPSAQELL 275
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
7-259 1.05e-41

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: 154.00  E-value: 1.05e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   7 VRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLrTSSRRERraAEQEAQLLSQL-KHPNIVMY-----RESWEGEDCQLYIV 80
Cdd:cd06608  11 VEVIGEGTYGKVYKARHKKTGQLAAIKIMDI-IEDEEEE--IKLEINILRKFsNHPNIATFygafiKKDPPGGDDQLWLV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MGFCEGG---DLYHRLKQqKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQ 157
Cdd:cd06608  88 MEYCGGGsvtDLVKGLRK-KGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGVSAQLDST 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 158 NDMASTLIGTPYYMSPELFS-----NKPYNYKSDVWALGCCVYEMATLKHAFNakDMNSL--VYRIVEGKLPQM--PSKY 228
Cdd:cd06608 167 LGRRNTFIGTPYWMAPEVIAcdqqpDASYDARCDVWSLGITAIELADGKPPLC--DMHPMraLFKIPRNPPPTLksPEKW 244
                       250       260       270
                ....*....|....*....|....*....|.
gi 41055987 229 DPQLGELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd06608 245 SKEFNDFISECLIKNYEQRPFTEELLEHPFI 275
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
10-258 2.30e-41

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: 152.14  E-value: 2.30e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYV----IKKLNLRTSsrreRRAAEQEAQLLSQLKHPNIVMYRESWEGEDCqLYIVMGFCE 85
Cdd:cd14120   1 IGHGAFAVVFKGRHRKKPDLPVaikcITKKNLSKS----QNLLGKEIKILKELSHENVVALLDCQETSSS-VYLVMEYCN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  86 GGDLYHRLkQQKGELlPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTK--------TNI-IKVGDLGIARVLEN 156
Cdd:cd14120  76 GGDLADYL-QAKGTL-SEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHnsgrkpspNDIrLKIADFGFARFLQD 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 157 qNDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSL--VYRIVEGKLPQMPSKYDPQLGE 234
Cdd:cd14120 154 -GMMAATLCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQAQTPQELkaFYEKNANLRPNIPSGTSPALKD 232
                       250       260
                ....*....|....*....|....
gi 41055987 235 LIKRMLCKKPEDRPDVKHILRQPY 258
Cdd:cd14120 233 LLLGLLKRNPKDRIDFEDFFSHPF 256
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
4-259 3.59e-41

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK1, also called ARK5 (AMPK-related protein kinase 5), regulates cell proliferation and displays tumor suppression through direct interaction and phosphorylation of p53. It is also involved in cell senescence and motility. High NUAK1 expression is associated with invasiveness of nonsmall cell lung cancer (NSCLC) and breast cancer cells. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. The NUAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270975 [Multi-domain]  Cd Length: 254  Bit Score: 151.77  E-value: 3.59e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKL-NLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMG 82
Cdd:cd14073   3 YELLETLGKGTYGKVKLAIERATGREVAIKSIkKDKIEDEQDMVRIRREIEIMSSLNHPHIIRIYEVFENKD-KIVIVME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FCEGGDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLEnQNDMAS 162
Cdd:cd14073  82 YASGGELYDYISERRR--LPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSNLYS-KDKLLQ 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 163 TLIGTPYYMSPELFSNKPYN-YKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQmPSKYDPQLGeLIKRMLC 241
Cdd:cd14073 159 TFCGSPLYASPEIVNGTPYQgPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISSGDYRE-PTQPSDASG-LIRWMLT 236
                       250
                ....*....|....*...
gi 41055987 242 KKPEDRPDVKHILRQPYI 259
Cdd:cd14073 237 VNPKRRATIEDIANHWWV 254
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
8-258 5.40e-41

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: 151.32  E-value: 5.40e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKQYVIKKL-NLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEG 86
Cdd:cd14188   7 KVLGKGGFAKCYEMTDLTTNKVYAAKIIpHSRVSKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKE-NIYILLEYCSR 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  87 GDLYHRLKQQKgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLIG 166
Cdd:cd14188  86 RSMAHILKARK--VLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLEPLEHRRRTICG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 167 TPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSlVYRIVEGKLPQMPSKYDPQLGELIKRMLCKKPED 246
Cdd:cd14188 164 TPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKE-TYRCIREARYSLPSSLLAPAKHLIASMLSKNPED 242
                       250
                ....*....|..
gi 41055987 247 RPDVKHILRQPY 258
Cdd:cd14188 243 RPSLDEIIRHDF 254
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
4-268 5.75e-41

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 157.72  E-value: 5.75e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987    4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDCQ------- 76
Cdd:PTZ00283  34 YWISRVLGSGATGTVLCAKRVSDGEPFAVKVVDMEGMSEADKNRAQAEVCCLLNCDFFSIVKCHEDFAKKDPRnpenvlm 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   77 LYIVMGFCEGGDLYHRLKQ--QKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVL 154
Cdd:PTZ00283 114 IALVLDYANAGDLRQEIKSraKTNRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDFGFSKMY 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  155 EN--QNDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPSKYDPQL 232
Cdd:PTZ00283 194 AAtvSDDVGRTFCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGENMEEVMHKTLAGRYDPLPPSISPEM 273
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 41055987  233 GELIKRMLCKKPEDRPDVKHILRQPYIKHQISMFLE 268
Cdd:PTZ00283 274 QEIVTALLSSDPKRRPSSSKLLNMPICKLFISGLLE 309
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
10-259 1.12e-40

Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of HAL4, Saccharomyces cerevisiae Ptk2/Stk2, and similar fungal proteins. Proteins in this subfamily are involved in regulating ion transporters. In budding and fission yeast, HAL4 promotes potassium ion uptake, which increases cellular resistance to other cations such as sodium, lithium, and calcium ions. HAL4 stabilizes the major high-affinity K+ transporter Trk1 at the plasma membrane under low K+ conditions, which prevents endocytosis and vacuolar degradation. Budding yeast Ptk2 phosphorylates and regulates the plasma membrane H+ ATPase, Pma1. The HAL4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 150.54  E-value: 1.12e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKS--DRKQYVIKKLNLRTSSR-----RERRAAEQEaqLLSQLKHPNIVM---YRESWEGEDCqlyI 79
Cdd:cd13994   1 IGKGATSVVRIVTKKNprSGVLYAVKEYRRRDDESkrkdyVKRLTSEYI--ISSKLHHPNIVKvldLCQDLHGKWC---L 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  80 VMGFCEGGDLYHRLKqqKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQND 159
Cdd:cd13994  76 VMEYCPGGDLFTLIE--KADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAEVFGMPAE 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 160 ----MASTLIGTPYYMSPELFSNKPYN-YKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPSKYDP---- 230
Cdd:cd13994 154 kespMSAGLCGSEPYMAPEVFTSGSYDgRAVDVWSCGIVLFALFTGRFPWRSAKKSDSAYKAYEKSGDFTNGPYEPienl 233
                       250       260       270
                ....*....|....*....|....*....|..
gi 41055987 231 ---QLGELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd13994 234 lpsECRRLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
11-247 1.37e-40

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: 149.75  E-value: 1.37e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  11 GKGSYGEVNLVRHKSDRKQYV----IKKLNLRTSSrrerraAE---QEAQLLSQLKHPNIVMYRE-SWEGEdcQLYIVMG 82
Cdd:cd14121   4 GSGTYATVYKAYRKSGAREVVavkcVSKSSLNKAS------TEnllTEIELLKKLKHPHIVELKDfQWDEE--HIYLIME 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FCEGGDLYHRLKQQKgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTK--TNIIKVGDLGIARVLENqNDM 160
Cdd:cd14121  76 YCSGGDLSRFIRSRR--TLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSryNPVLKLADFGFAQHLKP-NDE 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 161 ASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPSKydPQLG----ELI 236
Cdd:cd14121 153 AHSLRGSPLYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFASRSFEELEEKIRSSKPIEIPTR--PELSadcrDLL 230
                       250
                ....*....|.
gi 41055987 237 KRMLCKKPEDR 247
Cdd:cd14121 231 LRLLQRDPDRR 241
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
11-262 9.32e-40

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: 148.35  E-value: 9.32e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  11 GKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEaqLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEGGDLY 90
Cdd:cd06611  14 GDGAFGKVYKAQHKETGLFAAAKIIQIESEEELEDFMVEID--ILSECKHPNIVGLYEAYFYEN-KLWILIEFCDGGALD 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  91 H-RLKQQKGELLPERQVVEWfvQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLIGTPY 169
Cdd:cd06611  91 SiMLELERGLTEPQIRYVCR--QMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAKNKSTLQKRDTFIGTPY 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 170 YMSPEL-----FSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQM--PSKYDPQLGELIKRMLCK 242
Cdd:cd06611 169 WMAPEVvacetFKDNPYDYKADIWSLGITLIELAQMEPPHHELNPMRVLLKILKSEPPTLdqPSKWSSSFNDFLKSCLVK 248
                       250       260
                ....*....|....*....|
gi 41055987 243 KPEDRPDVKHILRQPYIKHQ 262
Cdd:cd06611 249 DPDDRPTAAELLKHPFVSDQ 268
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
11-258 9.97e-40

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: 147.40  E-value: 9.97e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  11 GKGSYGEVNLVRHKSDRKQYVIKKLnlrtSSRRERRAA------EQEAQLLSQLKHPNIVMYRESWEGEDCQ-LYIVMGF 83
Cdd:cd14119   2 GEGSYGKVKEVLDTETLCRRAVKIL----KKRKLRRIPngeanvKREIQILRRLNHRNVIKLVDVLYNEEKQkLYMVMEY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGGdLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLE--NQNDMA 161
Cdd:cd14119  78 CVGG-LQEMLDSAPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAEALDlfAEDDTC 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 162 STLIGTPYYMSPELFSNKPY--NYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLpQMPSKYDPQLGELIKRM 239
Cdd:cd14119 157 TTSQGSPAFQPPEIANGQDSfsGFKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKGEY-TIPDDVDPDLQDLLRGM 235
                       250
                ....*....|....*....
gi 41055987 240 LCKKPEDRPDVKHILRQPY 258
Cdd:cd14119 236 LEKDPEKRFTIEQIRQHPW 254
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
4-258 1.01e-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: 148.45  E-value: 1.01e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRE----RraaeqEAQLLSQLK-HPNIV----MYRESWEged 74
Cdd:cd07830   1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKMKKKFYSWEEcmnlR-----EVKSLRKLNeHPNIVklkeVFRENDE--- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  75 cqLYIVMGFCEGgDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVL 154
Cdd:cd07830  73 --LYFVFEYMEG-NLYQLMKDRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLAREI 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 155 ENQNDMaSTLIGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAF---NAKDMnslVYRIV------------E 218
Cdd:cd07830 150 RSRPPY-TDYVSTRWYRAPEiLLRSTSYSSPVDIWALGCIMAELYTLRPLFpgsSEIDQ---LYKICsvlgtptkqdwpE 225
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 41055987 219 G---------KLPQ---------MPSKYdPQLGELIKRMLCKKPEDRPDVKHILRQPY 258
Cdd:cd07830 226 GyklasklgfRFPQfaptslhqlIPNAS-PEAIDLIKDMLRWDPKKRPTASQALQHPY 282
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
9-259 1.79e-39

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: 147.20  E-value: 1.79e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   9 VVGKGSYGEV--NLVrhkSDRKQYVIKKLNLRTS----SRRERRAAEQEAQLLSQLKHPNIVMYRESWEgEDCQLYIVMG 82
Cdd:cd06631   8 VLGKGAYGTVycGLT---STGQLIAVKQVELDTSdkekAEKEYEKLQEEVDLLKTLKHVNIVGYLGTCL-EDNVVSIFME 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FCEGGDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVL------EN 156
Cdd:cd06631  84 FVPGGSIASILARFGA--LEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGCAKRLcinlssGS 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 157 QNDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFnaKDMNSL--VYRIVEGK--LPQMPSKYDPQL 232
Cdd:cd06631 162 QSQLLKSMRGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPW--ADMNPMaaIFAIGSGRkpVPRLPDKFSPEA 239
                       250       260
                ....*....|....*....|....*..
gi 41055987 233 GELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd06631 240 RDFVHACLTRDQDERPSAEQLLKHPFI 266
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
4-259 2.77e-39

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: 146.23  E-value: 2.77e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRtssRRERRAAEQEAQLLSQLK----HPNIVMYRESWEGEDCQ-LY 78
Cdd:cd05118   1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKND---FRHPKAALREIKLLKHLNdvegHPNIVKLLDVFEHRGGNhLC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  79 IVMGFCeGGDLYHRLKQQkGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTN-IIKVGDLGIARVLEnq 157
Cdd:cd05118  78 LVFELM-GMNLYELIKDY-PRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELgQLKLADFGLARSFT-- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 158 NDMASTLIGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVE--GKlpqmpskydPQLGE 234
Cdd:cd05118 154 SPPYTPYVATRWYRAPEvLLGAKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIVRllGT---------PEALD 224
                       250       260
                ....*....|....*....|....*
gi 41055987 235 LIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd05118 225 LLSKMLKYDPAKRITASQALAHPYF 249
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
4-256 3.20e-39

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: 146.71  E-value: 3.20e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLrtSSRRERRAAEQEAQLLSQL-KHPNIVMYRES--------WEGed 74
Cdd:cd13985   2 YQVTKQLGEGGFSYVYLAHDVNTGRRYALKRMYF--NDEEQLRVAIKEIEIMKRLcGHPNIVQYYDSailssegrKEV-- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  75 cqlYIVMGFCeGGDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKH--ILHRDLKTQNIFLTKTNIIKVGDLG--- 149
Cdd:cd13985  78 ---LLLMEYC-PGSLVDILEKSPPSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFGsat 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 150 -IARVLENQND--MASTLIG---TPYYMSPE---LFSNKPYNYKSDVWALGCCVYEMATLKHAFNAkdmnSLVYRIVEGK 220
Cdd:cd13985 154 tEHYPLERAEEvnIIEEEIQkntTPMYRAPEmidLYSKKPIGEKADIWALGCLLYKLCFFKLPFDE----SSKLAIVAGK 229
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 41055987 221 --LPQMPsKYDPQLGELIKRMLCKKPEDRPDVKHILRQ 256
Cdd:cd13985 230 ysIPEQP-RYSPELHDLIRHMLTPDPAERPDIFQVINI 266
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
8-247 3.29e-39

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, classical PKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. Novel PKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. Also included in this subfamily are the PKC-like proteins, called PKNs. The PKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 148.13  E-value: 3.29e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRT--------SSRRERRAaeqeaqLLSQLKHPNIVMYRESWEGEDcQLYI 79
Cdd:cd05570   1 KVLGKGSFGKVMLAERKKTDELYAIKVLKKEViiedddveCTMTEKRV------LALANRHPFLTGLHACFQTED-RLYF 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  80 VMGFCEGGDL-YHRLKQQKgelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARvlEN-- 156
Cdd:cd05570  74 VMEYVNGGDLmFHIQRARR---FTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCK--EGiw 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 157 QNDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEgKLPQMPSKYDPQLGELI 236
Cdd:cd05570 149 GGNTTSTFCGTPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILN-DEVLYPRWLSREAVSIL 227
                       250
                ....*....|.
gi 41055987 237 KRMLCKKPEDR 247
Cdd:cd05570 228 KGLLTKDPARR 238
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
10-255 4.98e-39

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: 145.56  E-value: 4.98e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEGGDL 89
Cdd:cd14075  10 LGSGNFSQVKLGIHQLTKEKVAIKILDKTKLDQKTQRLLSREISSMEKLHHPNIIRLYEVVETLS-KLHLVMEYASGGEL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  90 YHRLKQQkGELlPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENqNDMASTLIGTPY 169
Cdd:cd14075  89 YTKISTE-GKL-SESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFSTHAKR-GETLNTFCGSPP 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 170 YMSPELFSNKPY-NYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLpQMPSKYDPQLGELIKRMLCKKPEDRP 248
Cdd:cd14075 166 YAAPELFKDEHYiGIYVDIWALGVLLYFMVTGVMPFRAETVAKLKKCILEGTY-TIPSYVSEPCQELIRGILQPVPSDRY 244

                ....*..
gi 41055987 249 DVKHILR 255
Cdd:cd14075 245 SIDEIKN 251
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
35-259 5.67e-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: 145.45  E-value: 5.67e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  35 LNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDCQLYI-VMGFCEGGDLYHRLKQQKgeLLPERQVVEWFVQI 113
Cdd:cd13983  34 IKLRKLPKAERQRFKQEIEILKSLKHPNIIKFYDSWESKSKKEVIfITELMTSGTLKQYLKRFK--RLKLKVIKSWCRQI 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 114 AMALQYLH--EKHILHRDLKTQNIFLT-KTNIIKVGDLGIARVLenQNDMASTLIGTPYYMSPELFSNKpYNYKSDVWAL 190
Cdd:cd13983 112 LEGLNYLHtrDPPIIHRDLKCDNIFINgNTGEVKIGDLGLATLL--RQSFAKSVIGTPEFMAPEMYEEH-YDEKVDIYAF 188
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41055987 191 GCCVYEMATLKHAFNAKDMNSLVYRIV-EGKLPQMPSKY-DPQLGELIkrMLC-KKPEDRPDVKHILRQPYI 259
Cdd:cd13983 189 GMCLLEMATGEYPYSECTNAAQIYKKVtSGIKPESLSKVkDPELKDFI--EKClKPPDERPSARELLEHPFF 258
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
10-260 1.17e-38

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: 144.51  E-value: 1.17e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRErrAAEQEAQLLSQLKHPNIV-MYRESWEGEdcQLYIVMGFCEGGD 88
Cdd:cd06648  15 IGEGSTGIVCIATDKSTGRQVAVKKMDLRKQQRRE--LLFNEVVIMRDYQHPNIVeMYSSYLVGD--ELWVVMEFLEGGA 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  89 LYHRLKQQKgelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLIGTP 168
Cdd:cd06648  91 LTDIVTHTR---MNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQVSKEVPRRKSLVGTP 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 169 YYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQM--PSKYDPQLGELIKRMLCKKPED 246
Cdd:cd06648 168 YWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIRDNEPPKLknLHKVSPRLRSFLDRMLVRDPAQ 247
                       250
                ....*....|....
gi 41055987 247 RPDVKHILRQPYIK 260
Cdd:cd06648 248 RATAAELLNHPFLA 261
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
3-258 1.31e-38

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: 144.40  E-value: 1.31e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   3 GYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIV-MYRESWEGEDCqlYIVM 81
Cdd:cd14069   2 DWDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPGDCPENIKKEVCIQKMLSHKNVVrFYGHRREGEFQ--YLFL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  82 GFCEGGDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQND-- 159
Cdd:cd14069  80 EYASGGELFDKIEPDVG--MPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLATVFRYKGKer 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 160 MASTLIGTPYYMSPELFSNKPYN-YKSDVWALGCCVYEMATLKHAFNAKDMNSLVYR--IVEGKLPQMP-SKYDPQLGEL 235
Cdd:cd14069 158 LLNKMCGTLPYVAPELLAKKKYRaEPVDVWSCGIVLFAMLAGELPWDQPSDSCQEYSdwKENKKTYLTPwKKIDTAALSL 237
                       250       260
                ....*....|....*....|...
gi 41055987 236 IKRMLCKKPEDRPDVKHILRQPY 258
Cdd:cd14069 238 LRKILTENPNKRITIEDIKKHPW 260
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
2-263 1.79e-38

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: 144.87  E-value: 1.79e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLFVRVVGKGSYGEVNLVRHKSDrKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGE-DCQLYIV 80
Cdd:cd06621   1 DKIVELSSLGEGAGGSVTKCRLRNT-KTIFALKTITTDPNPDVQKQILRELEINKSCASPYIVKYYGAFLDEqDSSIGIA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MGFCEGGDL---YHRLKQQKGELlPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARvlENQ 157
Cdd:cd06621  80 MEYCEGGSLdsiYKKVKKKGGRI-GEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVSG--ELV 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 158 NDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNS-----LVYRIVEGKLPQMPSkyDPQL 232
Cdd:cd06621 157 NSLAGTFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFPPEGEPPlgpieLLSYIVNMPNPELKD--EPEN 234
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 41055987 233 G--------ELIKRMLCKKPEDRPDVKHILRQPYIKHQI 263
Cdd:cd06621 235 GikwsesfkDFIEKCLEKDGTRRPGPWQMLAHPWIKAQE 273
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
8-259 2.66e-38

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: 143.65  E-value: 2.66e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKQYVIKKLNL---RTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEgEDCQLYIVMGFC 84
Cdd:cd06625   6 KLLGQGAFGQVYLCYDADTGRELAVKQVEIdpiNTEASKEVKALECEIQLLKNLQHERIVQYYGCLQ-DEKSLSIFMEYM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  85 EGGDLYHRLKQQkGELlPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLEN---QNDMa 161
Cdd:cd06625  85 PGGSVKDEIKAY-GAL-TENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASKRLQTicsSTGM- 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 162 STLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIV-EGKLPQMPSKYDPQLGELIKRML 240
Cdd:cd06625 162 KSVTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPWAEFEPMAAIFKIAtQPTNPQLPPHVSEDARDFLSLIF 241
                       250
                ....*....|....*....
gi 41055987 241 CKKPEDRPDVKHILRQPYI 259
Cdd:cd06625 242 VRNKKQRPSAEELLSHSFV 260
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
4-259 3.84e-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: 143.61  E-value: 3.84e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVR--VVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDCqLYIVM 81
Cdd:cd14202   2 FEFSRkdLIGHGAFAVVFKGRHKEKHDLEVAVKCINKKNLAKSQTLLGKEIKILKELKHENIVALYDFQEIANS-VYLVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  82 GFCEGGDLYHRLKQQKgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLT-----KTN----IIKVGDLGIAR 152
Cdd:cd14202  81 EYCNGGDLADYLHTMR--TLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSysggrKSNpnniRIKIADFGFAR 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 153 VLENqNDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSL--VYRIVEGKLPQMPSKYDP 230
Cdd:cd14202 159 YLQN-NMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQDLrlFYEKNKSLSPNIPRETSS 237
                       250       260
                ....*....|....*....|....*....
gi 41055987 231 QLGELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd14202 238 HLRQLLLGLLQRNQKDRMDFDEFFHHPFL 266
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
4-258 1.61e-37

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: 141.31  E-value: 1.61e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERrAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGF 83
Cdd:cd14095   2 YDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGKEH-MIENEVAILRRVKHPNIVQLIEEYDTDT-ELYLVMEL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGGDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTK----TNIIKVGDLGIARVLENQnd 159
Cdd:cd14095  80 VKGGDLFDAITSSTK--FTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEhedgSKSLKLADFGLATEVKEP-- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 160 mASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNS--LVYRIVEGKLpQMPSKY----DPQLG 233
Cdd:cd14095 156 -LFTVCGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRSPDRDQeeLFDLILAGEF-EFLSPYwdniSDSAK 233
                       250       260
                ....*....|....*....|....*
gi 41055987 234 ELIKRMLCKKPEDRPDVKHILRQPY 258
Cdd:cd14095 234 DLISRMLVVDPEKRYSAGQVLDHPW 258
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
2-259 4.74e-37

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: 140.19  E-value: 4.74e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSsRRERRAAEQEAQLLSQLKHPNIVMYRESWEgEDCQLYIVM 81
Cdd:cd06610   1 DDYELIEVIGSGATAVVYAAYCLPKKEKVAIKRIDLEKC-QTSMDELRKEIQAMSQCNHPNVVSYYTSFV-VGDELWLVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  82 GFCEGGDLYHRLKQQ-KGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDM 160
Cdd:cd06610  79 PLLSGGSLLDIMKSSyPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVSASLATGGDR 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 161 AS----TLIGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAF-NAKDMNSLVyRIVEGKLPQMPS-----KYD 229
Cdd:cd06610 159 TRkvrkTFVGTPCWMAPEvMEQVRGYDFKADIWSFGITAIELATGAAPYsKYPPMKVLM-LTLQNDPPSLETgadykKYS 237
                       250       260       270
                ....*....|....*....|....*....|
gi 41055987 230 PQLGELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd06610 238 KSFRKMISLCLQKDPSKRPTAEELLKHKFF 267
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
2-260 1.41e-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: 141.27  E-value: 1.41e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAA-EQEAQLLSQLKHPNIVMYRESWEGEDcQLYIV 80
Cdd:cd05573   1 DDFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRKSDMLKREQIAHvRAERDILADADSPWIVRLHYAFQDED-HLYLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MGFCEGGDLYHRLkqQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIA--------- 151
Cdd:cd05573  80 MEYMPGGDLMNLL--IKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCtkmnksgdr 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 152 --------------------RVLENQNDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNS 211
Cdd:cd05573 158 esylndsvntlfqdnvlarrRPHKQRRVRAYSAVGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPPFYSDSLVE 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 41055987 212 LVYRIVEGK----LPQMPsKYDPQLGELIKRMLCkKPEDR-PDVKHILRQPYIK 260
Cdd:cd05573 238 TYSKIMNWKeslvFPDDP-DVSPEAIDLIRRLLC-DPEDRlGSAEEIKAHPFFK 289
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
9-260 1.45e-36

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: 138.99  E-value: 1.45e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   9 VVGKGSYGEVNLVRHKSDRK-QYVIKKLNLRTSSRRERRAAeQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEGG 87
Cdd:cd14201  13 LVGHGAFAVVFKGRHRKKTDwEVAIKSINKKNLSKSQILLG-KEIKILKELQHENIVALYDVQEMPN-SVFLVMEYCNGG 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  88 DLYHRLkQQKGELlPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLT-----KTNI----IKVGDLGIARVLENqN 158
Cdd:cd14201  91 DLADYL-QAKGTL-SEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSyasrkKSSVsgirIKIADFGFARYLQS-N 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 159 DMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSL--VYRIVEGKLPQMPSKYDPQLGELI 236
Cdd:cd14201 168 MMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQDLrmFYEKNKNLQPSIPRETSPYLADLL 247
                       250       260
                ....*....|....*....|....
gi 41055987 237 KRMLCKKPEDRPDVKHILRQPYIK 260
Cdd:cd14201 248 LGLLQRNQKDRMDFEAFFSHPFLE 271
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
4-258 2.01e-36

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: 137.92  E-value: 2.01e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNlRTSSRRERrAAEQ---EAQLLSQLKHPNIVMYRESWeGEDCQLYIV 80
Cdd:cd14663   2 YELGRTLGEGTFAKVKFARNTKTGESVAIKIID-KEQVAREG-MVEQikrEIAIMKLLRHPNIVELHEVM-ATKTKIFFV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MGFCEGGDLYHRLKqqKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLE--NQN 158
Cdd:cd14663  79 MELVTGGELFSKIA--KNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSALSEqfRQD 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 159 DMASTLIGTPYYMSPELFSNKPYN-YKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPqMPSKYDPQLGELIK 237
Cdd:cd14663 157 GLLHTTCGTPNYVAPEVLARRGYDgAKADIWSCGVILFVLLAGYLPFDDENLMALYRKIMKGEFE-YPRWFSPGAKSLIK 235
                       250       260
                ....*....|....*....|.
gi 41055987 238 RMLCKKPEDRPDVKHILRQPY 258
Cdd:cd14663 236 RILDPNPSTRITVEQIMASPW 256
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
4-253 2.06e-36

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


Pssm-ID: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 138.16  E-value: 2.06e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRkQYVIKklnlrtSSRRERRAAEQ-------EAQLLSQLKHPNIVMYRESWEGEDcQ 76
Cdd:cd14161   5 YEFLETLGKGTYGRVKKARDSSGR-LVAIK------SIRKDRIKDEQdllhirrEIEIMSSLNHPHIISVYEVFENSS-K 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  77 LYIVMGFCEGGDLYHRLKQQkgELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLeN 156
Cdd:cd14161  77 IVIVMEYASRGDLYDYISER--QRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSNLY-N 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 157 QNDMASTLIGTPYYMSPELFSNKPY-NYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQmPSKYDPQLGeL 235
Cdd:cd14161 154 QDKFLQTYCGSPLYASPEIVNGRPYiGPEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISSGAYRE-PTKPSDACG-L 231
                       250
                ....*....|....*...
gi 41055987 236 IKRMLCKKPEDRPDVKHI 253
Cdd:cd14161 232 IRWLLMVNPERRATLEDV 249
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
10-278 2.73e-36

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: 139.01  E-value: 2.73e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNlrTSSRRERRAAEQEAQLLSQLKHPNIVMYRES--WEGedcQLYIVMGFCEGG 87
Cdd:cd06644  20 LGDGAFGKVYKAKNKETGALAAAKVIE--TKSEEELEDYMVEIEILATCNHPYIVKLLGAfyWDG---KLWIMIEFCPGG 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  88 DL-YHRLKQQKGELLPERQVVewFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIA----RVLENQNdmas 162
Cdd:cd06644  95 AVdAIMLELDRGLTEPQIQVI--CRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSaknvKTLQRRD---- 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 163 TLIGTPYYMSPEL-----FSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQM--PSKYDPQLGEL 235
Cdd:cd06644 169 SFIGTPYWMAPEVvmcetMKDTPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSEPPTLsqPSKWSMEFRDF 248
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 41055987 236 IKRMLCKKPEDRPDVKHILRQPYIKHQISMflEATKEKTAKSR 278
Cdd:cd06644 249 LKTALDKHPETRPSAAQLLEHPFVSSVTSN--RPLRELVAEAK 289
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
8-247 2.98e-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: 139.76  E-value: 2.98e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRR--------ERRAaeqeaqLLSQLKHPNIVMYRESWEGEDcQLYI 79
Cdd:cd05575   1 KVIGKGSFGKVLLARHKAEGKLYAVKVLQKKAILKRnevkhimaERNV------LLKNVKHPFLVGLHYSFQTKD-KLYF 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  80 VMGFCEGGDLYHRLkqQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQND 159
Cdd:cd05575  74 VLDYVNGGELFFHL--QRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKEGIEPSD 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 160 MASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLpQMPSKYDPQLGELIKRM 239
Cdd:cd05575 152 TTSTFCGTPEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILHKPL-RLRTNVSPSARDLLEGL 230

                ....*...
gi 41055987 240 LCKKPEDR 247
Cdd:cd05575 231 LQKDRTKR 238
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
10-259 4.14e-36

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: 137.48  E-value: 4.14e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLnlrtssRRERRAAEQEAQLLSQL-------KHPNIVMYRESWEGEDcQLYIVMG 82
Cdd:cd14106  16 LGRGKFAVVRKCIHKETGKEYAAKFL------RKRRRGQDCRNEILHEIavlelckDCPRVVNLHEVYETRS-ELILILE 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FCEGGDLYHRLKQQkgELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNI---IKVGDLGIARVLENQND 159
Cdd:cd14106  89 LAAGGELQTLLDEE--ECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFPlgdIKLCDFGISRVIGEGEE 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 160 MAStLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPSKYD---PQLGELI 236
Cdd:cd14106 167 IRE-ILGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQCNLDFPEELFKdvsPLAIDFI 245
                       250       260
                ....*....|....*....|...
gi 41055987 237 KRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd14106 246 KRLLVKDPEKRLTAKECLEHPWL 268
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
4-285 6.16e-36

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


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 137.82  E-value: 6.16e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRerRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGF 83
Cdd:cd14166   5 FIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRD--SSLENEIAVLKRIKHENIVTLEDIYESTT-HYYLVMQL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGGDLYHRLKQQKgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNI-FLT--KTNIIKVGDLGIARVleNQNDM 160
Cdd:cd14166  82 VSGGELFDRILERG--VYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLlYLTpdENSKIMITDFGLSKM--EQNGI 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 161 ASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLpQMPSKYDPQLGE----LI 236
Cdd:cd14166 158 MSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGYY-EFESPFWDDISEsakdFI 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 41055987 237 KRMLCKKPEDRPDVKHILRQPYIKHQISMFLEATKEKTAKSRKNAANGK 285
Cdd:cd14166 237 RHLLEKNPSKRYTCEKALSHPWIIGNTALHRDIYPSVSEQIQKNFAKSK 285
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
4-259 8.22e-36

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: 136.81  E-value: 8.22e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRT-----SSRRERRAAE--------QEAQLLSQLKHPNIVMYRESW 70
Cdd:cd14077   3 WEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIPRASnaglkKEREKRLEKEisrdirtiREAALSSLLNHPHICRLRDFL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  71 EGEDCqLYIVMGFCEGGDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGI 150
Cdd:cd14077  83 RTPNH-YYMLFEYVDGGQLLDYIISHGK--LKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 151 ARVLENQnDMASTLIGTPYYMSPELFSNKPY-NYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLpQMPSKYD 229
Cdd:cd14077 160 SNLYDPR-RLLRTFCGSLYFAAPELLQAQPYtGPEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKIKKGKV-EYPSYLS 237
                       250       260       270
                ....*....|....*....|....*....|
gi 41055987 230 PQLGELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd14077 238 SECKSLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
9-259 9.72e-36

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: 136.38  E-value: 9.72e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   9 VVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSsrRERRAAEQEAQLLSQLKHPNIVMYRESWEgEDCQLYIVMGFCEGGD 88
Cdd:cd06624  15 VLGKGTFGVVYAARDLSTQVRIAIKEIPERDS--REVQPLHEEIALHSRLSHKNIVQYLGSVS-EDGFFKIFMEQVPGGS 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  89 LYHRLKQQKGELLPERQVVEWFV-QIAMALQYLHEKHILHRDLKTQNIFL-TKTNIIKVGDLGIARVLENQNDMASTLIG 166
Cdd:cd06624  92 LSALLRSKWGPLKDNENTIGYYTkQILEGLKYLHDNKIVHRDIKGDNVLVnTYSGVVKISDFGTSKRLAGINPCTETFTG 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 167 TPYYMSPELFSNKPYNY--KSDVWALGCCVYEMATLKHAF-NAKDMNSLVYRIVEGKL-PQMPSKYDPQLGELIKRMLCK 242
Cdd:cd06624 172 TLQYMAPEVIDKGQRGYgpPADIWSLGCTIIEMATGKPPFiELGEPQAAMFKVGMFKIhPEIPESLSEEAKSFILRCFEP 251
                       250
                ....*....|....*..
gi 41055987 243 KPEDRPDVKHILRQPYI 259
Cdd:cd06624 252 DPDKRATASDLLQDPFL 268
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
1-485 1.08e-35

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 146.04  E-value: 1.08e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987     1 MDGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDCQ-LYI 79
Cdd:PTZ00266   12 LNEYEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISYRGLKEREKSQLVIEVNVMRELKHKNIVRYIDRFLNKANQkLYI 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987    80 VMGFCEGGDLYHRLKQ--QKGELLPERQVVEWFVQIAMALQYLHE-------KHILHRDLKTQNIFLT-----------K 139
Cdd:PTZ00266   92 LMEFCDAGDLSRNIQKcyKMFGKIEEHAIVDITRQLLHALAYCHNlkdgpngERVLHRDLKPQNIFLStgirhigkitaQ 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   140 TN------IIKVGDLGIARVLENQNdMASTLIGTPYYMSPELF--SNKPYNYKSDVWALGCCVYEMATLKHAFN-AKDMN 210
Cdd:PTZ00266  172 ANnlngrpIAKIGDFGLSKNIGIES-MAHSCVGTPYYWSPELLlhETKSYDDKSDMWALGCIIYELCSGKTPFHkANNFS 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   211 SLVYRIVEGklPQMPSK-YDPQLGELIKRMLCKKPEDRPDVKHILRQPYIKHqismfleatkektAKSRKNAANGklnsa 289
Cdd:PTZ00266  251 QLISELKRG--PDLPIKgKSKELNILIKNLLNLSAKERPSALQCLGYQIIKN-------------VGPPVGAAGG----- 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   290 GSDASTKPNQVVQPQCLNSESKTCGKKAEEIYLNRQKPCNGAWENVAPKHHMPPKSPTRDIHNSTGQSIATISNIDIEIQ 369
Cdd:PTZ00266  311 GAGVAAAPGAVVARRNPSKEHPGLQLAAMEKAKHAEAANYGISPNTLINQRNEEQHGRRSSSCASRQSANNVTNITSITS 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   370 KQRKAKPPKPSShqnnnLPSVSKRREKEDPGapqTHPHKQVSGVGGTEDKMSANASSITPKPADRtkmpnksKALDvsld 449
Cdd:PTZ00266  391 VTSVASVASVAS-----VPSKDDRKYPQDGA---THCHAVNGHYGGRVDKDHAERARIEKENAHR-------KALE---- 451
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 41055987   450 ikddtMKLLQEAGVQDLPYEPTE-LHHNAEQKTESQR 485
Cdd:PTZ00266  452 -----MKILEKKRIERLEREERErLERERMERIERER 483
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
4-259 1.29e-35

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: 135.73  E-value: 1.29e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIK---KLNLRTSSRRErraAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIV 80
Cdd:cd14072   2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKiidKTQLNPSSLQK---LFREVRIMKILNHPNIVKLFEVIETEK-TLYLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MGFCEGGDLYHRLKQQkGELlPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDM 160
Cdd:cd14072  78 MEYASGGEVFDYLVAH-GRM-KEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFTPGNKL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 161 aSTLIGTPYYMSPELFSNKPYN-YKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLpQMPSKYDPQLGELIKRM 239
Cdd:cd14072 156 -DTFCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKY-RIPFYMSTDCENLLKKF 233
                       250       260
                ....*....|....*....|
gi 41055987 240 LCKKPEDRPDVKHILRQPYI 259
Cdd:cd14072 234 LVLNPSKRGTLEQIMKDRWM 253
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
2-240 2.33e-35

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: 136.03  E-value: 2.33e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSR-RERRAAEQEAQLLSQLKHPNIV-MYRESWEgeDCQLYI 79
Cdd:cd05612   1 DDFERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEVIRlKQEQHVHNEKRVLKEVSHPFIIrLFWTEHD--QRFLYM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  80 VMGFCEGGDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLenqND 159
Cdd:cd05612  79 LMEYVPGGELFSYLRNSGR--FSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKKL---RD 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 160 MASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLpQMPSKYDPQLGELIKRM 239
Cdd:cd05612 154 RTWTLCGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGKL-EFPRHLDLYAKDLIKKL 232

                .
gi 41055987 240 L 240
Cdd:cd05612 233 L 233
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
6-259 2.34e-35

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: 135.91  E-value: 2.34e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   6 FVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLrtsSRRERRAAEQEAQLLSQLKH-PNIVMY-----RESWEGEDCQLYI 79
Cdd:cd06636  20 LVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDV---TEDEEEEIKLEINMLKKYSHhRNIATYygafiKKSPPGHDDQLWL 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  80 VMGFCEGGDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQND 159
Cdd:cd06636  97 VMEFCGAGSVTDLVKNTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVG 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 160 MASTLIGTPYYMSPELFS-----NKPYNYKSDVWALGCCVYEMAtlKHAFNAKDMNSL--VYRIVEGKLPQMPS-KYDPQ 231
Cdd:cd06636 177 RRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMA--EGAPPLCDMHPMraLFLIPRNPPPKLKSkKWSKK 254
                       250       260
                ....*....|....*....|....*...
gi 41055987 232 LGELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd06636 255 FIDFIEGCLVKNYLSRPSTEQLLKHPFI 282
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
7-251 3.69e-35

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: 136.63  E-value: 3.69e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   7 VRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTS-SRRERRAAEQEAQ-LLSQLKHPNIVMYRESWEGEDcQLYIVMGFC 84
Cdd:cd05604   1 LKVIGKGSFGKVLLAKRKRDGKYYAVKVLQKKVIlNRKEQKHIMAERNvLLKNVKHPFLVGLHYSFQTTD-KLYFVLDFV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  85 EGGDLYHRLkqQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTL 164
Cdd:cd05604  80 NGGELFFHL--QRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKEGISNSDTTTTF 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 165 IGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPSKYDPQLgELIKRMLCKKP 244
Cdd:cd05604 158 CGTPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENILHKPLVLRPGISLTAW-SILEELLEKDR 236

                ....*..
gi 41055987 245 EDRPDVK 251
Cdd:cd05604 237 QLRLGAK 243
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
4-259 3.82e-35

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: 134.44  E-value: 3.82e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRK----QYVIKKLNLRTSSRRERRAAE--QEAQLLSQLK---HPNIVMYRESWEGED 74
Cdd:cd14004   2 YTILKEMGEGAYGQVNLAIYKSKGKevviKFIFKERILVDTWVRDRKLGTvpLEIHILDTLNkrsHPNIVKLLDFFEDDE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  75 cQLYIVM-GFCEGGDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARV 153
Cdd:cd14004  82 -FYYLVMeKHGSGMDLFDFIERKPN--MDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFGSAAY 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 154 LENQNdmASTLIGTPYYMSPELFSNKPYNYKS-DVWALGCCVYEMATLKHAFnakdmnSLVYRIVEGKLpQMPSKYDPQL 232
Cdd:cd14004 159 IKSGP--FDTFVGTIDYAAPEVLRGNPYGGKEqDIWALGVLLYTLVFKENPF------YNIEEILEADL-RIPYAVSEDL 229
                       250       260
                ....*....|....*....|....*..
gi 41055987 233 GELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd14004 230 IDLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
3-258 5.17e-35

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: 133.96  E-value: 5.17e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   3 GYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNlrtssrrERRAAE--------QEAQLLSQLKHPNIVMYRESWEGED 74
Cdd:cd14162   1 GYIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVS-------KKKAPEdylqkflpREIEVIKGLKHPNLICFYEAIETTS 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  75 cQLYIVMGFCEGGDLYHRLKQQKgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIAR-- 152
Cdd:cd14162  74 -RVYIIMELAENGDLLDYIRKNG--ALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFARgv 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 153 --VLENQNDMASTLIGTPYYMSPELFSNKPYN-YKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEG-KLPQMPSKY 228
Cdd:cd14162 151 mkTKDGKPKLSETYCGSYAYASPEILRGIPYDpFLSDIWSMGVVLYTMVYGRLPFDDSNLKVLLKQVQRRvVFPKNPTVS 230
                       250       260       270
                ....*....|....*....|....*....|
gi 41055987 229 DPqLGELIKRMLCKKPEdRPDVKHILRQPY 258
Cdd:cd14162 231 EE-CKDLILRMLSPVKK-RITIEEIKRDPW 258
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
4-259 5.73e-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: 134.17  E-value: 5.73e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRE--RRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVM 81
Cdd:cd14070   4 YLIGRKLGEGSFAKVREGLHAVTGEKVAIKVIDKKKAKKDSyvTKNLRREGRIQQMIRHPNITQLLDILETEN-SYYLVM 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  82 GFCEGGDLYHRLKQQKgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARV--LENQND 159
Cdd:cd14070  83 ELCPGGNLMHRIYDKK--RLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNCagILGYSD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 160 MASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMN--SLVYRIVEGKLPQMPSKYDPQLGELIK 237
Cdd:cd14070 161 PFSTQCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPFTVEPFSlrALHQKMVDKEMNPLPTDLSPGAISFLR 240
                       250       260
                ....*....|....*....|..
gi 41055987 238 RMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd14070 241 SLLEPDPLKRPNIKQALANRWL 262
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
4-258 6.77e-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: 133.51  E-value: 6.77e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKL-NLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMG 82
Cdd:cd14189   3 YCKGRLLGKGGFARCYEMTDLATNKTYAVKVIpHSRVAKPHQREKIVNEIELHRDLHHKHVVKFSHHFEDAE-NIYIFLE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FCEGGDLYHRLKQQKGELLPErqvVEWFV-QIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMA 161
Cdd:cd14189  82 LCSRKSLAHIWKARHTLLEPE---VRYYLkQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAARLEPPEQRK 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 162 STLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSlVYRIVEGKLPQMPSKYDPQLGELIKRMLC 241
Cdd:cd14189 159 KTICGTPNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETLDLKE-TYRCIKQVKYTLPASLSLPARHLLAGILK 237
                       250
                ....*....|....*..
gi 41055987 242 KKPEDRPDVKHILRQPY 258
Cdd:cd14189 238 RNPGDRLTLDQILEHEF 254
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
38-257 9.87e-35

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: 133.71  E-value: 9.87e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  38 RTSSRRERRAAE---QEAQLLSQLKHPNIV-MYRESweGEDCQLYIVMGFCEGGDLYHRLKQQKGelLPERQVVEWFVQI 113
Cdd:cd06630  37 RNSSSEQEEVVEairEEIRMMARLNHPNIVrMLGAT--QHKSHFNIFVEWMAGGSVASLLSKYGA--FSENVIINYTLQI 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 114 AMALQYLHEKHILHRDLKTQNIFLTKT-NIIKVGDLGIARVLENQNDMAS----TLIGTPYYMSPELFSNKPYNYKSDVW 188
Cdd:cd06630 113 LRGLAYLHDNQIIHRDLKGANLLVDSTgQRLRIADFGAAARLASKGTGAGefqgQLLGTIAFMAPEVLRGEQYGRSCDVW 192
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41055987 189 ALGCCVYEMATLKHAFNAKDMN---SLVYRIVEG-KLPQMPSKYDPQLGELIKRMLCKKPEDRPDVKHILRQP 257
Cdd:cd06630 193 SVGCVIIEMATAKPPWNAEKISnhlALIFKIASAtTPPPIPEHLSPGLRDVTLRCLELQPEDRPPARELLKHP 265
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
11-258 1.01e-34

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: 132.78  E-value: 1.01e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  11 GKGSYGEVNLVRHKSDRKQYVIKKLNLRtssRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEGGDLY 90
Cdd:cd14006   2 GRGRFGVVKRCIEKATGREFAAKFIPKR---DKKKEAVLREISILNQLQHPRIIQLHEAYESPT-ELVLILELCSGGELL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  91 HRLKQQkgELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLT--KTNIIKVGDLGIARVLeNQNDMASTLIGTP 168
Cdd:cd14006  78 DRLAER--GSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLAdrPSPQIKIIDFGLARKL-NPGEELKEIFGTP 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 169 YYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKL---PQMPSKYDPQLGELIKRMLCKKPE 245
Cdd:cd14006 155 EFVAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVdfsEEYFSSVSQEAKDFIRKLLVKEPR 234
                       250
                ....*....|...
gi 41055987 246 DRPDVKHILRQPY 258
Cdd:cd14006 235 KRPTAQEALQHPW 247
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
42-249 1.27e-34

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 139.93  E-value: 1.27e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   42 RRERRaaeqEAQLLSQLKHPNIV-MYrESWEGEDCQlYIVMGFCEGGDLyHRLKQQKGELLPERqVVEWFVQIAMALQYL 120
Cdd:NF033483  52 ARFRR----EAQSAASLSHPNIVsVY-DVGEDGGIP-YIVMEYVDGRTL-KDYIREHGPLSPEE-AVEIMIQILSALEHA 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  121 HEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLeNQNDMAST--LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMA 198
Cdd:NF033483 124 HRNGIVHRDIKPQNILITKDGRVKVTDFGIARAL-SSTTMTQTnsVLGTVHYLSPEQARGGTVDARSDIYSLGIVLYEML 202
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41055987  199 T--------------LKHaFNaKDMNSlvyrivegklpqmPSKYDP----QLGELIKRMLCKKPEDRPD 249
Cdd:NF033483 203 TgrppfdgdspvsvaYKH-VQ-EDPPP-------------PSELNPgipqSLDAVVLKATAKDPDDRYQ 256
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
8-247 1.72e-34

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: 133.61  E-value: 1.72e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKQYVIKKL-NLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDCqLYIVMGFCEG 86
Cdd:cd05630   6 RVLGKGGFGEVCACQVRATGKMYACKKLeKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDA-LCLVLTLMNG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  87 GDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIA-RVLENQNDMAStlI 165
Cdd:cd05630  85 GDLKFHIYHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAvHVPEGQTIKGR--V 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 166 GTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNA---KDMNSLVYRIVEGKLPQMPSKYDPQLGELIKRMLCK 242
Cdd:cd05630 163 GTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQrkkKIKREEVERLVKEVPEEYSEKFSPQARSLCSMLLCK 242

                ....*
gi 41055987 243 KPEDR 247
Cdd:cd05630 243 DPAER 247
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
4-256 2.10e-34

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: 133.19  E-value: 2.10e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLnlRTSSRRERRAAEQEAQLLSQLKHPNI-------VMYREsweGEDCQ 76
Cdd:cd13986   2 YRIQRLLGEGGFSFVYLVEDLSTGRLYALKKI--LCHSKEDVKEAMREIENYRLFNHPNIlrlldsqIVKEA---GGKKE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  77 LYIVMGFCEGGDLYH--RLKQQKGELLPERQVVEWFVQIAMALQYLHE---KHILHRDLKTQNIFLTKTNIIKVGDLG-- 149
Cdd:cd13986  77 VYLLLPYYKRGSLQDeiERRLVKGTFFPEDRILHIFLGICRGLKAMHEpelVPYAHRDIKPGNVLLSEDDEPILMDLGsm 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 150 -IARVLENQNDMASTLI------GTPYYMSPELFSNKPY---NYKSDVWALGCCVYEMATLKHAFnakDM-----NSLVY 214
Cdd:cd13986 157 nPARIEIEGRREALALQdwaaehCTMPYRAPELFDVKSHctiDEKTDIWSLGCTLYALMYGESPF---ERifqkgDSLAL 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 41055987 215 RIVEGKL-PQMPSKYDPQLGELIKRMLCKKPEDRPDVKHILRQ 256
Cdd:cd13986 234 AVLSGNYsFPDNSRYSEELHQLVKSMLVVNPAERPSIDDLLSR 276
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
8-261 2.18e-34

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: 134.06  E-value: 2.18e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDR---KQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFC 84
Cdd:cd05582   1 KVLGQGSFGKVFLVRKITGPdagTLYAMKVLKKATLKVRDRVRTKMERDILADVNHPFIVKLHYAFQTEG-KLYLILDFL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  85 EGGDLYHRLkqQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTL 164
Cdd:cd05582  80 RGGDLFTRL--SKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKESIDHEKKAYSF 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 165 IGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLpQMPSKYDPQLGELIkRMLCKK- 243
Cdd:cd05582 158 CGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAKL-GMPQFLSPEAQSLL-RALFKRn 235
                       250       260
                ....*....|....*....|...
gi 41055987 244 PEDR----PD-VKHILRQPYIKH 261
Cdd:cd05582 236 PANRlgagPDgVEEIKRHPFFAT 258
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
10-248 4.17e-34

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: 131.81  E-value: 4.17e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIV----MYRESWEgedcqLYIVMGFCE 85
Cdd:cd13978   1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIEERKALLKEAEKMERARHSYVLpllgVCVERRS-----LGLVMEYME 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  86 GGDLYHRLKQqkgellpERQVVEWFV------QIAMALQYLH--EKHILHRDLKTQNIFLTKTNIIKVGDLGIARV---- 153
Cdd:cd13978  76 NGSLKSLLER-------EIQDVPWSLrfriihEIALGMNFLHnmDPPLLHHDLKPENILLDNHFHVKISDFGLSKLgmks 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 154 -LENQNDMASTLIGTPYYMSPELFS--NKPYNYKSDVWALGCCVYEMATLKHAF-NAKDMNSLVYRIVEGKLPQMPS--- 226
Cdd:cd13978 149 iSANRRRGTENLGGTPIYMAPEAFDdfNKKPTSKSDVYSFAIVIWAVLTRKEPFeNAINPLLIMQIVSKGDRPSLDDigr 228
                       250       260
                ....*....|....*....|....*.
gi 41055987 227 -KYDPQLGELIKRM-LC--KKPEDRP 248
Cdd:cd13978 229 lKQIENVQELISLMiRCwdGNPDARP 254
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
10-259 4.69e-34

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: 132.42  E-value: 4.69e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRErrAAEQEAQLLSQLKHPNIV-MYRESWEGEdcQLYIVMGFCEGGD 88
Cdd:cd06659  29 IGEGSTGVVCIAREKHSGRQVAVKMMDLRKQQRRE--LLFNEVVIMRDYQHPNVVeMYKSYLVGE--ELWVLMEYLQGGA 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  89 LYHRLKQQKgelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLIGTP 168
Cdd:cd06659 105 LTDIVSQTR---LNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFCAQISKDVPKRKSLVGTP 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 169 YYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQM--PSKYDPQLGELIKRMLCKKPED 246
Cdd:cd06659 182 YWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRDSPPPKLknSHKASPVLRDFLERMLVRDPQE 261
                       250
                ....*....|...
gi 41055987 247 RPDVKHILRQPYI 259
Cdd:cd06659 262 RATAQELLDHPFL 274
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
6-197 4.85e-34

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: 133.60  E-value: 4.85e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   6 FVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRT--SSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGF 83
Cdd:cd05602  11 FLKVIGKGSFGKVLLARHKSDEKFYAVKVLQKKAilKKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQTTD-KLYFVLDY 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGGDLYHRLKQQKGELLPERQVveWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMAST 163
Cdd:cd05602  90 INGGELFYHLQRERCFLEPRARF--YAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIEPNGTTST 167
                       170       180       190
                ....*....|....*....|....*....|....
gi 41055987 164 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEM 197
Cdd:cd05602 168 FCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEM 201
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
9-259 5.93e-34

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: 131.12  E-value: 5.93e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   9 VVGKGSYGEVNLVRHKSDRKQYVIKKLNLRtssRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEGGD 88
Cdd:cd14087   8 LIGRGSFSRVVRVEHRVTRQPYAIKMIETK---CRGREVCESELNVLRRVRHTNIIQLIEVFETKE-RVYMVMELATGGE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  89 LYHRLKQqKGELlPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNI---IKVGDLGIARVLE-NQNDMASTL 164
Cdd:cd14087  84 LFDRIIA-KGSF-TERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPdskIMITDFGLASTRKkGPNCLMKTT 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 165 IGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKL---PQMPSKYDPQLGELIKRMLC 241
Cdd:cd14087 162 CGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYsysGEPWPSVSNLAKDFIDRLLT 241
                       250
                ....*....|....*...
gi 41055987 242 KKPEDRPDVKHILRQPYI 259
Cdd:cd14087 242 VNPGERLSATQALKHPWI 259
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
4-257 1.18e-33

Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Myt1 is a cytoplasmic cell cycle checkpoint kinase that can keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of N-terminal thr (T14) and tyr (Y15) residues, leading to the delay of meiosis I entry. Meiotic progression is ensured by a two-step inhibition and downregulation of Myt1 by CDK1/XRINGO and p90Rsk during oocyte maturation. In addition, Myt1 targets cyclin B1/B2 and is essential for Golgi and ER assembly during telophase. In Drosophila, Myt1 may be a downstream target of Notch during eye development. The Myt1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 129.74  E-value: 1.18e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLK-HPNIVMYRESWEgEDCQLYIVMG 82
Cdd:cd14050   3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKRSRSRFRGEKDRKRKLEEVERHEKLGeHPNCVRFIKAWE-EKGILYIQTE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FCEGGDLYHRLKQQKgelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIarVLE-NQNDMA 161
Cdd:cd14050  82 LCDTSLQQYCEETHS---LPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGL--VVElDKEDIH 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 162 STLIGTPYYMSPELFsNKPYNYKSDVWALGCCVYEMATlkhafnakDMN-----SLVYRIVEGKLPQ-MPSKYDPQLGEL 235
Cdd:cd14050 157 DAQEGDPRYMAPELL-QGSFTKAADIFSLGITILELAC--------NLElpsggDGWHQLRQGYLPEeFTAGLSPELRSI 227
                       250       260
                ....*....|....*....|..
gi 41055987 236 IKRMLCKKPEDRPDVKHILRQP 257
Cdd:cd14050 228 IKLMMDPDPERRPTAEDLLALP 249
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
4-258 1.22e-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: 130.90  E-value: 1.22e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGF 83
Cdd:cd07833   3 YEVLGVVGEGAYGVVLKCRNKATGEIVAIKKFKESEDDEDVKKTALREVKVLRQLRHENIVNLKEAFRRKG-RLYLVFEY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGgDLYHRLKQQKGELLPErQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMAST 163
Cdd:cd07833  82 VER-TLLELLEASPGGLPPD-AVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARALTARPASPLT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 164 -LIGTPYYMSPELF-SNKPYNYKSDVWALGCCVYEMATLKHAFNAK-DMNSLvYRI--VEGKLPQ--------------- 223
Cdd:cd07833 160 dYVATRWYRAPELLvGDTNYGKPVDVWAIGCIMAELLDGEPLFPGDsDIDQL-YLIqkCLGPLPPshqelfssnprfagv 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 41055987 224 --------------MPSKYDPQLGELIKRMLCKKPEDRPDVKHILRQPY 258
Cdd:cd07833 239 afpepsqpeslerrYPGKVSSPALDFLKACLRMDPKERLTCDELLQHPY 287
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
11-246 1.23e-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: 131.03  E-value: 1.23e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  11 GKGSYGEVNLVRHKSDRKQYVIKKLNLRTS-SRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDCQL-----YIVMGFC 84
Cdd:cd13989   2 GSGGFGYVTLWKHQDTGEYVAIKKCRQELSpSDKNRERWCLEVQIMKKLNHPNVVSARDVPPELEKLSpndlpLLAMEYC 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  85 EGGDLYHRLKQQKGEL-LPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTN---IIKVGDLGIARVLEnQNDM 160
Cdd:cd13989  82 SGGDLRKVLNQPENCCgLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGgrvIYKLIDLGYAKELD-QGSL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 161 ASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEmatlkhafnakdmnslvyrIVEGKLPQMPSKYDPQLGELIKRml 240
Cdd:cd13989 161 CTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFE-------------------CITGYRPFLPNWQPVQWHGKVKQ-- 219

                ....*.
gi 41055987 241 cKKPED 246
Cdd:cd13989 220 -KKPEH 224
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
3-259 1.82e-33

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: 129.90  E-value: 1.82e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   3 GYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRR-ERRAAEQEAQLLSQLKHPNIVMYRESWEGEDCQLYIVM 81
Cdd:cd14165   2 GYILGINLGEGSYAKVKSAYSERLKCNVAIKIIDKKKAPDDfVEKFLPRELEILARLNHKSIIKTYEIFETSDGKVYIVM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  82 GFCEGGDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQND-- 159
Cdd:cd14165  82 ELGVQGDLLEFIKLRGA--LPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCLRDENgr 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 160 --MASTLIGTPYYMSPELFSNKPYNYK-SDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPSKYDP-QLGEL 235
Cdd:cd14165 160 ivLSKTFCGSAAYAAPEVLQGIPYDPRiYDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQKEHRVRFPRSKNLTsECKDL 239
                       250       260
                ....*....|....*....|....
gi 41055987 236 IKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd14165 240 IYRLLQPDVSQRLCIDEVLSHPWL 263
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
10-247 1.85e-33

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: 130.34  E-value: 1.85e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNL-RTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEGGD 88
Cdd:cd05577   1 LGRGGFGEVCACQVKATGKMYACKKLDKkRIKKKKGETMALNEKIILEKVSSPFIVSLAYAFETKD-KLCLVLTLMNGGD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  89 LYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTlIGTP 168
Cdd:cd05577  80 LKYHIYNVGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVEFKGGKKIKGR-VGTH 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 169 YYMSPELFSNK-PYNYKSDVWALGCCVYEMATLKHAFNA---KDMNSLVYRIVEGKLPQMPSKYDPQLGELIKRMLCKKP 244
Cdd:cd05577 159 GYMAPEVLQKEvAYDFSVDWFALGCMLYEMIAGRSPFRQrkeKVDKEELKRRTLEMAVEYPDSFSPEARSLCEGLLQKDP 238

                ...
gi 41055987 245 EDR 247
Cdd:cd05577 239 ERR 241
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
10-255 1.89e-33

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: 130.09  E-value: 1.89e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRkQYVIKKLNLRTSSRRERRAaEQEAQLLSQLKHPNIVMYRE-SWEGEDCQLyiVMGFCEGGD 88
Cdd:cd14066   1 IGSGGFGTVYKGVLENGT-VVAVKRLNEMNCAASKKEF-LTELEMLGRLRHPNLVRLLGyCLESDEKLL--VYEYMPNGS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  89 LYHRLKQQKG-ELLPERQVVEWFVQIAMALQYLHE---KHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMAST- 163
Cdd:cd14066  77 LEDRLHCHKGsPPLPWPQRLKIAKGIARGLEYLHEecpPPIIHGDIKSSNILLDEDFEPKLTDFGLARLIPPSESVSKTs 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 164 -LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEgklpQMPSKYDPQLGELIKRMLCK 242
Cdd:cd14066 157 aVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDENRENASRKDLVE----WVESKGKEELEDILDKRLVD 232
                       250
                ....*....|....
gi 41055987 243 KPEDRPD-VKHILR 255
Cdd:cd14066 233 DDGVEEEeVEALLR 246
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
7-253 2.36e-33

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: 129.99  E-value: 2.36e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   7 VRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLrTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGE----------DCQ 76
Cdd:cd14048  11 IQCLGRGGFGVVFEAKNKVDDCNYAVKRIRL-PNNELAREKVLREVRALAKLDHPGIVRYFNAWLERppegwqekmdEVY 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  77 LYIVMGFCEGGDLYHRLKQQKGELLPERQV-VEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIA---- 151
Cdd:cd14048  90 LYIQMQLCRKENLKDWMNRRCTMESRELFVcLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVGDFGLVtamd 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 152 --------RVLENQNDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEmatLKHAFNAKDMNSLVYRIVE-GKLP 222
Cdd:cd14048 170 qgepeqtvLTPMPAYAKHTGQVGTRLYMSPEQIHGNQYSEKVDIFALGLILFE---LIYSFSTQMERIRTLTDVRkLKFP 246
                       250       260       270
                ....*....|....*....|....*....|.
gi 41055987 223 QMPSKYDPQLGELIKRMLCKKPEDRPDVKHI 253
Cdd:cd14048 247 ALFTNKYPEERDMVQQMLSPSPSERPEAHEV 277
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
10-259 3.89e-33

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: 129.38  E-value: 3.89e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNlrTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEGGDL 89
Cdd:cd06643  13 LGDGAFGKVYKAQNKETGILAAAKVID--TKSEEELEDYMVEIDILASCDHPNIVKLLDAFYYEN-NLWILIEFCAGGAV 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  90 YH-RLKQQKGELLPERQVVewFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIA----RVLENQNdmasTL 164
Cdd:cd06643  90 DAvMLELERPLTEPQIRVV--CKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSakntRTLQRRD----SF 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 165 IGTPYYMSPELF-----SNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQM--PSKYDPQLGELIK 237
Cdd:cd06643 164 IGTPYWMAPEVVmcetsKDRPYDYKADVWSLGVTLIEMAQIEPPHHELNPMRVLLKIAKSEPPTLaqPSRWSPEFKDFLR 243
                       250       260
                ....*....|....*....|..
gi 41055987 238 RMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd06643 244 KCLEKNVDARWTTSQLLQHPFV 265
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
10-258 4.31e-33

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 130.71  E-value: 4.31e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSR-RERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEGGD 88
Cdd:PTZ00263  26 LGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKmKQVQHVAQEKSILMELSHPFIVNMMCSFQDEN-RVYFLLEFVVGGE 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   89 LYHRLKqqKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLenqNDMASTLIGTP 168
Cdd:PTZ00263 105 LFTHLR--KAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKV---PDRTFTLCGTP 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  169 YYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLpQMPSKYDPQLGELIKRMLCKKPEDR- 247
Cdd:PTZ00263 180 EYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRL-KFPNWFDGRARDLVKGLLQTDHTKRl 258
                        250
                 ....*....|....*...
gi 41055987  248 -------PDVKhilRQPY 258
Cdd:PTZ00263 259 gtlkggvADVK---NHPY 273
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
4-261 5.26e-33

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


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 130.34  E-value: 5.26e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNL----RTSSRRERRaaeqEAQLLSQLKHPNIV-----MYRESWEGED 74
Cdd:cd07834   2 YELLKPIGSGAYGVVCSAYDKRTGRKVAIKKISNvfddLIDAKRILR----EIKILRHLKHENIIglldiLRPPSPEEFN 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  75 cQLYIVMGFCEGgDLyHRLKQQKGELLPERqvVEWFV-QIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARV 153
Cdd:cd07834  78 -DVYIVTELMET-DL-HKVIKSPQPLTDDH--IQYFLyQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGLARG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 154 LENQNDmASTLIG---TPYYMSPEL-FSNKPYNYKSDVWALGCCVYEMATLKHAFNAKD--------------------- 208
Cdd:cd07834 153 VDPDED-KGFLTEyvvTRWYRAPELlLSSKKYTKAIDIWSVGCIFAELLTRKPLFPGRDyidqlnlivevlgtpseedlk 231
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41055987 209 ----------MNSLVYRivEGK-LPQMPSKYDPQLGELIKRMLCKKPEDRPDVKHILRQPYIKH 261
Cdd:cd07834 232 fissekarnyLKSLPKK--PKKpLSEVFPGASPEAIDLLEKMLVFNPKKRITADEALAHPYLAQ 293
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
8-227 7.59e-33

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: 129.70  E-value: 7.59e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRA---AEQEAqLLSQLKHPNIVMYRESWEGEDcQLYIVMGFC 84
Cdd:cd05603   1 KVIGKGSFGKVLLAKRKCDGKFYAVKVLQKKTILKKKEQNhimAERNV-LLKNLKHPFLVGLHYSFQTSE-KLYFVLDYV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  85 EGGDLYHRLKQQKGELLPERQVveWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTL 164
Cdd:cd05603  79 NGGELFFHLQRERCFLEPRARF--YAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEGMEPEETTSTF 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41055987 165 IGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPSK 227
Cdd:cd05603 157 CGTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILHKPLHLPGGK 219
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
10-254 9.13e-33

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: 126.84  E-value: 9.13e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDrkQYVIKKLnlrtssrreRRAAEQEAQLLSQLKHPNIVMYRESWEGEDCQLyIVMGFCEGGDL 89
Cdd:cd14059   1 LGSGAQGAVFLGKFRGE--EVAVKKV---------RDEKETDIKHLRKLNHPNIIKFKGVCTQAPCYC-ILMEYCPYGQL 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  90 YHRLKQQKgELLPERqVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLeNQNDMASTLIGTPY 169
Cdd:cd14059  69 YEVLRAGR-EITPSL-LVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKEL-SEKSTKMSFAGTVA 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 170 YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEG--KLPqMPSKYDPQLGELIKRMLCKKPEDR 247
Cdd:cd14059 146 WMAPEVIRNEPCSEKVDIWSFGVVLWELLTGEIPYKDVDSSAIIWGVGSNslQLP-VPSTCPDGFKLLMKQCWNSKPRNR 224

                ....*..
gi 41055987 248 PDVKHIL 254
Cdd:cd14059 225 PSFRQIL 231
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
4-259 1.04e-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: 127.12  E-value: 1.04e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIK--------KLNLRTSSRrerraaeqEAQLLSQLKHPNIVMYRESWEGEDc 75
Cdd:cd14071   2 YDIERTIGKGNFAVVKLARHRITKTEVAIKiidksqldEENLKKIYR--------EVQIMKMLNHPHIIKLYQVMETKD- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  76 QLYIVMGFCEGGDLYHRLKQQkgELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLE 155
Cdd:cd14071  73 MLYLVTEYASNGEIFDYLAQH--GRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSNFFK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 156 NqNDMASTLIGTPYYMSPELFSNKPYN-YKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLpQMPSKYDPQLGE 234
Cdd:cd14071 151 P-GELLKTWCGSPPYAAPEVFEGKEYEgPQLDIWSLGVVLYVLVCGALPFDGSTLQTLRDRVLSGRF-RIPFFMSTDCEH 228
                       250       260
                ....*....|....*....|....*
gi 41055987 235 LIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd14071 229 LIRRMLVLDPSKRLTIEQIKKHKWM 253
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
8-259 1.31e-32

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: 127.27  E-value: 1.31e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRT-SSRRERR------AAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIV 80
Cdd:cd06628   6 ALIGSGSFGSVYLGMNASSGELMAVKQVELPSvSAENKDRkksmldALQREIALLRELQHENIVQYLGSSSDAN-HLNIF 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MGFCEGGDLYHRLKQQkGELlpERQVVEWFV-QIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLE---- 155
Cdd:cd06628  85 LEYVPGGSVATLLNNY-GAF--EESLVRNFVrQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKKLEansl 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 156 --NQNDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPSKYDPQLG 233
Cdd:cd06628 162 stKNNGARPSLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFPDCTQMQAIFKIGENASPTIPSNISSEAR 241
                       250       260
                ....*....|....*....|....*.
gi 41055987 234 ELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd06628 242 DFLEKTFEIDHNKRPTADELLKHPFL 267
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
2-259 1.44e-32

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


Pssm-ID: 271069 [Multi-domain]  Cd Length: 263  Bit Score: 127.07  E-value: 1.44e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERrAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVM 81
Cdd:cd14167   3 DIYDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGKET-SIENEIAVLHKIKHPNIVALDDIYESGG-HLYLIM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  82 GFCEGGDLYHRLkQQKGeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIF---LTKTNIIKVGDLGIARVlENQN 158
Cdd:cd14167  81 QLVSGGELFDRI-VEKG-FYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGLSKI-EGSG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 159 DMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLpQMPSKYDPQLG----E 234
Cdd:cd14167 158 SVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEY-EFDSPYWDDISdsakD 236
                       250       260
                ....*....|....*....|....*
gi 41055987 235 LIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd14167 237 FIQHLMEKDPEKRFTCEQALQHPWI 261
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
3-247 1.59e-32

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: 127.08  E-value: 1.59e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   3 GYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKL-----NLRTSSRRERRAAEQEAQLLSQL-KHPNIVMYRESWEGEDCq 76
Cdd:cd13993   1 RYQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLyksgpNSKDGNDFQKLPQLREIDLHRRVsRHPNIITLHDVFETEVA- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  77 LYIVMGFCEGGDLY-----HRLKQQKGELLpeRQVvewFVQIAMALQYLHEKHILHRDLKTQNIFLT-KTNIIKVGDLGI 150
Cdd:cd13993  80 IYIVLEYCPNGDLFeaiteNRIYVGKTELI--KNV---FLQLIDAVKHCHSLGIYHRDIKPENILLSqDEGTVKLCDFGL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 151 ARVLENQNDMAstlIGTPYYMSPELFSNKPYNYKS------DVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQM 224
Cdd:cd13993 155 ATTEKISMDFG---VGSEFYMAPECFDEVGRSLKGypcaagDIWSLGIILLNLTFGRNPWKIASESDPIFYDYYLNSPNL 231
                       250       260
                ....*....|....*....|....*.
gi 41055987 225 PSKYDP---QLGELIKRMLCKKPEDR 247
Cdd:cd13993 232 FDVILPmsdDFYNLLRQIFTVNPNNR 257
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
2-258 1.86e-32

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: 126.68  E-value: 1.86e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNlRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEgEDCQLYIVM 81
Cdd:cd14184   1 EKYKIGKVIGDGNFAVVKECVERSTGKEFALKIID-KAKCCGKEHLIENEVSILRRVKHPNIIMLIEEMD-TPAELYLVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  82 GFCEGGDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFL----TKTNIIKVGDLGIARVLENQ 157
Cdd:cd14184  79 ELVKGGDLFDAITSSTK--YTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVceypDGTKSLKLGDFGLATVVEGP 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 158 ndmASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKD--MNSLVYRIVEGKLpQMPSKYDPQLG-- 233
Cdd:cd14184 157 ---LYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSENnlQEDLFDQILLGKL-EFPSPYWDNITds 232
                       250       260
                ....*....|....*....|....*..
gi 41055987 234 --ELIKRMLCKKPEDRPDVKHILRQPY 258
Cdd:cd14184 233 akELISHMLQVNVEARYTAEQILSHPW 259
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
2-260 1.92e-32

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: 127.80  E-value: 1.92e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRErraAEQEAQLLSQL-KHPNIVM-YRESWEGEDC---Q 76
Cdd:cd06639  22 DTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKILDPISDVDEE---IEAEYNILRSLpNHPNVVKfYGMFYKADQYvggQ 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  77 LYIVMGFCEGGDLYHRLKQ--QKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVL 154
Cdd:cd06639  99 LWLVLELCNGGSVTELVKGllKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQL 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 155 ENQNDMASTLIGTPYYMSPELFS-----NKPYNYKSDVWALGCCVYEMATLKHAFNakDMNSL--VYRIVEGKLPQM--P 225
Cdd:cd06639 179 TSARLRRNTSVGTPFWMAPEVIAceqqyDYSYDARCDVWSLGITAIELADGDPPLF--DMHPVkaLFKIPRNPPPTLlnP 256
                       250       260       270
                ....*....|....*....|....*....|....*
gi 41055987 226 SKYDPQLGELIKRMLCKKPEDRPDVKHILRQPYIK 260
Cdd:cd06639 257 EKWCRGFSHFISQCLIKDFEKRPSVTHLLEHPFIK 291
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
10-261 2.02e-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: 127.54  E-value: 2.02e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDCQlYIVMGFCEGGDL 89
Cdd:cd14086   9 LGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFH-YLVFDLVTGGEL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  90 YHRLKQQkgELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFL---TKTNIIKVGDLGIARVLENQNDMASTLIG 166
Cdd:cd14086  88 FEDIVAR--EFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLaskSKGAAVKLADFGLAIEVQGDQQAWFGFAG 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 167 TPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPSKYD---PQLGELIKRMLCKK 243
Cdd:cd14086 166 TPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSPEWDtvtPEAKDLINQMLTVN 245
                       250
                ....*....|....*...
gi 41055987 244 PEDRPDVKHILRQPYIKH 261
Cdd:cd14086 246 PAKRITAAEALKHPWICQ 263
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
8-259 2.05e-32

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: 126.41  E-value: 2.05e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRER-RAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEG 86
Cdd:cd06607   7 REIGHGSFGAVYYARNKRTSEVVAIKKMSYSGKQSTEKwQDIIKEVKFLRQLRHPNTIEYKGCYLREH-TAWLVMEYCLG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  87 --GDLYHRLKQqkgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLenqnDMASTL 164
Cdd:cd06607  86 saSDIVEVHKK----PLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFGSASLV----CPANSF 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 165 IGTPYYMSPEL---FSNKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLvYRIVEGKLPQMPS-KYDPQLGELIKRM 239
Cdd:cd06607 158 VGTPYWMAPEVilaMDEGQYDGKVDVWSLGITCIELAERKPPlFNMNAMSAL-YHIAQNDSPTLSSgEWSDDFRNFVDSC 236
                       250       260
                ....*....|....*....|
gi 41055987 240 LCKKPEDRPDVKHILRQPYI 259
Cdd:cd06607 237 LQKIPQDRPSAEDLLKHPFV 256
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
3-261 2.15e-32

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: 127.36  E-value: 2.15e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   3 GYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLnlrtssRRERRAAEQEAQ-LLSQLKHPNIVMYRESWEgEDCQLYIVM 81
Cdd:cd14091   1 EYEIKEEIGKGSYSVCKRCIHKATGKEYAVKII------DKSKRDPSEEIEiLLRYGQHPNIITLRDVYD-DGNSVYLVT 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  82 GFCEGGDLYHRLKQQKgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNI-FLTKT---NIIKVGDLGIARVLENQ 157
Cdd:cd14091  74 ELLRGGELLDRILRQK--FFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNIlYADESgdpESLRICDFGFAKQLRAE 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 158 NDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMAT--LKHAFNAKDM-NSLVYRIVEGKLPQMPSKYD---PQ 231
Cdd:cd14091 152 NGLLMTPCYTANFVAPEVLKKQGYDAACDIWSLGVLLYTMLAgyTPFASGPNDTpEVILARIGSGKIDLSGGNWDhvsDS 231
                       250       260       270
                ....*....|....*....|....*....|
gi 41055987 232 LGELIKRMLCKKPEDRPDVKHILRQPYIKH 261
Cdd:cd14091 232 AKDLVRKMLHVDPSQRPTAAQVLQHPWIRN 261
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
8-256 2.38e-32

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: 127.24  E-value: 2.38e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKQYVIKKLnlRTSSRRERRAAEQEAQLLSQLK-HPNIVMY--------RESWEGEDcQLY 78
Cdd:cd14036   6 RVIAEGGFAFVYEAQDVGTGKEYALKRL--LSNEEEKNKAIIQEINFMKKLSgHPNIVQFcsaasigkEESDQGQA-EYL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  79 IVMGFCEGGdLYHRLKQ--QKGELLPErQVVEWFVQIAMALQYLHEKH--ILHRDLKTQNIFLTKTNIIKVGDLGIARVL 154
Cdd:cd14036  83 LLTELCKGQ-LVDFVKKveAPGPFSPD-TVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQIKLCDFGSATTE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 155 ---------ENQNDMASTLIG---TPYYMSPE---LFSNKPYNYKSDVWALGCCVYEMATLKHAFNakdmNSLVYRIVEG 219
Cdd:cd14036 161 ahypdyswsAQKRSLVEDEITrntTPMYRTPEmidLYSNYPIGEKQDIWALGCILYLLCFRKHPFE----DGAKLRIINA 236
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 41055987 220 K--LPQMPSKYDpQLGELIKRMLCKKPEDRPDVKHILRQ 256
Cdd:cd14036 237 KytIPPNDTQYT-VFHDLIRSTLKVNPEERLSITEIVEQ 274
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
4-278 2.51e-32

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: 127.53  E-value: 2.51e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRErraAEQEAQLLSQLKH-PNIVMY-----RESWEGEDCQL 77
Cdd:cd06637   8 FELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDVTGDEEEE---IKQEINMLKKYSHhRNIATYygafiKKNPPGMDDQL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  78 YIVMGFCEGGDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQ 157
Cdd:cd06637  85 WLVMEFCGAGSVTDLIKNTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 158 NDMASTLIGTPYYMSPELFS-----NKPYNYKSDVWALGCCVYEMAtlKHAFNAKDMNSL--VYRIVEGKLPQMPS-KYD 229
Cdd:cd06637 165 VGRRNTFIGTPYWMAPEVIAcdenpDATYDFKSDLWSLGITAIEMA--EGAPPLCDMHPMraLFLIPRNPAPRLKSkKWS 242
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 41055987 230 PQLGELIKRMLCKKPEDRPDVKHILRQPYIK-----HQISMFLEATKEKTAKSR 278
Cdd:cd06637 243 KKFQSFIESCLVKNHSQRPSTEQLMKHPFIRdqpneRQVRIQLKDHIDRTKKKR 296
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
6-257 3.68e-32

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: 126.38  E-value: 3.68e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   6 FVRV--VGKGSYGEVNLVRHKSDR-KQYVIKKLNLRTSSRRERRAAEQEAQLLSQLK---HPNIVMYRESWEGEDcQLYI 79
Cdd:cd14052   2 FANVelIGSGEFSQVYKVSERVPTgKVYAVKKLKPNYAGAKDRLRRLEEVSILRELTldgHDNIVQLIDSWEYHG-HLYI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  80 VMGFCEGGDLYHRLKQ--QKGELLPERqVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQ 157
Cdd:cd14052  81 QTELCENGSLDVFLSElgLLGRLDEFR-VWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMATVWPLI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 158 NDMasTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMAT------------------LKHAFNAKDMNSLVYRIVEG 219
Cdd:cd14052 160 RGI--EREGDREYIAPEILSEHMYDKPADIFSLGLILLEAAAnvvlpdngdawqklrsgdLSDAPRLSSTDLHSASSPSS 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 41055987 220 KLPQMPSKyDPQLGE----LIKRMLCKKPEDRPDVKHILRQP 257
Cdd:cd14052 238 NPPPDPPN-MPILSGsldrVVRWMLSPEPDRRPTADDVLATP 278
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
3-259 3.95e-32

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: 125.74  E-value: 3.95e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   3 GYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLN-LRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDCQLYIVM 81
Cdd:cd14164   1 GYTLGTTIGEGSFSKVKLATSQKYCCKVAIKIVDrRRASPDFVQKFLPRELSILRRVNHPNIVQMFECIEVANGRLYIVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  82 GFCEGgDLYHRLKQQKgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTN-IIKVGDLGIARVLENQNDM 160
Cdd:cd14164  81 EAAAT-DLLQKIQEVH--HIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDrKIKIADFGFARFVEDYPEL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 161 ASTLIGTPYYMSPELFSNKPYNYKS-DVWALGCCVYEMATLKHAFNAKDMNSLvyrivegKLPQMPSKYDPQLG------ 233
Cdd:cd14164 158 STTFCGSRAYTPPEVILGTPYDPKKyDVWSLGVVLYVMVTGTMPFDETNVRRL-------RLQQRGVLYPSGVAleepcr 230
                       250       260
                ....*....|....*....|....*.
gi 41055987 234 ELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd14164 231 ALIRTLLQFNPSTRPSIQQVAGNSWL 256
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
8-258 6.61e-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: 125.06  E-value: 6.61e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKQYVIKKLNlRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEgEDCQLYIVMGFCEGG 87
Cdd:cd14185   6 RTIGDGNFAVVKECRHWNENQEYAMKIID-KSKLKGKEDMIESEILIIKSLSHPNIVKLFEVYE-TEKEIYLILEYVRGG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  88 DLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLT----KTNIIKVGDLGIARVLENQndmAST 163
Cdd:cd14185  84 DLFDAIIESVK--FTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQhnpdKSTTLKLADFGLAKYVTGP---IFT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 164 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNS-LVYRIVE-GKLPQMPSKYD---PQLGELIKR 238
Cdd:cd14185 159 VCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRSPERDQeELFQIIQlGHYEFLPPYWDnisEAAKDLISR 238
                       250       260
                ....*....|....*....|
gi 41055987 239 MLCKKPEDRPDVKHILRQPY 258
Cdd:cd14185 239 LLVVDPEKRYTAKQVLQHPW 258
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
7-260 9.50e-32

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: 125.63  E-value: 9.50e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   7 VRVVGKGSYGEVNLVRHKSDRKqYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDCQLYIVMGFCEG 86
Cdd:cd06620  10 LKDLGAGNGGSVSKVLHIPTGT-IMAKKVIHIDAKSSVRKQILRELQILHECHSPYIVSFYGAFLNENNNIIICMEYMDC 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  87 GDLYHRLKqqKGELLPERQVVEWFVQIAMALQYLHEKH-ILHRDLKTQNIFLTKTNIIKVGDLGIARvlENQNDMASTLI 165
Cdd:cd06620  89 GSLDKILK--KKGPFPEEVLGKIAVAVLEGLTYLYNVHrIIHRDIKPSNILVNSKGQIKLCDFGVSG--ELINSIADTFV 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 166 GTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNS-----------LVYRIVEGKLPQMPSK--YDPQL 232
Cdd:cd06620 165 GTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFAGSNDDDdgyngpmgildLLQRIVNEPPPRLPKDriFPKDL 244
                       250       260
                ....*....|....*....|....*...
gi 41055987 233 GELIKRMLCKKPEDRPDVKHILRQPYIK 260
Cdd:cd06620 245 RDFVDRCLLKDPRERPSPQLLLDHDPFI 272
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
4-258 1.03e-31

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: 125.12  E-value: 1.03e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEV----NLVRHKsdrkqYVIKKLNLRTSSRRE------RRAAEQEAQLLSQLKHPNIVMYRESWEGE 73
Cdd:cd13990   2 YLLLNLLGKGGFSEVykafDLVEQR-----YVACKIHQLNKDWSEekkqnyIKHALREYEIHKSLDHPRIVKLYDVFEID 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  74 DCQLYIVMGFCEGGDLYHRLKQQKgeLLPERQVVEWFVQIAMALQYLHEKH--ILHRDLKTQNIFLTKTNI---IKVGDL 148
Cdd:cd13990  77 TDSFCTVLEYCDGNDLDFYLKQHK--SIPEREARSIIMQVVSALKYLNEIKppIIHYDLKPGNILLHSGNVsgeIKITDF 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 149 GIARVLENQNDMASTLI------GTPYYMSPELFSNKP----YNYKSDVWALGCCVYEMATLKHAFnAKDMNS---LVYR 215
Cdd:cd13990 155 GLSKIMDDESYNSDGMEltsqgaGTYWYLPPECFVVGKtppkISSKVDVWSVGVIFYQMLYGRKPF-GHNQSQeaiLEEN 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 41055987 216 -IVEGKLPQMPSKydPQLG----ELIKRMLCKKPEDRPDVKHILRQPY 258
Cdd:cd13990 234 tILKATEVEFPSK--PVVSseakDFIRRCLTYRKEDRPDVLQLANDPY 279
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
10-259 1.58e-31

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: 124.42  E-value: 1.58e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNL-RTSSRR--ERR-----AAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVM 81
Cdd:cd06629   9 IGKGTYGRVYLAMNATTGEMLAVKQVELpKTSSDRadSRQktvvdALKSEIDTLKDLDHPNIVQYLGFEETED-YFSIFL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  82 GFCEGGDLYHRLKQQKGEllpERQVVEWFV-QIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLEN--QN 158
Cdd:cd06629  88 EYVPGGSIGSCLRKYGKF---EEDLVRFFTrQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISKKSDDiyGN 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 159 DMASTLIGTPYYMSPELFSN--KPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIveGKLPQMPS-KYDPQLGEL 235
Cdd:cd06629 165 NGATSMQGSVFWMAPEVIHSqgQGYSAKVDIWSLGCVVLEMLAGRRPWSDDEAIAAMFKL--GNKRSAPPvPEDVNLSPE 242
                       250       260
                ....*....|....*....|....*...
gi 41055987 236 IKRMLCKK----PEDRPDVKHILRQPYI 259
Cdd:cd06629 243 ALDFLNACfaidPRDRPTAAELLSHPFL 270
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
4-258 1.95e-31

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: 124.25  E-value: 1.95e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRhKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKH-PNIV-MYreSWE--GEDCQLYI 79
Cdd:cd14131   3 YEILKQLGKGGSSKVYKVL-NPKKKIYALKRVDLEGADEQTLQSYKNEIELLKKLKGsDRIIqLY--DYEvtDEDDYLYM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  80 VMGFCEGgDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNiFLTKTNIIKVGDLGIARVLenQND 159
Cdd:cd14131  80 VMECGEI-DLATILKKKRPKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPAN-FLLVKGRLKLIDFGIAKAI--QND 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 160 MASTL----IGTPYYMSPELF---SNKPYN-------YKSDVWALGCCVYEMATLKHAF-NAKDMNSLVYRIVEGKLP-Q 223
Cdd:cd14131 156 TTSIVrdsqVGTLNYMSPEAIkdtSASGEGkpkskigRPSDVWSLGCILYQMVYGKTPFqHITNPIAKLQAIIDPNHEiE 235
                       250       260       270
                ....*....|....*....|....*....|....*
gi 41055987 224 MPSKYDPQLGELIKRMLCKKPEDRPDVKHILRQPY 258
Cdd:cd14131 236 FPDIPNPDLIDVMKRCLQRDPKKRPSIPELLNHPF 270
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
10-255 2.57e-31

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: 123.32  E-value: 2.57e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSdrKQYVIKKLNlrtsSRRERRAAEQEAQLLSQLKHPNIV-MYRESWEGEdcQLYIVMGFCEGGD 88
Cdd:cd14058   1 VGRGSFGVVCKARWRN--QIVAVKIIE----SESEKKAFEVEVRQLSRVDHPNIIkLYGACSNQK--PVCLVMEYAEGGS 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  89 LYHRLKQQKGelLPE---RQVVEWFVQIAMALQYLH---EKHILHRDLKTQNIFLT-KTNIIKVGDLGIArvLENQNDMA 161
Cdd:cd14058  73 LYNVLHGKEP--KPIytaAHAMSWALQCAKGVAYLHsmkPKALIHRDLKPPNLLLTnGGTVLKICDFGTA--CDISTHMT 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 162 STLiGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFnaKDMNSLVYRIV----EGKLPQMPSKYDPQLGELIK 237
Cdd:cd14058 149 NNK-GSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPF--DHIGGPAFRIMwavhNGERPPLIKNCPKPIESLMT 225
                       250
                ....*....|....*...
gi 41055987 238 RMLCKKPEDRPDVKHILR 255
Cdd:cd14058 226 RCWSKDPEKRPSMKEIVK 243
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
8-261 3.15e-31

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: 125.21  E-value: 3.15e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKQ---YVIKKLNLRTSSRRERRAAEQEAQ--LLSQLKHPNIV--MYRESWEGedcQLYIV 80
Cdd:cd05584   2 KVLGKGGYGKVFQVRKTTGSDKgkiFAMKVLKKASIVRNQKDTAHTKAErnILEAVKHPFIVdlHYAFQTGG---KLYLI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MGFCEGGDLYHRLkQQKGeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDM 160
Cdd:cd05584  79 LEYLSGGELFMHL-EREG-IFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLCKESIHDGTV 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 161 ASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLpQMPSKYDPQLGELIKRML 240
Cdd:cd05584 157 THTFCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGKL-NLPPYLTNEARDLLKKLL 235
                       250       260
                ....*....|....*....|....*.
gi 41055987 241 CKKPEDR-----PDVKHILRQPYIKH 261
Cdd:cd05584 236 KRNVSSRlgsgpGDAEEIKAHPFFRH 261
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
8-259 3.80e-31

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: 123.21  E-value: 3.80e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSR---RERRAAEQEAQLLSQLKHPNIVMYRESW-EGEDCQLYIVMGF 83
Cdd:cd06653   8 KLLGRGAFGEVYLCYDADTGRELAVKQVPFDPDSQetsKEVNALECEIQLLKNLRHDRIVQYYGCLrDPEEKKLSIFVEY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGGDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLEN---QNDM 160
Cdd:cd06653  88 MPGGSVKDQLKAYGA--LTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRIQTicmSGTG 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 161 ASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRI-VEGKLPQMPSKYDPQLGELIKRM 239
Cdd:cd06653 166 IKSVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPWAEYEAMAAIFKIaTQPTKPQLPDGVSDACRDFLRQI 245
                       250       260
                ....*....|....*....|
gi 41055987 240 LCKKpEDRPDVKHILRQPYI 259
Cdd:cd06653 246 FVEE-KRRPTAEFLLRHPFV 264
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
4-258 4.03e-31

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: 123.12  E-value: 4.03e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQY---VIKKLNLRTSSRRERRAAEQEAQllSQLKHPNIVMYRESWEGEDCqLYIV 80
Cdd:cd14187   9 YVRGRFLGKGGFAKCYEITDADTKEVFagkIVPKSLLLKPHQKEKMSMEIAIH--RSLAHQHVVGFHGFFEDNDF-VYVV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MGFCEGGDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDM 160
Cdd:cd14187  86 LELCRRRSLLELHKRRKA--LTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKVEYDGER 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 161 ASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLpQMPSKYDPQLGELIKRML 240
Cdd:cd14187 164 KKTLCGTPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEY-SIPKHINPVAASLIQKML 242
                       250
                ....*....|....*...
gi 41055987 241 CKKPEDRPDVKHILRQPY 258
Cdd:cd14187 243 QTDPTARPTINELLNDEF 260
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
9-247 4.84e-31

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: 124.22  E-value: 4.84e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   9 VVGKGSYGEVNLVRHKSDRKQYVIKKL-NLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEGG 87
Cdd:cd05585   1 VIGKGSFGKVMQVRKKDTSRIYALKTIrKAHIVSRSEVTHTLAERTVLAQVDCPFIVPLKFSFQSPE-KLYLVLAFINGG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  88 DLYHRLkQQKGELLPERQVVeWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLIGT 167
Cdd:cd05585  80 ELFHHL-QREGRFDLSRARF-YTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKLNMKDDDKTNTFCGT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 168 PYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLpQMPSKYDPQLGELIKRMLCKKPEDR 247
Cdd:cd05585 158 PEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPL-RFPDGFDRDAKDLLIGLLNRDPTKR 236
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
8-259 5.45e-31

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: 122.37  E-value: 5.45e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRkqyVIKKLNLRTSSRRERRAAE----QEAQLLSQLKHPNIV-MYreSWEGEDCQLYIVMG 82
Cdd:cd14116  11 RPLGKGKFGNVYLAREKQSK---FILALKVLFKAQLEKAGVEhqlrREVEIQSHLRHPNILrLY--GYFHDATRVYLILE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FCEGGDLYHRLkqQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIArvLENQNDMAS 162
Cdd:cd14116  86 YAPLGTVYREL--QKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWS--VHAPSSRRT 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 163 TLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRI--VEGKLPQMPSKydpQLGELIKRML 240
Cdd:cd14116 162 TLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRIsrVEFTFPDFVTE---GARDLISRLL 238
                       250
                ....*....|....*....
gi 41055987 241 CKKPEDRPDVKHILRQPYI 259
Cdd:cd14116 239 KHNPSQRPMLREVLEHPWI 257
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
8-258 6.19e-31

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: 123.15  E-value: 6.19e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGK---GSYGEVNLVRHKSDRKQYVIKKLNLRTSSrrerraAEQ-----EAQLLSQLK-HPNIVMYRES-WEGEDCQL 77
Cdd:cd07831   2 KILGKigeGTFSEVLKAQSRKTGKYYAIKCMKKHFKS------LEQvnnlrEIQALRRLSpHPNILRLIEVlFDRKTGRL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  78 YIVMGFCEGgDLYHRLKQQKgELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIfLTKTNIIKVGDLGIARVLeNQ 157
Cdd:cd07831  76 ALVFELMDM-NLYELIKGRK-RPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENI-LIKDDILKLADFGSCRGI-YS 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 158 NDMASTLIGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAF---NAKDMNSLVYRIV----------EGKLPQ 223
Cdd:cd07831 152 KPPYTEYISTRWYRAPEcLLTDGYYGPKMDIWAVGCVFFEILSLFPLFpgtNELDQIAKIHDVLgtpdaevlkkFRKSRH 231
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 41055987 224 MPSKYDPQLG---------------ELIKRMLCKKPEDRPDVKHILRQPY 258
Cdd:cd07831 232 MNYNFPSKKGtglrkllpnasaeglDLLKKLLAYDPDERITAKQALRHPY 281
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
8-247 6.26e-31

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: 124.35  E-value: 6.26e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAE-QEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEG 86
Cdd:cd05595   1 KLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTvTESRVLQNTRHPFLTALKYAFQTHD-RLCFVMEYANG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  87 GDLYHRLKQQKgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARvlENQNDMAS--TL 164
Cdd:cd05595  80 GELFFHLSRER--VFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCK--EGITDGATmkTF 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 165 IGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLpQMPSKYDPQLGELIKRMLCKKP 244
Cdd:cd05595 156 CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEI-RFPRTLSPEAKSLLAGLLKKDP 234

                ...
gi 41055987 245 EDR 247
Cdd:cd05595 235 KQR 237
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
49-259 6.41e-31

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: 122.28  E-value: 6.41e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  49 EQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEGGDLYHRLKQQKgELLPERQVVEWFVQIAMALQYLHEKHILHR 128
Cdd:cd14186  49 RNEVEIHCQLKHPSILELYNYFEDSN-YVYLVLEMCHNGEMSRYLKNRK-KPFTEDEARHFMHQIVTGMLYLHSHGILHR 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 129 DLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKD 208
Cdd:cd14186 127 DLTLSNLLLTRNMNIKIADFGLATQLKMPHEKHFTMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDT 206
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 41055987 209 MNSLVYRIVEGKLpQMPSKYDPQLGELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd14186 207 VKNTLNKVVLADY-EMPAFLSREAQDLIHQLLRKNPADRLSLSSVLDHPFM 256
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
8-259 7.91e-31

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK2 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK2 also activates ERK1/2, c-Jun N-terminal kinase (JNK) and p38 through their respective MAPKKs MEK1/2, JNK-activating kinase 2 (JNKK2), and MKK3/6. MEKK2 plays roles in T cell receptor signaling, immune synapse formation, cytokine gene expression, as well as in EGF and FGF receptor signaling. The MEKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 122.07  E-value: 7.91e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSS---RRERRAAEQEAQLLSQLKHPNIVMY----RESWEGedcQLYIV 80
Cdd:cd06652   8 KLLGQGAFGRVYLCYDADTGRELAVKQVQFDPESpetSKEVNALECEIQLLKNLLHERIVQYygclRDPQER---TLSIF 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MGFCEGGDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLEN---Q 157
Cdd:cd06652  85 MEYMPGGSIKDQLKSYGA--LTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGASKRLQTiclS 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 158 NDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRI-VEGKLPQMPSKYDPQLGELI 236
Cdd:cd06652 163 GTGMKSVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPWAEFEAMAAIFKIaTQPTNPQLPAHVSDHCRDFL 242
                       250       260
                ....*....|....*....|...
gi 41055987 237 KRMLCKKpEDRPDVKHILRQPYI 259
Cdd:cd06652 243 KRIFVEA-KLRPSADELLRHTFV 264
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
34-258 8.04e-31

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: 122.11  E-value: 8.04e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  34 KLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWE----GEDCqLYIVMGFCEGGDLYHRLKQQKgeLLPERQVVEW 109
Cdd:cd14032  33 ELQDRKLTKVERQRFKEEAEMLKGLQHPNIVRFYDFWEscakGKRC-IVLVTELMTSGTLKTYLKRFK--VMKPKVLRSW 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 110 FVQIAMALQYLHEKH--ILHRDLKTQNIFLT-KTNIIKVGDLGIARVleNQNDMASTLIGTPYYMSPELFSNKpYNYKSD 186
Cdd:cd14032 110 CRQILKGLLFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLATL--KRASFAKSVIGTPEFMAPEMYEEH-YDESVD 186
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41055987 187 VWALGCCVYEMATLKHAFNAKDMNSLVYRIVE-GKLPQMPSK-YDPQLGELIKRMLCKKPEDRPDVKHILRQPY 258
Cdd:cd14032 187 VYAFGMCMLEMATSEYPYSECQNAAQIYRKVTcGIKPASFEKvTDPEIKEIIGECICKNKEERYEIKDLLSHAF 260
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
4-259 8.17e-31

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: 122.21  E-value: 8.17e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDR-----KQYVIKkLNLRTSSRRERRAA--EQEAQLLSQLKHPNIVMYrESWEGEDCQ 76
Cdd:cd14076   3 YILGRTLGEGEFGKVKLGWPLPKAnhrsgVQVAIK-LIRRDTQQENCQTSkiMREINILKGLTHPNIVRL-LDVLKTKKY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  77 LYIVMGFCEGGDLYHRLkqQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVL-E 155
Cdd:cd14076  81 IGIVLEFVSGGELFDYI--LARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANTFdH 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 156 NQNDMASTLIGTPYYMSPELF-SNKPYN-YKSDVWALGCCVYEMATLKHAF-------NAKDMNSLVYRIVEGKLpQMPS 226
Cdd:cd14076 159 FNGDLMSTSCGSPCYAAPELVvSDSMYAgRKADIWSCGVILYAMLAGYLPFdddphnpNGDNVPRLYRYICNTPL-IFPE 237
                       250       260       270
                ....*....|....*....|....*....|...
gi 41055987 227 KYDPQLGELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd14076 238 YVTPKARDLLRRILVPNPRKRIRLSAIMRHAWL 270
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
4-221 8.52e-31

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


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 122.27  E-value: 8.52e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGF 83
Cdd:cd14097   3 YTFGRKLGQGSFGVVIEATHKETQTKWAIKKINREKAGSSAVKLLEREVDILKHVNHAHIIHLEEVFETPK-RMYLVMEL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGGDLyHRLKQQKGELlpERQVVEWFVQ-IAMALQYLHEKHILHRDLKTQNIFLTKTNI-------IKVGDLGIARVLE 155
Cdd:cd14097  82 CEDGEL-KELLLRKGFF--SENETRHIIQsLASAVAYLHKNDIVHRDLKLENILVKSSIIdnndklnIKVTDFGLSVQKY 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41055987 156 NQN-DMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKL 221
Cdd:cd14097 159 GLGeDMLQETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDL 225
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
10-258 1.02e-30

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: 121.65  E-value: 1.02e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWE----GEDCqLYIVMGFCE 85
Cdd:cd14033   9 IGRGSFKTVYRGLDTETTVEVAWCELQTRKLSKGERQRFSEEVEMLKGLQHPNIVRFYDSWKstvrGHKC-IILVTELMT 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  86 GGDL---YHRLKQQKGELLPerqvvEWFVQIAMALQYLHEKH--ILHRDLKTQNIFLT-KTNIIKVGDLGIARVleNQND 159
Cdd:cd14033  88 SGTLktyLKRFREMKLKLLQ-----RWSRQILKGLHFLHSRCppILHRDLKCDNIFITgPTGSVKIGDLGLATL--KRAS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 160 MASTLIGTPYYMSPELFSNKpYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYR-IVEGKLPQMPSKYD-PQLGELIK 237
Cdd:cd14033 161 FAKSVIGTPEFMAPEMYEEK-YDEAVDVYAFGMCILEMATSEYPYSECQNAAQIYRkVTSGIKPDSFYKVKvPELKEIIE 239
                       250       260
                ....*....|....*....|.
gi 41055987 238 RMLCKKPEDRPDVKHILRQPY 258
Cdd:cd14033 240 GCIRTDKDERFTIQDLLEHRF 260
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
4-258 1.23e-30

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


Pssm-ID: 271039 [Multi-domain]  Cd Length: 293  Bit Score: 122.61  E-value: 1.23e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKK--LNLRTSSRrerraaeqEAQLLSQLKHPNIV---MY---RESWEGEDC 75
Cdd:cd14137   6 YTIEKVIGSGSFGVVYQAKLLETGEVVAIKKvlQDKRYKNR--------ELQIMRRLKHPNIVklkYFfysSGEKKDEVY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  76 qLYIVMGFCEGgDLYHRLKQ--QKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFL-TKTNIIKVGDLGIAR 152
Cdd:cd14137  78 -LNLVMEYMPE-TLYRVIRHysKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVdPETGVLKLCDFGSAK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 153 VLeNQNDMASTLIGTPYYMSPEL-FSNKPYNYKSDVWALGCCVYEMATLKHAFNA----------------------KDM 209
Cdd:cd14137 156 RL-VPGEPNVSYICSRYYRAPELiFGATDYTTAIDIWSAGCVLAELLLGQPLFPGessvdqlveiikvlgtptreqiKAM 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 41055987 210 NSLVYRIvegKLPQ---------MPSKYDPQLGELIKRMLCKKPEDRPDVKHILRQPY 258
Cdd:cd14137 235 NPNYTEF---KFPQikphpwekvFPKRTPPDAIDLLSKILVYNPSKRLTALEALAHPF 289
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
10-254 1.24e-30

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: 122.23  E-value: 1.24e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESW-EGEDCQLYIVMGFCEGGD 88
Cdd:cd14049  14 LGKGGYGKVYKVRNKLDGQYYAIKKILIKKVTKRDCMKVLREVKVLAGLQHPNIVGYHTAWmEHVQLMLYIQMQLCELSL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  89 ---LYHRLKQQKGELLPER----QVVEW----FVQIAMALQYLHEKHILHRDLKTQNIFLTKTNI-IKVGDLGIA--RVL 154
Cdd:cd14049  94 wdwIVERNKRPCEEEFKSApytpVDVDVttkiLQQLLEGVTYIHSMGIVHRDLKPRNIFLHGSDIhVRIGDFGLAcpDIL 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 155 ENQNDMASTL----------IGTPYYMSPELFSNKPYNYKSDVWALGCCVYEmatLKHAFNAkDMN--SLVYRIVEGKLP 222
Cdd:cd14049 174 QDGNDSTTMSrlnglthtsgVGTCLYAAPEQLEGSHYDFKSDMYSIGVILLE---LFQPFGT-EMEraEVLTQLRNGQIP 249
                       250       260       270
                ....*....|....*....|....*....|..
gi 41055987 223 QMPSKYDPQLGELIKRMLCKKPEDRPDVKHIL 254
Cdd:cd14049 250 KSLCKRWPVQAKYIKLLTSTEPSERPSASQLL 281
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
2-260 1.24e-30

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: 122.65  E-value: 1.24e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNL---RTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEgEDCQLY 78
Cdd:cd14094   3 DVYELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVakfTSSPGLSTEDLKREASICHMLKHPHIVELLETYS-SDGMLY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  79 IVMGFCEGGDLYHRLKQQ--KGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNI---IKVGDLGIARV 153
Cdd:cd14094  82 MVFEFMDGADLCFEIVKRadAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQ 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 154 LENQNDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNsLVYRIVEGKLPQMPSKYD---P 230
Cdd:cd14094 162 LGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKER-LFEGIIKGKYKMNPRQWShisE 240
                       250       260       270
                ....*....|....*....|....*....|
gi 41055987 231 QLGELIKRMLCKKPEDRPDVKHILRQPYIK 260
Cdd:cd14094 241 SAKDLVRRMLMLDPAERITVYEALNHPWIK 270
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
8-247 1.27e-30

Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the GRK4-like group include GRK4, GRK5, GRK6, and similar GRKs. They contain an N-terminal RGS homology (RH) domain and a catalytic domain, but lack a G protein betagamma-subunit binding domain. They are localized to the plasma membrane through post-translational lipid modification or direct binding to PIP2. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 122.08  E-value: 1.27e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKQYVIKKL-NLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDCqLYIVMGFCEG 86
Cdd:cd05605   6 RVLGKGGFGEVCACQVRATGKMYACKKLeKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDA-LCLVLTIMNG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  87 GDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENqNDMASTLIG 166
Cdd:cd05605  85 GDLKFHIYNMGNPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVEIPE-GETIRGRVG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 167 TPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNA---KDMNSLVYRIVEGKLPQMPSKYDPQLGELIKRMLCKK 243
Cdd:cd05605 164 TVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRArkeKVKREEVDRRVKEDQEEYSEKFSEEAKSICSQLLQKD 243

                ....
gi 41055987 244 PEDR 247
Cdd:cd05605 244 PKTR 247
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
4-260 1.30e-30

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: 121.57  E-value: 1.30e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRErrAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGF 83
Cdd:cd06647   9 YTRFEKIGQGASGTVYTAIDVATGQEVAIKQMNLQQQPKKE--LIINEILVMRENKNPNIVNYLDSYLVGD-ELWVVMEY 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGGDLYHRLKQQkgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMAST 163
Cdd:cd06647  86 LAGGSLTDVVTET---CMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRST 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 164 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQM--PSKYDPQLGELIKRMLC 241
Cdd:cd06647 163 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELqnPEKLSAIFRDFLNRCLE 242
                       250
                ....*....|....*....
gi 41055987 242 KKPEDRPDVKHILRQPYIK 260
Cdd:cd06647 243 MDVEKRGSAKELLQHPFLK 261
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
10-259 1.36e-30

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: 121.66  E-value: 1.36e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLR--TSSRR--ERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCE 85
Cdd:cd14194  13 LGSGQFAVVKKCREKSTGLQYAAKFIKKRrtKSSRRgvSREDIEREVSILKEIQHPNVITLHEVYENKT-DVILILELVA 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  86 GGDLYHRLKQQkgELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNI----IKVGDLGIARVLENQNDMA 161
Cdd:cd14194  92 GGELFDFLAEK--ESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVpkprIKIIDFGLAHKIDFGNEFK 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 162 StLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAF-------NAKDMNSLVYRIVEgklpQMPSKYDPQLGE 234
Cdd:cd14194 170 N-IFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFlgdtkqeTLANVSAVNYEFED----EYFSNTSALAKD 244
                       250       260
                ....*....|....*....|....*
gi 41055987 235 LIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd14194 245 FIRRLLVKDPKKRMTIQDSLQHPWI 269
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
2-260 1.81e-30

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: 123.17  E-value: 1.81e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIV----MYRESWEGEDCQ- 76
Cdd:cd07851  15 DRYQNLSPVGSGAYGQVCSAFDTKTGRKVAIKKLSRPFQSAIHAKRTYRELRLLKHMKHENVIglldVFTPASSLEDFQd 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  77 LYIVMGFCeGGDLYHRLKQQKgelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLEn 156
Cdd:cd07851  95 VYLVTHLM-GADLNNIVKCQK---LSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLARHTD- 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 157 qNDMaSTLIGTPYYMSPELFSNK-PYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVE----------------- 218
Cdd:cd07851 170 -DEM-TGYVATRWYRAPEIMLNWmHYNQTVDIWSVGCIMAELLTGKTLFPGSDHIDQLKRIMNlvgtpdeellkkisses 247
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 41055987 219 -----GKLPQMPSK--------YDPQLGELIKRMLCKKPEDRPDVKHILRQPYIK 260
Cdd:cd07851 248 arnyiQSLPQMPKKdfkevfsgANPLAIDLLEKMLVLDPDKRITAAEALAHPYLA 302
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
10-254 1.96e-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: 120.58  E-value: 1.96e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDrkqYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYReSWEGEDcQLYIVMGFCEGGDL 89
Cdd:cd14062   1 IGSGSFGTVYKGRWHGD---VAVKKLNVTDPTPSQLQAFKNEVAVLRKTRHVNILLFM-GYMTKP-QLAIVTQWCEGSSL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  90 YHRLKQQ--KGELLperQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARV--LENQNDMASTLI 165
Cdd:cd14062  76 YKHLHVLetKFEML---QLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLATVktRWSGSQQFEQPT 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 166 GTPYYMSPELFSNK---PYNYKSDVWALGCCVYEMATLK---HAFNAKDMnsLVYRIVEGKL-PQMpSKYDPQLGELIKR 238
Cdd:cd14062 153 GSILWMAPEVIRMQdenPYSFQSDVYAFGIVLYELLTGQlpySHINNRDQ--ILFMVGRGYLrPDL-SKVRSDTPKALRR 229
                       250       260
                ....*....|....*....|
gi 41055987 239 ML--C--KKPEDRPDVKHIL 254
Cdd:cd14062 230 LMedCikFQRDERPLFPQIL 249
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
10-258 2.03e-30

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: 121.90  E-value: 2.03e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLnlRTSSRRE--RRAAEQEAQLLSQLKHPNIVMYRE---SWEGEDCQ--LYIVMG 82
Cdd:cd07840   7 IGEGTYGQVYKARNKKTGELVALKKI--RMENEKEgfPITAIREIKLLQKLDHPNVVRLKEivtSKGSAKYKgsIYMVFE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FCEGgDLyHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMAS 162
Cdd:cd07840  85 YMDH-DL-TGLLDNPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLARPYTKENNADY 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 163 T--LIgTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVE------------------GKL 221
Cdd:cd07840 163 TnrVI-TLWYRPPElLLGATRYGPEVDMWSVGCILAELFTGKPIFQGKTELEQLEKIFElcgspteenwpgvsdlpwFEN 241
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 41055987 222 PQMPSKY------------DPQLGELIKRMLCKKPEDRPDVKHILRQPY 258
Cdd:cd07840 242 LKPKKPYkrrlrevfknviDPSALDLLDKLLTLDPKKRISADQALQHEY 290
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
2-258 2.04e-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: 120.94  E-value: 2.04e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERrAAEQEAQLLSQLKHPNIVMYRESWEGEDCqLYIVM 81
Cdd:cd14083   3 DKYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKALKGKED-SLENEIAVLRKIKHPNIVQLLDIYESKSH-LYLVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  82 GFCEGGDLYHRLkQQKGELlPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIF---LTKTNIIKVGDLGIARVlENQN 158
Cdd:cd14083  81 ELVTGGELFDRI-VEKGSY-TEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLyysPDEDSKIMISDFGLSKM-EDSG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 159 DMaSTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLpQMPSKYDPQLGE---- 234
Cdd:cd14083 158 VM-STACGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILKAEY-EFDSPYWDDISDsakd 235
                       250       260
                ....*....|....*....|....
gi 41055987 235 LIKRMLCKKPEDRPDVKHILRQPY 258
Cdd:cd14083 236 FIRHLMEKDPNKRYTCEQALEHPW 259
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
10-196 2.59e-30

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKalpha is involved in the non-canonical or alternative pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The non-canonical pathway functions in cells lacking NEMO (NF-kB Essential MOdulator) and IKKbeta. It is induced by a subset of TNFR family members including CD40, RANK, and B cell-activating factor receptor. IKKalpha processes the Inhibitor of NF-kB (IkB)-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus. This pathway is dependent on NIK (NF-kB Inducing Kinase) which phosphorylates and activates IKKalpha. The IKKalpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 121.56  E-value: 2.59e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAeQEAQLLSQLKHPNIVMYRESWEGEDCQL----YIVMGFCE 85
Cdd:cd14039   1 LGTGGFGNVCLYQNQETGEKIAIKSCRLELSVKNKDRWC-HEIQIMKKLNHPNVVKACDVPEEMNFLVndvpLLAMEYCS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  86 GGDLYHRL-KQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTN---IIKVGDLGIARVLEnQNDMA 161
Cdd:cd14039  80 GGDLRKLLnKPENCCGLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINgkiVHKIIDLGYAKDLD-QGSLC 158
                       170       180       190
                ....*....|....*....|....*....|....*
gi 41055987 162 STLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYE 196
Cdd:cd14039 159 TSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFE 193
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
10-260 2.88e-30

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: 120.66  E-value: 2.88e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKL--------NLRTSSRRERraaeqeAQLLSQLKHPNIVMYRESWEGEDcQLYIVM 81
Cdd:cd05611   4 ISKGAFGSVYLAKKRSTGDYFAIKVLkksdmiakNQVTNVKAER------AIMMIQGESPYVAKLYYSFQSKD-YLYLVM 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  82 GFCEGGDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLEnQNDMA 161
Cdd:cd05611  77 EYLNGGDCASLIKTLGG--LPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSRNGL-EKRHN 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 162 STLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLpQMPSKYD----PQLGELIK 237
Cdd:cd05611 154 KKFVGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRRI-NWPEEVKefcsPEAVDLIN 232
                       250       260
                ....*....|....*....|....*.
gi 41055987 238 RMLCKKPEDR---PDVKHILRQPYIK 260
Cdd:cd05611 233 RLLCMDPAKRlgaNGYQEIKSHPFFK 258
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
10-260 4.65e-30

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: 120.91  E-value: 4.65e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRErrAAEQEAQLLSQLKHPNIV-MYRESWEGEdcQLYIVMGFCEGGD 88
Cdd:cd06658  30 IGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQRRE--LLFNEVVIMRDYHHENVVdMYNSYLVGD--ELWVVMEFLEGGA 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  89 LYHRLKQQKgelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLIGTP 168
Cdd:cd06658 106 LTDIVTHTR---MNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQVSKEVPKRKSLVGTP 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 169 YYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPS--KYDPQLGELIKRMLCKKPED 246
Cdd:cd06658 183 YWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRDNLPPRVKDshKVSSVLRGFLDLMLVREPSQ 262
                       250
                ....*....|....
gi 41055987 247 RPDVKHILRQPYIK 260
Cdd:cd06658 263 RATAQELLQHPFLK 276
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
10-259 5.43e-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: 120.16  E-value: 5.43e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRE---RRAAE------------------QEAQLLSQLKHPNIVMYRE 68
Cdd:cd14118   2 IGKGSYGIVKLAYNEEDNTLYAMKILSKKKLLKQAgffRRPPPrrkpgalgkpldpldrvyREIAILKKLDHPNVVKLVE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  69 SWE--GEDcQLYIVMGFCEGGDLyhrLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVG 146
Cdd:cd14118  82 VLDdpNED-NLYMVFELVDKGAV---MEVPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 147 DLGIARVLENQNDMASTLIGTPYYMSPELFSNKPYNYKS---DVWALGCCVYEMATLKHAFNAKDMNSLVYRIV--EGKL 221
Cdd:cd14118 158 DFGVSNEFEGDDALLSSTAGTPAFMAPEALSESRKKFSGkalDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIKtdPVVF 237
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 41055987 222 PQMPsKYDPQLGELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd14118 238 PDDP-VVSEQLKDLILRMLDKNPSERITLPEIKEHPWV 274
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
8-258 6.61e-30

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


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 119.32  E-value: 6.61e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQllsqlkHPNIV----MYRESWEGEDCqLYIVMGF 83
Cdd:cd14089   7 QVLGLGINGKVLECFHKKTGEKFALKVLRDNPKARREVELHWRASG------CPHIVriidVYENTYQGRKC-LLVVMEC 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGGDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTN---IIKVGDLGIARVLENQNDM 160
Cdd:cd14089  80 MEGGELFSRIQERADSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGpnaILKLTDFGFAKETTTKKSL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 161 AsTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMA-------TLKHAFNAKDMNSlvyRIVEGKLpQMP----SKYD 229
Cdd:cd14089 160 Q-TPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLcgyppfySNHGLAISPGMKK---RIRNGQY-EFPnpewSNVS 234
                       250       260
                ....*....|....*....|....*....
gi 41055987 230 PQLGELIKRMLCKKPEDRPDVKHILRQPY 258
Cdd:cd14089 235 EEAKDLIRGLLKTDPSERLTIEEVMNHPW 263
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
3-258 7.69e-30

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: 118.91  E-value: 7.69e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   3 GYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLR--TSSRRERRAaEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIV 80
Cdd:cd14079   3 NYILGKTLGVGSFGKVKLAEHELTGHKVAVKILNRQkiKSLDMEEKI-RREIQILKLFRHPHIIRLYEVIETPT-DIFMV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MGFCEGGDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENqNDM 160
Cdd:cd14079  81 MEYVSGGELFDYIVQKGR--LSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLSNIMRD-GEF 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 161 ASTLIGTPYYMSPELFSNKPY-NYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPqMPSKYDPQLGELIKRM 239
Cdd:cd14079 158 LKTSCGSPNYAAPEVISGKLYaGPEVDVWSCGVILYALLCGSLPFDDEHIPNLFKKIKSGIYT-IPSHLSPGARDLIKRM 236
                       250
                ....*....|....*....
gi 41055987 240 LCKKPEDRPDVKHILRQPY 258
Cdd:cd14079 237 LVVDPLKRITIPEIRQHPW 255
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
34-258 8.35e-30

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: 119.44  E-value: 8.35e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  34 KLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWE----GEDCqLYIVMGFCEGGDLYHRLKQQKgeLLPERQVVEW 109
Cdd:cd14031  42 ELQDRKLTKAEQQRFKEEAEMLKGLQHPNIVRFYDSWEsvlkGKKC-IVLVTELMTSGTLKTYLKRFK--VMKPKVLRSW 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 110 FVQIAMALQYLHEKH--ILHRDLKTQNIFLT-KTNIIKVGDLGIARVLenQNDMASTLIGTPYYMSPELFSNKpYNYKSD 186
Cdd:cd14031 119 CRQILKGLQFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLATLM--RTSFAKSVIGTPEFMAPEMYEEH-YDESVD 195
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41055987 187 VWALGCCVYEMATLKHAFNAKDMNSLVYR-IVEGKLPQMPSKY-DPQLGELIKRMLCKKPEDRPDVKHILRQPY 258
Cdd:cd14031 196 VYAFGMCMLEMATSEYPYSECQNAAQIYRkVTSGIKPASFNKVtDPEVKEIIEGCIRQNKSERLSIKDLLNHAF 269
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
10-278 1.17e-29

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: 119.83  E-value: 1.17e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRErrAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEGGDL 89
Cdd:cd06655  27 IGQGASGTVFTAIDVATGQEVAIKQINLQKQPKKE--LIINEILVMKELKNPNIVNFLDSFLVGD-ELFVVMEYLAGGSL 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  90 YHRLKQQkgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLIGTPY 169
Cdd:cd06655 104 TDVVTET---CMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPY 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 170 YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQM--PSKYDPQLGELIKRMLCKKPEDR 247
Cdd:cd06655 181 WMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELqnPEKLSPIFRDFLNRCLEMDVEKR 260
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 41055987 248 PDVKHILRQPYIK-----HQISMFLEATKEKTAKSR 278
Cdd:cd06655 261 GSAKELLQHPFLKlakplSSLTPLILAAKEAMKSNR 296
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
10-199 1.19e-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: 119.40  E-value: 1.19e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLnlrTSSRRE---RRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEG 86
Cdd:cd07847   9 IGEGSYGVVFKCRNRETGQIVAIKKF---VESEDDpviKKIALREIRMLKQLKHPNLVNLIEVFRRKR-KLHLVFEYCDH 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  87 GDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLIG 166
Cdd:cd07847  85 TVLNELEKNPRG--VPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARILTGPGDDYTDYVA 162
                       170       180       190
                ....*....|....*....|....*....|....
gi 41055987 167 TPYYMSPELF-SNKPYNYKSDVWALGCCVYEMAT 199
Cdd:cd07847 163 TRWYRAPELLvGDTQYGPPVDVWAIGCVFAELLT 196
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
10-262 1.31e-29

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: 120.14  E-value: 1.31e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRER-RAAEQEAQLLSQLKHPNIVMYRESWEGEDCQlYIVMGFCEGG- 87
Cdd:cd06633  29 IGHGSFGAVYFATNSHTNEVVAIKKMSYSGKQTNEKwQDIIKEVKFLQQLKHPNTIEYKGCYLKDHTA-WLVMEYCLGSa 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  88 -DLYHRLKQQkgelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNdmasTLIG 166
Cdd:cd06633 108 sDLLEVHKKP----LQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIASPAN----SFVG 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 167 TPYYMSPEL---FSNKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLvYRIVEGKLPQMPS-KYDPQLGELIKRMLC 241
Cdd:cd06633 180 TPYWMAPEVilaMDEGQYDGKVDIWSLGITCIELAERKPPlFNMNAMSAL-YHIAQNDSPTLQSnEWTDSFRGFVDYCLQ 258
                       250       260
                ....*....|....*....|.
gi 41055987 242 KKPEDRPDVKHILRQPYIKHQ 262
Cdd:cd06633 259 KIPQERPSSAELLRHDFVRRE 279
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
8-258 1.34e-29

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


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 120.15  E-value: 1.34e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAE-QEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEG 86
Cdd:cd05571   1 KVLGKGTFGKVILCREKATGELYAIKILKKEVIIAKDEVAHTlTENRVLQNTRHPFLTSLKYSFQTND-RLCFVMEYVNG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  87 GDLYHRLKQQKgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLIG 166
Cdd:cd05571  80 GELFFHLSRER--VFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCKEEISYGATTKTFCG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 167 TPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLpQMPSKYDPQLGELIKRMLCKKPED 246
Cdd:cd05571 158 TPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEV-RFPSTLSPEAKSLLAGLLKKDPKK 236
                       250
                ....*....|....*..
gi 41055987 247 R-----PDVKHILRQPY 258
Cdd:cd05571 237 RlgggpRDAKEIMEHPF 253
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
8-253 2.48e-29

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: 117.91  E-value: 2.48e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVN---LVRHKSDRKQYVIK--KLNLrTSSRRERRAaeQEAQLLSQLKHPNIVmyRESWEGEDCQLYIVMG 82
Cdd:cd05056  12 RCIGEGQFGDVYqgvYMSPENEKIAVAVKtcKNCT-SPSVREKFL--QEAYIMRQFDHPHIV--KLIGVITENPVWIVME 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FCEGGDLYHRLKQQKgELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMAS 162
Cdd:cd05056  87 LAPLGELRSYLQVNK-YSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSRYMEDESYYKA 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 163 TLIGTPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATL-KHAFNAKDMNSLVYRIVEGKLPQMPSKYDPQLGELIKRML 240
Cdd:cd05056 166 SKGKLPIkWMAPESINFRRFTSASDVWMFGVCMWEILMLgVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCW 245
                       250
                ....*....|...
gi 41055987 241 CKKPEDRPDVKHI 253
Cdd:cd05056 246 AYDPSKRPRFTEL 258
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
2-247 2.65e-29

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: 118.45  E-value: 2.65e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNL-RTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEdCQLYIV 80
Cdd:cd05608   1 DWFLDFRVLGKGGFGEVSACQMRATGKLYACKKLNKkRLKKRKGYEGAMVEKRILAKVHSRFIVSLAYAFQTK-TDLCLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MGFCEGGDL-YHRLK-QQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQN 158
Cdd:cd05608  80 MTIMNGGDLrYHIYNvDEENPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVELKDGQ 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 159 DMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAK----DMNSLVYRIVEGKLpQMPSKYDPQLGE 234
Cdd:cd05608 160 TKTKGYAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFRARgekvENKELKQRILNDSV-TYSEKFSPASKS 238
                       250
                ....*....|...
gi 41055987 235 LIKRMLCKKPEDR 247
Cdd:cd05608 239 ICEALLAKDPEKR 251
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
2-259 2.94e-29

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: 117.97  E-value: 2.94e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLFVRVVGKGSYGEVNLVRHKSDRKQYV---IKKLNLRtSSRR--ERRAAEQEAQLLSQLKHPNIVMYRESWEGEdCQ 76
Cdd:cd14105   5 DFYDIGEELGSGQFAVVKKCREKSTGLEYAakfIKKRRSK-ASRRgvSREDIEREVSILRQVLHPNIITLHDVFENK-TD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  77 LYIVMGFCEGGDLYHRLKQQkgELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNI----IKVGDLGIAR 152
Cdd:cd14105  83 VVLILELVAGGELFDFLAEK--ESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNVpiprIKLIDFGLAH 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 153 VLENQNDMAStLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLpQMPSKYDPQL 232
Cdd:cd14105 161 KIEDGNEFKN-IFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVNY-DFDDEYFSNT 238
                       250       260       270
                ....*....|....*....|....*....|.
gi 41055987 233 GEL----IKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd14105 239 SELakdfIRQLLVKDPRKRMTIQESLRHPWI 269
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
2-259 3.77e-29

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: 117.80  E-value: 3.77e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRErraAEQEAQLLSQLK-HPNIVMYRESWEGEDC----Q 76
Cdd:cd06638  18 DTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDPIHDIDEE---IEAEYNILKALSdHPNVVKFYGMYYKKDVkngdQ 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  77 LYIVMGFCEGGDLYHRLKQ--QKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVL 154
Cdd:cd06638  95 LWLVLELCNGGSVTDLVKGflKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQL 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 155 ENQNDMASTLIGTPYYMSPELFS-----NKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLP--QMPSK 227
Cdd:cd06638 175 TSTRLRRNTSVGTPFWMAPEVIAceqqlDSTYDARCDVWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPtlHQPEL 254
                       250       260       270
                ....*....|....*....|....*....|..
gi 41055987 228 YDPQLGELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd06638 255 WSNEFNDFIRKCLTKDYEKRPTVSDLLQHVFI 286
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
3-259 4.89e-29

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: 116.63  E-value: 4.89e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   3 GYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRE-RRAAEQEAQLLSQLKHPNIVMYRESWEGEDCQLYIVM 81
Cdd:cd14163   1 GYQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIIDKSGGPEEFiQRFLPRELQIVERLDHKNIIHVYEMLESADGKIYLVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  82 GFCEGGDLYHRLKQqkGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNiIKVGDLGIARVL-ENQNDM 160
Cdd:cd14163  81 ELAEDGDVFDCVLH--GGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGFT-LKLTDFGFAKQLpKGGREL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 161 ASTLIGTPYYMSPELFSNKPYNY-KSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEG-KLP-QMPSKYDPQlgELIK 237
Cdd:cd14163 158 SQTFCGSTAYAAPEVLQGVPHDSrKGDIWSMGVVLYVMLCAQLPFDDTDIPKMLCQQQKGvSLPgHLGVSRTCQ--DLLK 235
                       250       260
                ....*....|....*....|..
gi 41055987 238 RMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd14163 236 RLLEPDMVLRPSIEEVSWHPWL 257
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
8-262 4.94e-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: 4.94e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRT--------SSRRERRAaeqeaqLLSQLKHPNIVMYRESWEGEDcQLYI 79
Cdd:cd05592   1 KVLGKGSFGKVMLAELKGTNQYFAIKALKKDVvledddveCTMIERRV------LALASQHPFLTHLFCTFQTES-HLFF 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  80 VMGFCEGGDLYHRLkQQKGELLPERQVVeWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQND 159
Cdd:cd05592  74 VMEYLNGGDLMFHI-QQSGRFDEDRARF-YGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCKENIYGEN 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 160 MASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKlPQMPSKYDPQLGELIKRM 239
Cdd:cd05592 152 KASTFCGTPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICNDT-PHYPRWLTKEAASCLSLL 230
                       250       260
                ....*....|....*....|...
gi 41055987 240 LCKKPEDRPDVKHILRQPYIKHQ 262
Cdd:cd05592 231 LERNPEKRLGVPECPAGDIRDHP 253
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
10-259 5.06e-29

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: 117.82  E-value: 5.06e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRErrAAEQEAQLLSQLKHPNIV-MYRESWEGEdcQLYIVMGFCEGGD 88
Cdd:cd06657  28 IGEGSTGIVCIATVKSSGKLVAVKKMDLRKQQRRE--LLFNEVVIMRDYQHENVVeMYNSYLVGD--ELWVVMEFLEGGA 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  89 LYHRLKQQKgelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLIGTP 168
Cdd:cd06657 104 LTDIVTHTR---MNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTP 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 169 YYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLvyRIVEGKLP---QMPSKYDPQLGELIKRMLCKKP 244
Cdd:cd06657 181 YWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPyFNEPPLKAM--KMIRDNLPpklKNLHKVSPSLKGFLDRLLVRDP 258
                       250
                ....*....|....*
gi 41055987 245 EDRPDVKHILRQPYI 259
Cdd:cd06657 259 AQRATAAELLKHPFL 273
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
4-259 5.09e-29

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: 116.74  E-value: 5.09e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQY---VIKKLNLRTSSRRErraAEQEAQLLSQLKHPNIVMYRESWEGEdCQLYIV 80
Cdd:cd14074   5 YDLEETLGRGHFAVVKLARHVFTGEKVavkVIDKTKLDDVSKAH---LFQEVRCMKLVQHPNVVRLYEVIDTQ-TKLYLI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MGFCEGGDLY-HRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQN-IFLTKTNIIKVGDLGIARVLEnQN 158
Cdd:cd14074  81 LELGDGGDMYdYIMKHENG--LNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENvVFFEKQGLVKLTDFGFSNKFQ-PG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 159 DMASTLIGTPYYMSPELFSNKPYNY-KSDVWALGCCVYEMATLKHAFN-AKDMNSLVyRIVEGKLpQMPSKYDPQLGELI 236
Cdd:cd14074 158 EKLETSCGSLAYSAPEILLGDEYDApAVDIWSLGVILYMLVCGQPPFQeANDSETLT-MIMDCKY-TVPAHVSPECKDLI 235
                       250       260
                ....*....|....*....|...
gi 41055987 237 KRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd14074 236 RRMLIRDPKKRASLEEIENHPWL 258
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
2-260 5.37e-29

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: 117.53  E-value: 5.37e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRaaeqeaqLLSQLK-------HPNIV-----MYRES 69
Cdd:cd06617   1 DDLEVIEELGRGAYGVVDKMRHVPTGTIMAVKRIRATVNSQEQKR-------LLMDLDismrsvdCPYTVtfygaLFREG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  70 wegedcQLYIVMGFCEGG-DLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEK-HILHRDLKTQNIFLTKTNIIKVGD 147
Cdd:cd06617  74 ------DVWICMEVMDTSlDKFYKKVYDKGLTIPEDILGKIAVSIVKALEYLHSKlSVIHRDVKPSNVLINRNGQVKLCD 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 148 LGIARVLenQNDMASTL-IGTPYYMSPELF----SNKPYNYKSDVWALGCCVYEMATLKHAF-NAKDMNSLVYRIVEGKL 221
Cdd:cd06617 148 FGISGYL--VDSVAKTIdAGCKPYMAPERInpelNQKGYDVKSDVWSLGITMIELATGRFPYdSWKTPFQQLKQVVEEPS 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 41055987 222 PQMPS-KYDPQLGELIKRMLCKKPEDRPDVKHILRQPYIK 260
Cdd:cd06617 226 PQLPAeKFSPEFQDFVNKCLKKNYKERPNYPELLQHPFFE 265
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
10-195 6.94e-29

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: 116.17  E-value: 6.94e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLnlRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEGGDL 89
Cdd:cd14103   1 LGRGKFGTVYRCVEKATGKELAAKFI--KCRKAKDREDVRNEIEIMNQLRHPRLLQLYDAFETPR-EMVLVMEYVAGGEL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  90 YHRLKQQKGELlPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIF-LTKT-NIIKVGDLGIARVLeNQNDMASTLIGT 167
Cdd:cd14103  78 FERVVDDDFEL-TERDCILFMRQICEGVQYMHKQGILHLDLKPENILcVSRTgNQIKIIDFGLARKY-DPDKKLKVLFGT 155
                       170       180
                ....*....|....*....|....*...
gi 41055987 168 PYYMSPELFSNKPYNYKSDVWALGCCVY 195
Cdd:cd14103 156 PEFVAPEVVNYEPISYATDMWSVGVICY 183
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
10-259 7.08e-29

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: 117.10  E-value: 7.08e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRtSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEgEDCQLYIVMGFCEGGDL 89
Cdd:cd06641  12 IGKGSFGEVFKGIDNRTQKVVAIKIIDLE-EAEDEIEDIQQEITVLSQCDSPYVTKYYGSYL-KDTKLWIIMEYLGGGSA 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  90 YHRLKQQKgelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLIGTPY 169
Cdd:cd06641  90 LDLLEPGP---LDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIKRN*FVGTPF 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 170 YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPSKYDPQLGELIKRMLCKKPEDRPD 249
Cdd:cd06641 167 WMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIPKNNPPTLEGNYSKPLKEFVEACLNKEPSFRPT 246
                       250
                ....*....|
gi 41055987 250 VKHILRQPYI 259
Cdd:cd06641 247 AKELLKHKFI 256
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
1-258 7.86e-29

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: 118.64  E-value: 7.86e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   1 MDGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAE-QEAQLLSQLKHPNIVMYRESWEGEDcQLYI 79
Cdd:cd05593  14 MNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTlTESRVLKNTRHPFLTSLKYSFQTKD-RLCF 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  80 VMGFCEGGDLYHRLKQQKgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARvlENQND 159
Cdd:cd05593  93 VMEYVNGGELFFHLSRER--VFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCK--EGITD 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 160 MAS--TLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLpQMPSKYDPQLGELIK 237
Cdd:cd05593 169 AATmkTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDI-KFPRTLSADAKSLLS 247
                       250       260
                ....*....|....*....|....*.
gi 41055987 238 RMLCKKPEDR-----PDVKHILRQPY 258
Cdd:cd05593 248 GLLIKDPNKRlgggpDDAKEIMRHSF 273
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
9-256 1.14e-28

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


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 115.57  E-value: 1.14e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   9 VVGKGSYGEVnlvRHKSDRKQYVIKKLNLRTSSRRERRAAE---QEAQLLSQLKHPNIVMYResweG---EDCQLYIVMG 82
Cdd:cd14061   1 VIGVGGFGKV---YRGIWRGEEVAVKAARQDPDEDISVTLEnvrQEARLFWMLRHPNIIALR----GvclQPPNLCLVME 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FCEGGDLYHRLKqqkGELLPERQVVEWFVQIAMALQYLHEKH---ILHRDLKTQNIFLTKT--------NIIKVGDLGIA 151
Cdd:cd14061  74 YARGGALNRVLA---GRKIPPHVLVDWAIQIARGMNYLHNEApvpIIHRDLKSSNILILEAienedlenKTLKITDFGLA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 152 RVLENQNDMASTliGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGK--LPqMPSKYD 229
Cdd:cd14061 151 REWHKTTRMSAA--GTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPYKGIDGLAVAYGVAVNKltLP-IPSTCP 227
                       250       260
                ....*....|....*....|....*..
gi 41055987 230 PQLGELIKRMLCKKPEDRPDVKHILRQ 256
Cdd:cd14061 228 EPFAQLMKDCWQPDPHDRPSFADILKQ 254
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
3-259 1.25e-28

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: 116.77  E-value: 1.25e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   3 GYLFVRVVGKGSYGEVNLVRHKSDRKQYV----IKKLNLRTSSRR--ERRAAEQEAQLLSQLKHPNIVMYRESWEgEDCQ 76
Cdd:cd14096   2 NYRLINKIGEGAFSNVYKAVPLRNTGKPVaikvVRKADLSSDNLKgsSRANILKEVQIMKRLSHPNIVKLLDFQE-SDEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  77 LYIVMGFCEGGDLYHRLKQQK--GELLpERQVvewFVQIAMALQYLHEKHILHRDLKTQNIFL----------------- 137
Cdd:cd14096  81 YYIVLELADGGEIFHQIVRLTyfSEDL-SRHV---ITQVASAVKYLHEIGVVHRDIKPENLLFepipfipsivklrkadd 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 138 --TKTN--------------IIKVGDLGIARVLENQNDMasTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLK 201
Cdd:cd14096 157 deTKVDegefipgvggggigIVKLADFGLSKQVWDSNTK--TPCGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGF 234
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41055987 202 HAFNAKDMNSLVYRIVEGKLPQMPSKYDP---QLGELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd14096 235 PPFYDESIETLTEKISRGDYTFLSPWWDEiskSAKDLISHLLTVDPAKRYDIDEFLAHPWI 295
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
11-254 1.42e-28

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: 115.05  E-value: 1.42e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  11 GKGSYGEVNLVRHKSDRKQYVIKKLNlrtssrrerrAAEQEAQLLSQLKHPNIV-MYRESWEG-EDCqlyIVMGFCEGGD 88
Cdd:cd14060   2 GGGSFGSVYRAIWVSQDKEVAVKKLL----------KIEKEAEILSVLSHRNIIqFYGAILEApNYG---IVTEYASYGS 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  89 LYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEK---HILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMasTLI 165
Cdd:cd14060  69 LFDYLNSNESEEMDMDQIMTWATDIAKGMHYLHMEapvKVIHRDLKSRNVVIAADGVLKICDFGASRFHSHTTHM--SLV 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 166 GTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVE-GKLPQMPSKYDPQLGELIKRMLCKKP 244
Cdd:cd14060 147 GTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPFKGLEGLQVAWLVVEkNERPTIPSSCPRSFAELMRRCWEADV 226
                       250
                ....*....|
gi 41055987 245 EDRPDVKHIL 254
Cdd:cd14060 227 KERPSFKQII 236
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
3-265 1.42e-28

Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK8, CDC2L6, and similar proteins. CDK8 functions as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II-dependent transcription. CDC2L6 also associates with Mediator in complexes lacking CDK8. In VP16-dependent transcriptional activation, CDK8 and CDC2L6 exerts opposing effects by positive and negative regulation, respectively, in similar conditions. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 117.00  E-value: 1.42e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   3 GYLFVRVVGKGSYGEVNLVRHK--SDRKQYVIKKLnlRTSSRRE---RRAAEQEAQLLSQLKHPNIVMYRESW-EGEDCQ 76
Cdd:cd07842   1 KYEIEGCIGRGTYGRVYKAKRKngKDGKEYAIKKF--KGDKEQYtgiSQSACREIALLRELKHENVVSLVEVFlEHADKS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  77 LYIVMGFCEGgDLYHRLK---QQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLT----KTNIIKVGDLG 149
Cdd:cd07842  79 VYLLFDYAEH-DLWQIIKfhrQAKRVSIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVMgegpERGVVKIGDLG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 150 IARVLENQNDMASTLIG---TPYYMSPEL-FSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDmnslvyrivEGKLPQMP 225
Cdd:cd07842 158 LARLFNAPLKPLADLDPvvvTIWYRAPELlLGARHYTKAIDIWAIGCIFAELLTLEPIFKGRE---------AKIKKSNP 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 41055987 226 SKYDpQLGELIKRMLCKKPEDRPDVKHILRQPYIKHQISM 265
Cdd:cd07842 229 FQRD-QLERIFEVLGTPTEKDWPDIKKMPEYDTLKSDTKA 267
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
10-199 1.66e-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: 116.22  E-value: 1.66e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAeQEAQLLSQLKHPNIVMYRESWEG------EDCQLyIVMGF 83
Cdd:cd14038   2 LGTGGFGNVLRWINQETGEQVAIKQCRQELSPKNRERWC-LEIQIMKRLNHPNVVAARDVPEGlqklapNDLPL-LAMEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGGDLYHRLKQQKGEL-LPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTN---IIKVGDLGIARVLEnQND 159
Cdd:cd14038  80 CQGGDLRKYLNQFENCCgLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGEqrlIHKIIDLGYAKELD-QGS 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 41055987 160 MASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMAT 199
Cdd:cd14038 159 LCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECIT 198
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
5-259 2.38e-28

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: 115.54  E-value: 2.38e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   5 LFVRV--VGKGSYGEVNLVRHKSDRKQYVIKKLNLRtSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEgEDCQLYIVMG 82
Cdd:cd06642   5 LFTKLerIGKGSFGEVYKGIDNRTKEVVAIKIIDLE-EAEDEIEDIQQEITVLSQCDSPYITRYYGSYL-KGTKLWIIME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FCEGGDLYHRLKQQKgelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMAS 162
Cdd:cd06642  83 YLGGGSALDLLKPGP---LEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRN 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 163 TLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPSKYDPQLGELIKRMLCK 242
Cdd:cd06642 160 TFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDLHPMRVLFLIPKNSPPTLEGQHSKPFKEFVEACLNK 239
                       250
                ....*....|....*..
gi 41055987 243 KPEDRPDVKHILRQPYI 259
Cdd:cd06642 240 DPRFRPTAKELLKHKFI 256
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
8-247 2.47e-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: 116.75  E-value: 2.47e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKQY---VIKKlNLRTSS------RRERRAAEQEAQllsqlkHPNIVMYRESWEGEDcQLY 78
Cdd:cd05588   1 RVIGRGSYAKVLMVELKKTKRIYamkVIKK-ELVNDDedidwvQTEKHVFETASN------HPFLVGLHSCFQTES-RLF 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  79 IVMGFCEGGDL-YHRLKQQKgelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQ 157
Cdd:cd05588  73 FVIEFVNGGDLmFHMQRQRR---LPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRP 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 158 NDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAF------NAKDMNS--LVYRIVEGKLPQMPSKYD 229
Cdd:cd05588 150 GDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPFdivgssDNPDQNTedYLFQVILEKPIRIPRSLS 229
                       250
                ....*....|....*...
gi 41055987 230 PQLGELIKRMLCKKPEDR 247
Cdd:cd05588 230 VKAASVLKGFLNKNPAER 247
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
7-260 2.63e-28

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: 116.56  E-value: 2.63e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   7 VRVVGKGSYGEVNLVRHKSDRKQYVIKKLnlRTSSRRERRAAEQ---EAQLLSQLKHPNIVMYRESWEGEDCqLYIVMGF 83
Cdd:cd05599   6 LKVIGRGAFGEVRLVRKKDTGHVYAMKKL--RKSEMLEKEQVAHvraERDILAEADNPWVVKLYYSFQDEEN-LYLIMEF 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGGDLYHRLkqQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNdMAST 163
Cdd:cd05599  83 LPGGDMMTLL--MKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGLCTGLKKSH-LAYS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 164 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKL-----PQMPskYDPQLGELIKR 238
Cdd:cd05599 160 TVGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKIMNWREtlvfpPEVP--ISPEAKDLIER 237
                       250       260
                ....*....|....*....|....*
gi 41055987 239 MLCkKPEDR---PDVKHILRQPYIK 260
Cdd:cd05599 238 LLC-DAEHRlgaNGVEEIKSHPFFK 261
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
6-247 2.73e-28

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: 116.64  E-value: 2.73e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   6 FVRVVGKGSYGEVNLVRHKSDRKQYVIKKLN---LRTSSRRERRAAEQEAQLLSQlKHPNIVMYRESWEGEDcQLYIVMG 82
Cdd:cd05616   4 FLMVLGKGSFGKVMLAERKGTDELYAVKILKkdvVIQDDDVECTMVEKRVLALSG-KPPFLTQLHSCFQTMD-RLYFVME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FCEGGDLYHRLkQQKGELlPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARvlENQND--M 160
Cdd:cd05616  82 YVNGGDLMYHI-QQVGRF-KEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCK--ENIWDgvT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 161 ASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLpQMPSKYDPQLGELIKRML 240
Cdd:cd05616 158 TKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNV-AYPKSMSKEAVAICKGLM 236

                ....*..
gi 41055987 241 CKKPEDR 247
Cdd:cd05616 237 TKHPGKR 243
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
10-259 2.80e-28

The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2 (also called STK17B). Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. DRAK2 has been implicated in inducing or enhancing apoptosis in beta cells, fibroblasts, and lymphoid cells, where it is highly expressed. It is involved in regulating many immune processes including the germinal center (GC) reaction, responses to thymus-dependent antigens, activated T cell survival, memory T cell responses. It may be involved in the development of autoimmunity. The DRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 115.02  E-value: 2.80e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLK-HPNIVMYRESWEgEDCQLYIVMGFCEGGD 88
Cdd:cd14198  16 LGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDCRAEILHEIAVLELAKsNPRVVNLHEVYE-TTSEIILILEYAAGGE 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  89 LYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNI---IKVGDLGIARVLENQNDMAStLI 165
Cdd:cd14198  95 IFNLCVPDLAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYPlgdIKIVDFGMSRKIGHACELRE-IM 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 166 GTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRI----VEGKLPQMPSKYDPQLgELIKRMLC 241
Cdd:cd14198 174 GTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNIsqvnVDYSEETFSSVSQLAT-DFIQKLLV 252
                       250
                ....*....|....*...
gi 41055987 242 KKPEDRPDVKHILRQPYI 259
Cdd:cd14198 253 KNPEKRPTAEICLSHSWL 270
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
4-259 3.70e-28

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: 114.40  E-value: 3.70e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIK---KLNLRTSSRRERRaaeqEAQLLSQLKHPNIVMYRESWEGEDcQLYIV 80
Cdd:cd14078   5 YELHETIGSGGFAKVKLATHILTGEKVAIKimdKKALGDDLPRVKT----EIEALKNLSHQHICRLYHVIETDN-KIFMV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MGFCEGGDLYHRLKQQkgELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGI-ARVLENQND 159
Cdd:cd14078  80 LEYCPGGELFDYIVAK--DRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLcAKPKGGMDH 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 160 MASTLIGTPYYMSPELFSNKPY-NYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLpQMPSKYDPQLGELIKR 238
Cdd:cd14078 158 HLETCCGSPAYAAPELIQGKPYiGSEADVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSGKY-EEPEWLSPSSKLLLDQ 236
                       250       260
                ....*....|....*....|.
gi 41055987 239 MLCKKPEDRPDVKHILRQPYI 259
Cdd:cd14078 237 MLQVDPKKRITVKELLNHPWV 257
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
9-260 3.81e-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: 114.41  E-value: 3.81e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   9 VVGKGSYGEVNLVRH---KSDRKQYVIKKLNlRTSSRRERRAAEQ---EAQLLSQLKH-PNIVMYRESWEgEDCQLYIVM 81
Cdd:cd05583   1 VLGTGAYGKVFLVRKvggHDAGKLYAMKVLK-KATIVQKAKTAEHtmtERQVLEAVRQsPFLVTLHYAFQ-TDAKLHLIL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  82 GFCEGGDLYHRLKQQkgELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIAR-VLENQNDM 160
Cdd:cd05583  79 DYVNGGELFTHLYQR--EHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKeFLPGENDR 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 161 ASTLIGTPYYMSPELFSNKP--YNYKSDVWALGCCVYEMATLKHAF---NAKDMNSLVYRIVEGKLPQMPSKYDPQLGEL 235
Cdd:cd05583 157 AYSFCGTIEYMAPEVVRGGSdgHDKAVDWWSLGVLTYELLTGASPFtvdGERNSQSEISKRILKSHPPIPKTFSAEAKDF 236
                       250       260       270
                ....*....|....*....|....*....|
gi 41055987 236 IKRMLCKKPEDR-----PDVKHILRQPYIK 260
Cdd:cd05583 237 ILKLLEKDPKKRlgagpRGAHEIKEHPFFK 266
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
2-247 5.93e-28

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: 114.62  E-value: 5.93e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLF-VRVVGKGSYGEVNLVRHKSDRKQYVIKKLNL-RTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEdCQLYI 79
Cdd:cd05607   1 DKYFYeFRVLGKGGFGEVCAVQVKNTGQMYACKKLDKkRLKKKSGEKMALLEKEILEKVNSPFIVSLAYAFETK-THLCL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  80 VMGFCEGGDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQND 159
Cdd:cd05607  80 VMSLMNGGDLKYHIYNVGERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEVKEGKP 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 160 MASTlIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAF-NAKDMNS---LVYRIVEGKLPQMPSKYDPQLGEL 235
Cdd:cd05607 160 ITQR-AGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFrDHKEKVSkeeLKRRTLEDEVKFEHQNFTEEAKDI 238
                       250
                ....*....|..
gi 41055987 236 IKRMLCKKPEDR 247
Cdd:cd05607 239 CRLFLAKKPENR 250
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
4-259 6.15e-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: 113.97  E-value: 6.15e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSrrERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGF 83
Cdd:cd06646  11 YELIQRVGSGTYGDVYKARNLHTGELAAVKIIKLEPGD--DFSLIQQEIFMVKECKHCNIVAYFGSYLSRE-KLWICMEY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGG---DLYHRLKQqkgelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDM 160
Cdd:cd06646  88 CGGGslqDIYHVTGP-----LSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAAKITATIAK 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 161 ASTLIGTPYYMSPELFS---NKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLVYRIVEGKLP---QMPSKYDPQLG 233
Cdd:cd06646 163 RKSFIGTPYWMAPEVAAvekNGGYNQLCDIWAVGITAIELAELQPPmFDLHPMRALFLMSKSNFQPpklKDKTKWSSTFH 242
                       250       260
                ....*....|....*....|....*.
gi 41055987 234 ELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd06646 243 NFVKISLTKNPKKRPTAERLLTHLFV 268
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
9-256 6.60e-28

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: 113.98  E-value: 6.60e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   9 VVGKGSYGEVnlvRHKSDRKQYVIKKLNLRTSSRRERRAAE---QEAQLLSQLKHPNIVmyreSWEG---EDCQLYIVMG 82
Cdd:cd14146   1 IIGVGGFGKV---YRATWKGQEVAVKAARQDPDEDIKATAEsvrQEAKLFSMLRHPNII----KLEGvclEEPNLCLVME 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FCEGGDLYHRL-------KQQKGELLPERQVVEWFVQIAMALQYLHEKH---ILHRDLKTQNIFLTK--------TNIIK 144
Cdd:cd14146  74 FARGGTLNRALaaanaapGPRRARRIPPHILVNWAVQIARGMLYLHEEAvvpILHRDLKSSNILLLEkiehddicNKTLK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 145 VGDLGIARVLENQNDMASTliGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLP-Q 223
Cdd:cd14146 154 ITDFGLAREWHRTTKMSAA--GTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYRGIDGLAVAYGVAVNKLTlP 231
                       250       260       270
                ....*....|....*....|....*....|...
gi 41055987 224 MPSKYDPQLGELIKRMLCKKPEDRPDVKHILRQ 256
Cdd:cd14146 232 IPSTCPEPFAKLMKECWEQDPHIRPSFALILEQ 264
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
6-247 7.06e-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: 115.89  E-value: 7.06e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   6 FVRVVGKGSYGEVNLVRHKSDRKQYVIKKLnlrtssRRERRAAEQEAQLLSQLKH--------PNIVMYRESWEGEDcQL 77
Cdd:cd05617  19 LIRVIGRGSYAKVLLVRLKKNDQIYAMKVV------KKELVHDDEDIDWVQTEKHvfeqassnPFLVGLHSCFQTTS-RL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  78 YIVMGFCEGGDL-YHRLKQQKgelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLEN 156
Cdd:cd05617  92 FLVIEYVNGGDLmFHMQRQRK---LPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLG 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 157 QNDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNA----KDMNS--LVYRIVEGKLPQMPSKYDP 230
Cdd:cd05617 169 PGDTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIitdnPDMNTedYLFQVILEKPIRIPRFLSV 248
                       250
                ....*....|....*..
gi 41055987 231 QLGELIKRMLCKKPEDR 247
Cdd:cd05617 249 KASHVLKGFLNKDPKER 265
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
8-247 7.12e-28

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: 114.32  E-value: 7.12e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKQYVIKKL-NLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDCqLYIVMGFCEG 86
Cdd:cd05631   6 RVLGKGGFGEVCACQVRATGKMYACKKLeKKRIKKRKGEAMALNEKRILEKVNSRFVVSLAYAYETKDA-LCLVLTIMNG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  87 GDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIArVLENQNDMASTLIG 166
Cdd:cd05631  85 GDLKFHIYNMGNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLA-VQIPEGETVRGRVG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 167 TPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAF---NAKDMNSLVYRIVEGKLPQMPSKYDPQLGELIKRMLCKK 243
Cdd:cd05631 164 TVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFrkrKERVKREEVDRRVKEDQEEYSEKFSEDAKSICRMLLTKN 243

                ....
gi 41055987 244 PEDR 247
Cdd:cd05631 244 PKER 247
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
10-262 7.32e-28

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: 114.38  E-value: 7.32e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWE----GEDCqLYIVMGFCE 85
Cdd:cd14030  33 IGRGSFKTVYKGLDTETTVEVAWCELQDRKLSKSERQRFKEEAGMLKGLQHPNIVRFYDSWEstvkGKKC-IVLVTELMT 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  86 GGDLYHRLKQQKgeLLPERQVVEWFVQIAMALQYLHEKH--ILHRDLKTQNIFLT-KTNIIKVGDLGIARVleNQNDMAS 162
Cdd:cd14030 112 SGTLKTYLKRFK--VMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLATL--KRASFAK 187
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 163 TLIGTPYYMSPELFSNKpYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPqmPSKYD----PQLGELIKR 238
Cdd:cd14030 188 SVIGTPEFMAPEMYEEK-YDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRRVTSGVK--PASFDkvaiPEVKEIIEG 264
                       250       260
                ....*....|....*....|....
gi 41055987 239 MLCKKPEDRPDVKHILRQPYIKHQ 262
Cdd:cd14030 265 CIRQNKDERYAIKDLLNHAFFQEE 288
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
8-258 8.52e-28

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: 113.64  E-value: 8.52e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSS---RRERRAAEQEAQLLSQLKHPNIVMY----RESWEGedcQLYIV 80
Cdd:cd06651  13 KLLGQGAFGRVYLCYDVDTGRELAAKQVQFDPESpetSKEVSALECEIQLLKNLQHERIVQYygclRDRAEK---TLTIF 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MGFCEGGDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLEN---Q 157
Cdd:cd06651  90 MEYMPGGSVKDQLKAYGA--LTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTicmS 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 158 NDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRI-VEGKLPQMPSKYDPQLGELI 236
Cdd:cd06651 168 GTGIRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIaTQPTNPQLPSHISEHARDFL 247
                       250       260
                ....*....|....*....|..
gi 41055987 237 KRMLCKKpEDRPDVKHILRQPY 258
Cdd:cd06651 248 GCIFVEA-RHRPSAEELLRHPF 268
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
4-260 1.04e-27

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: 114.21  E-value: 1.04e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLnlRTSSRRER-----RAAEQEAQLLSQLKHPNIVMYRESWeGEDCQLY 78
Cdd:cd07841   2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKKI--KLGERKEAkdginFTALREIKLLQELKHPNIIGLLDVF-GHKSNIN 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  79 IVMGFCEGgDLYHRLKQqKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQN 158
Cdd:cd07841  79 LVFEFMET-DLEKVIKD-KSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLARSFGSPN 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 159 DMASTLIGTPYYMSPEL-FSNKPYNYKSDVWALGCCVYEMAT-------------LKHAFNA---------KDMNSLVYR 215
Cdd:cd07841 157 RKMTHQVVTRWYRAPELlFGARHYGVGVDMWSVGCIFAELLLrvpflpgdsdidqLGKIFEAlgtpteenwPGVTSLPDY 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 41055987 216 IVEGKLPQMP-SKYDPQLGE----LIKRMLCKKPEDRPDVKHILRQPYIK 260
Cdd:cd07841 237 VEFKPFPPTPlKQIFPAASDdaldLLQRLLTLNPNKRITARQALEHPYFS 286
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
6-247 1.28e-27

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: 115.51  E-value: 1.28e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   6 FVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRER-RAAEQEAQLLSQLK-HPNIVMYRESWEGEDcQLYIVMGF 83
Cdd:cd05618  24 LLRVIGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDDEDiDWVQTEKHVFEQASnHPFLVGLHSCFQTES-RLFFVIEY 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGGDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMAST 163
Cdd:cd05618 103 VNGGDLMFHMQRQRK--LPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTST 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 164 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNA--------KDMNSLVYRIVEGKLPQMPSKYDPQLGEL 235
Cdd:cd05618 181 FCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDIvgssdnpdQNTEDYLFQVILEKQIRIPRSLSVKAASV 260
                       250
                ....*....|..
gi 41055987 236 IKRMLCKKPEDR 247
Cdd:cd05618 261 LKSFLNKDPKER 272
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
6-289 1.62e-27

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: 113.60  E-value: 1.62e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   6 FVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERrAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCE 85
Cdd:cd14168  14 FKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKGKES-SIENEIAVLRKIKHENIVALEDIYESPN-HLYLVMQLVS 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  86 GGDLYHRLKQQKgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFL---TKTNIIKVGDLGIARvLENQNDMAS 162
Cdd:cd14168  92 GGELFDRIVEKG--FYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYfsqDEESKIMISDFGLSK-MEGKGDVMS 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 163 TLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPSKYD---PQLGELIKRM 239
Cdd:cd14168 169 TACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKADYEFDSPYWDdisDSAKDFIRNL 248
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 41055987 240 LCKKPEDRPDVKHILRQPYIKHQISMFLEATKEKTAKSRKNAANGKLNSA 289
Cdd:cd14168 249 MEKDPNKRYTCEQALRHPWIAGDTALCKNIHESVSAQIRKNFAKSKWRQA 298
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
10-258 1.70e-27

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: 113.14  E-value: 1.70e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLK---HPNIVMYRESWEGED----CQLYIVMG 82
Cdd:cd07838   7 IGEGAYGTVYKARDLQDGRFVALKKVRVPLSEEGIPLSTIREIALLKQLEsfeHPNVVRLLDVCHGPRtdreLKLTLVFE 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FCEGgDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQndMAS 162
Cdd:cd07838  87 HVDQ-DLATYLDKCPKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFGLARIYSFE--MAL 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 163 TLI-GTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAF---NAKDM------------------NSLVYRI---- 216
Cdd:cd07838 164 TSVvVTLWYRAPEVLLQSSYATPVDMWSVGCIFAELFNRRPLFrgsSEADQlgkifdviglpseeewprNSALPRSsfps 243
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 41055987 217 -----VEGKLPQMpskyDPQLGELIKRMLCKKPEDRPDVKHILRQPY 258
Cdd:cd07838 244 ytprpFKSFVPEI----DEEGLDLLKKMLTFNPHKRISAFEALQHPY 286
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
10-259 2.90e-27

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: 112.35  E-value: 2.90e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNL----------RTSSRRERRAAE--------------QEAQLLSQLKHPNIVM 65
Cdd:cd14200   8 IGKGSYGVVKLAYNESDDKYYAMKVLSKkkllkqygfpRRPPPRGSKAAQgeqakplaplervyQEIAILKKLDHVNIVK 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  66 YRESWE--GEDcQLYIVMGFCEGGDLYHRLKQQKgelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNII 143
Cdd:cd14200  88 LIEVLDdpAED-NLYMVFDLLRKGPVMEVPSDKP---FSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDDGHV 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 144 KVGDLGIARVLENQNDMASTLIGTPYYMSPELFSNKPYNYKS---DVWALG----CCVYEMATLKHAFNAKDMNSLVYRI 216
Cdd:cd14200 164 KIADFGVSNQFEGNDALLSSTAGTPAFMAPETLSDSGQSFSGkalDVWAMGvtlyCFVYGKCPFIDEFILALHNKIKNKP 243
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 41055987 217 VEgkLPQMPSKYDpQLGELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd14200 244 VE--FPEEPEISE-ELKDLILKMLDKNPETRITVPEIKVHPWV 283
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
7-247 3.30e-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: 113.10  E-value: 3.30e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   7 VRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRER-RAAEQEAQLLSQLKHPNIVMYRESWEGEDCqLYIVMGFCE 85
Cdd:cd05574   6 IKLLGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMIKRNKvKRVLTEREILATLDHPFLPTLYASFQTSTH-LCFVMDYCP 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  86 GGDLYHRLKQQKGELLPErQVVEWFV-QIAMALQYLHEKHILHRDLKTQNIFL-------------------TKTNIIKV 145
Cdd:cd05574  85 GGELFRLLQKQPGKRLPE-EVARFYAaEVLLALEYLHLLGFVYRDLKPENILLhesghimltdfdlskqssvTPPPVRKS 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 146 GDLGIAR--VLENQNDMAST--------LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYR 215
Cdd:cd05574 164 LRKGSRRssVKSIEKETFVAepsarsnsFVGTEEYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTTPFKGSNRDETFSN 243
                       250       260       270
                ....*....|....*....|....*....|....
gi 41055987 216 IVEGKL--PQMPSKYDpQLGELIKRMLCKKPEDR 247
Cdd:cd05574 244 ILKKELtfPESPPVSS-EAKDLIRKLLVKDPSKR 276
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
2-259 3.31e-27

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: 112.01  E-value: 3.31e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNlRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVM 81
Cdd:cd14183   6 ERYKVGRTIGDGNFAVVKECVERSTGREYALKIIN-KSKCRGKEHMIQNEVSILRRVKHPNIVLLIEEMDMPT-ELYLVM 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  82 GFCEGGDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTK----TNIIKVGDLGIARVLENQ 157
Cdd:cd14183  84 ELVKGGDLFDAITSTNK--YTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEhqdgSKSLKLGDFGLATVVDGP 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 158 ndmASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAF--NAKDMNSLVYRIVEGKLpQMPSKY----DPQ 231
Cdd:cd14183 162 ---LYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFrgSGDDQEVLFDQILMGQV-DFPSPYwdnvSDS 237
                       250       260
                ....*....|....*....|....*...
gi 41055987 232 LGELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd14183 238 AKELITMMLQVDVDQRYSALQVLEHPWV 265
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
9-247 3.62e-27

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: 112.87  E-value: 3.62e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   9 VVGKGSYGEVNLVRHKSDRKQYVIKKLNLRT--------SSRRERRAaeqeaqLLSQLKHPNIVMYRESWEGEDcQLYIV 80
Cdd:cd05587   3 VLGKGSFGKVMLAERKGTDELYAIKILKKDViiqdddveCTMVEKRV------LALSGKPPFLTQLHSCFQTMD-RLYFV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MGFCEGGDLYHRLkQQKGELlPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDM 160
Cdd:cd05587  76 MEYVNGGDLMYHI-QQVGKF-KEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKEGIFGGKT 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 161 ASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKlPQMPSKYDPQLGELIKRML 240
Cdd:cd05587 154 TRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHN-VSYPKSLSKEAVSICKGLL 232

                ....*..
gi 41055987 241 CKKPEDR 247
Cdd:cd05587 233 TKHPAKR 239
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
4-247 3.62e-27

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: 113.55  E-value: 3.62e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRER-RAAEQEAQLLSQLKHPNIVMYRESWEGEDCQLYIVMG 82
Cdd:cd05615  12 FNFLMVLGKGSFGKVMLAERKGSDELYAIKILKKDVVIQDDDvECTMVEKRVLALQDKPPFLTQLHSCFQTVDRLYFVME 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FCEGGDLYHRLkQQKGELlPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMAS 162
Cdd:cd05615  92 YVNGGDLMYHI-QQVGKF-KEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMVEGVTTR 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 163 TLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLpQMPSKYDPQLGELIKRMLCK 242
Cdd:cd05615 170 TFCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNV-SYPKSLSKEAVSICKGLMTK 248

                ....*
gi 41055987 243 KPEDR 247
Cdd:cd05615 249 HPAKR 253
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
10-269 4.09e-27

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK10, also called PISSLRE, is essential for cell growth and proliferation, and acts through the G2/M phase of the cell cycle. CDK10 has also been identified as an important factor in endocrine therapy resistance in breast cancer. CDK10 silencing increases the transcription of c-RAF and the activation of the p42/p44 MAPK pathway, which leads to antiestrogen resistance. Patients who express low levels of CDK10 relapse early on tamoxifen. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK10 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 112.46  E-value: 4.09e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLN-------LRTSSRRERRaaeqeaqLLSQLKHPNIVMYRESWEGEDCQ-LYIVM 81
Cdd:cd07845  15 IGEGTYGIVYRARDTTSGEIVALKKVRmdnerdgIPISSLREIT-------LLLNLRHPNIVELKEVVVGKHLDsIFLVM 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  82 GFCEGgDLyHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLEN-QNDM 160
Cdd:cd07845  88 EYCEQ-DL-ASLLDNMPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLARTYGLpAKPM 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 161 ASTLIgTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMatLKHAfnakdmnslvyrivegklPQMPSKYDPQLGELIKRM 239
Cdd:cd07845 166 TPKVV-TLWYRAPElLLGCTTYTTAIDMWAVGCILAEL--LAHK------------------PLLPGKSEIEQLDLIIQL 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 41055987 240 LCKKPE-------DRPDVKHIL--RQPY--IKHQISMFLEA 269
Cdd:cd07845 225 LGTPNEsiwpgfsDLPLVGKFTlpKQPYnnLKHKFPWLSEA 265
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
10-254 4.12e-27

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: 111.69  E-value: 4.12e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDrkqYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESweGEDCQLYIVMGFCEGGDL 89
Cdd:cd14151  16 IGSGSFGTVYKGKWHGD---VAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGY--STKPQLAIVTQWCEGSSL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  90 YHRLK--QQKGELlpeRQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLE--NQNDMASTLI 165
Cdd:cd14151  91 YHHLHiiETKFEM---IKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSrwSGSHQFEQLS 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 166 GTPYYMSPELF---SNKPYNYKSDVWALGCCVYEMATLKHAF-NAKDMNSLVYRIVEGKLPQMPSKYDPQLGELIKRMLC 241
Cdd:cd14151 168 GSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPYsNINNRDQIIFMVGRGYLSPDLSKVRSNCPKAMKRLMA 247
                       250
                ....*....|....*..
gi 41055987 242 ----KKPEDRPDVKHIL 254
Cdd:cd14151 248 eclkKKRDERPLFPQIL 264
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
10-274 4.33e-27

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: 112.13  E-value: 4.33e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRErrAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEGGDL 89
Cdd:cd06654  28 IGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKKE--LIINEILVMRENKNPNIVNYLDSYLVGD-ELWVVMEYLAGGSL 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  90 YHRLKQQkgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLIGTPY 169
Cdd:cd06654 105 TDVVTET---CMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPY 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 170 YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQM--PSKYDPQLGELIKRMLCKKPEDR 247
Cdd:cd06654 182 WMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELqnPEKLSAIFRDFLNRCLEMDVEKR 261
                       250       260       270
                ....*....|....*....|....*....|..
gi 41055987 248 PDVKHILRQPYIK-----HQISMFLEATKEKT 274
Cdd:cd06654 262 GSAKELLQHQFLKiakplSSLTPLIAAAKEAT 293
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
10-260 4.47e-27

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: 112.12  E-value: 4.47e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRErrAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEGGDL 89
Cdd:cd06656  27 IGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKE--LIINEILVMRENKNPNIVNYLDSYLVGD-ELWVVMEYLAGGSL 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  90 YHRLKQQkgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLIGTPY 169
Cdd:cd06656 104 TDVVTET---CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPY 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 170 YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQM--PSKYDPQLGELIKRMLCKKPEDR 247
Cdd:cd06656 181 WMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELqnPERLSAVFRDFLNRCLEMDVDRR 260
                       250
                ....*....|...
gi 41055987 248 PDVKHILRQPYIK 260
Cdd:cd06656 261 GSAKELLQHPFLK 273
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
9-248 4.75e-27

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: 111.32  E-value: 4.75e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   9 VVGKGSYGEVNLVRHKSDrkQYVIKKLNLRTSSRRERRAAEQEAQLLSqLKHPNIV--MYRESWEGEDCQLYIVMGFCEG 86
Cdd:cd13979  10 PLGSGGFGSVYKATYKGE--TVAVKIVRRRRKNRASRQSFWAELNAAR-LRHENIVrvLAAETGTDFASLGLIIMEYCGN 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  87 GDLYHRLKQQKGELLPERQVvEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDM---AST 163
Cdd:cd13979  87 GTLQQLIYEGSEPLPLAHRI-LISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSVKLGEGNEVgtpRSH 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 164 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFnAKDMNSLVYRIVEGKL-PQMPSKYDPQLGE----LIKR 238
Cdd:cd13979 166 IGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPY-AGLRQHVLYAVVAKDLrPDLSGLEDSEFGQrlrsLISR 244
                       250
                ....*....|
gi 41055987 239 MLCKKPEDRP 248
Cdd:cd13979 245 CWSAQPAERP 254
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
10-260 4.77e-27

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK3, also called DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk), contains an N-terminal kinase domain and a C-terminal region with nuclear localization signals (NLS) and a leucine zipper motif that mediates homodimerization and interaction with other leucine zipper proteins. It interacts with Par-4, a protein that contains a death domain and interacts with actin filaments. DAPK3 is present in both the cytoplasm and nucleus. Its co-expression with Par-4 results in the co-localization of the two proteins to actin filaments. In addition to cell death, DAPK3 is also implicated in mediating cell motility and the contraction of smooth muscles. The DAPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271097 [Multi-domain]  Cd Length: 271  Bit Score: 111.63  E-value: 4.77e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLR--TSSRR--ERRAAEQEAQLLSQLKHPNIVMYRESWEGEdCQLYIVMGFCE 85
Cdd:cd14195  13 LGSGQFAIVRKCREKGTGKEYAAKFIKKRrlSSSRRgvSREEIEREVNILREIQHPNIITLHDIFENK-TDVVLILELVS 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  86 GGDLYHRLKQQkgELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNI----IKVGDLGIARVLENQNDMA 161
Cdd:cd14195  92 GGELFDFLAEK--ESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVpnprIKLIDFGIAHKIEAGNEFK 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 162 StLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIvEGKLPQMPSKYDPQLGEL----IK 237
Cdd:cd14195 170 N-IFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNI-SAVNYDFDEEYFSNTSELakdfIR 247
                       250       260
                ....*....|....*....|...
gi 41055987 238 RMLCKKPEDRPDVKHILRQPYIK 260
Cdd:cd14195 248 RLLVKDPKKRMTIAQSLEHSWIK 270
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
4-260 5.09e-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: 112.84  E-value: 5.09e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKL----NLRTSSRRERRaaeqEAQLLSQLKHPNIVMYRE-------SWEG 72
Cdd:cd07855   7 YEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIpnafDVVTTAKRTLR----ELKILRHFKHDNIIAIRDilrpkvpYADF 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  73 EDcqLYIVMGFCEGgDLYHRLkqQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIAR 152
Cdd:cd07855  83 KD--VYVVLDLMES-DLHHII--HSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMAR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 153 VL-----ENQNDMAStLIGTPYYMSPEL-FSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDM----------------- 209
Cdd:cd07855 158 GLctspeEHKYFMTE-YVATRWYRAPELmLSLPEYTQAIDMWSVGCIFAEMLGRRQLFPGKNYvhqlqliltvlgtpsqa 236
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41055987 210 ------NSLVYRIVEGkLPQ---------MPSKyDPQLGELIKRMLCKKPEDRPDVKHILRQPYIK 260
Cdd:cd07855 237 vinaigADRVRRYIQN-LPNkqpvpwetlYPKA-DQQALDLLSQMLRFDPSERITVAEALQHPFLA 300
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
2-265 5.65e-27

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: 111.66  E-value: 5.65e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNlrtssRRERRAAEQEAQLLSQLKHPNIVMYRESWEgEDCQLYIVM 81
Cdd:cd14175   1 DGYVVKETIGVGSYSVCKRCVHKATNMEYAVKVID-----KSKRDPSEEIEILLRYGQHPNIITLKDVYD-DGKHVYLVT 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  82 GFCEGGDLYHRLKQQKgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTN----IIKVGDLGIARVLENQ 157
Cdd:cd14175  75 ELMRGGELLDKILRQK--FFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVDESgnpeSLRICDFGFAKQLRAE 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 158 NDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFN---AKDMNSLVYRIVEGKLPQMPSKYDP---Q 231
Cdd:cd14175 153 NGLLMTPCYTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFAngpSDTPEEILTRIGSGKFTLSGGNWNTvsdA 232
                       250       260       270
                ....*....|....*....|....*....|....
gi 41055987 232 LGELIKRMLCKKPEDRPDVKHILRQPYIKHQISM 265
Cdd:cd14175 233 AKDLVSKMLHVDPHQRLTAKQVLQHPWITQKDKL 266
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
4-259 6.52e-27

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


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 110.68  E-value: 6.52e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKklnLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGF 83
Cdd:cd14111   5 YTFLDEKARGRFGVIRRCRENATGKNFPAK---IVPYQAEEKQGVLQEYEILKSLHHERIMALHEAYITPR-YLVLIAEF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGGDLYHRLKQQKgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQN-DMAS 162
Cdd:cd14111  81 CSGKELLHSLIDRF--RYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSAQSFNPLSlRQLG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 163 TLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPqmPSKYDPQLGE----LIKR 238
Cdd:cd14111 159 RRTGTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKILVAKFD--AFKLYPNVSQsaslFLKK 236
                       250       260
                ....*....|....*....|.
gi 41055987 239 MLCKKPEDRPDVKHILRQPYI 259
Cdd:cd14111 237 VLSSYPWSRPTTKDCFAHAWL 257
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
1-258 7.59e-27

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: 112.82  E-value: 7.59e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   1 MDGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAE-QEAQLLSQLKHPNIVMYRESWEGEDcQLYI 79
Cdd:cd05594  24 MNDFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTlTENRVLQNSRHPFLTALKYSFQTHD-RLCF 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  80 VMGFCEGGDLYHRLKQQKgeLLPERQVVEWFVQIAMALQYLH-EKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQN 158
Cdd:cd05594 103 VMEYANGGELFFHLSRER--VFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDG 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 159 DMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLpQMPSKYDPQLGELIKR 238
Cdd:cd05594 181 ATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEI-RFPRTLSPEAKSLLSG 259
                       250       260
                ....*....|....*....|....*
gi 41055987 239 MLCKKPEDR-----PDVKHILRQPY 258
Cdd:cd05594 260 LLKKDPKQRlgggpDDAKEIMQHKF 284
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
2-259 7.77e-27

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: 110.91  E-value: 7.77e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSsrRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVM 81
Cdd:cd06645  11 EDFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEPG--EDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRD-KLWICM 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  82 GFCEGG---DLYHRLKQqkgelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQN 158
Cdd:cd06645  88 EFCGGGslqDIYHVTGP-----LSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITATI 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 159 DMASTLIGTPYYMSPELFS---NKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLVYRIVEGKLP---QMPSKYDPQ 231
Cdd:cd06645 163 AKRKSFIGTPYWMAPEVAAverKGGYNQLCDIWAVGITAIELAELQPPmFDLHPMRALFLMTKSNFQPpklKDKMKWSNS 242
                       250       260
                ....*....|....*....|....*...
gi 41055987 232 LGELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd06645 243 FHHFVKMALTKNPKKRPTAEKLLQHPFV 270
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
50-256 8.89e-27

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: 110.46  E-value: 8.89e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  50 QEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEGGDLYHRLKqqkGELLPERQVVEWFVQIAMALQYLHEKH---IL 126
Cdd:cd14148  42 QEARLFWMLQHPNIIALRGVCLNPP-HLCLVMEYARGGALNRALA---GKKVPPHVLVNWAVQIARGMNYLHNEAivpII 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 127 HRDLKTQNIFLTK--------TNIIKVGDLGIARVLENQNDMASTliGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMA 198
Cdd:cd14148 118 HRDLKSSNILILEpienddlsGKTLKITDFGLAREWHKTTKMSAA--GTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELL 195
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 41055987 199 TLKHAFNAKDMNSLVYRIVEGKLP-QMPSKYDPQLGELIKRMLCKKPEDRPDVKHILRQ 256
Cdd:cd14148 196 TGEVPYREIDALAVAYGVAMNKLTlPIPSTCPEPFARLLEECWDPDPHGRPDFGSILKR 254
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
8-269 1.03e-26

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: 111.60  E-value: 1.03e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKQYVIKKL-NLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDCqLYIVMGFCEG 86
Cdd:cd05632   8 RVLGKGGFGEVCACQVRATGKMYACKRLeKKRIKKRKGESMALNEKQILEKVNSQFVVNLAYAYETKDA-LCLVLTIMNG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  87 GDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIArVLENQNDMASTLIG 166
Cdd:cd05632  87 GDLKFHIYNMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLA-VKIPEGESIRGRVG 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 167 TPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKD---MNSLVYRIVEGKLPQMPSKYDPQLGELIKRMLCKK 243
Cdd:cd05632 166 TVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKekvKREEVDRRVLETEEVYSAKFSEEAKSICKMLLTKD 245
                       250       260       270
                ....*....|....*....|....*....|.
gi 41055987 244 PEDRPDVK-----HILRQPYIKHQISMFLEA 269
Cdd:cd05632 246 PKQRLGCQeegagEVKRHPFFRNMNFKRLEA 276
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
9-258 1.12e-26

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: 110.59  E-value: 1.12e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   9 VVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEGGD 88
Cdd:cd07846   8 LVGEGSYGMVMKCRHKETGQIVAIKKFLESEDDKMVKKIAMREIKMLKQLRHENLVNLIEVFRRKK-RWYLVFEFVDHTV 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  89 LYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLIGTP 168
Cdd:cd07846  87 LDDLEKYPNG--LDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDYVATR 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 169 YYMSPELFSNKP-YNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEG---------------------KLPQMPS 226
Cdd:cd07846 165 WYRAPELLVGDTkYGKAVDVWAVGCLVTEMLTGEPLFPGDSDIDQLYHIIKClgnliprhqelfqknplfagvRLPEVKE 244
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 41055987 227 ---------KYDPQLGELIKRMLCKKPEDRPDVKHILRQPY 258
Cdd:cd07846 245 veplerrypKLSGVVIDLAKKCLHIDPDKRPSCSELLHHEF 285
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
5-259 1.17e-26

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: 110.53  E-value: 1.17e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   5 LFVRV--VGKGSYGEVnlVRHKSDRKQYV--IKKLNLRtSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEgEDCQLYIV 80
Cdd:cd06640   5 LFTKLerIGKGSFGEV--FKGIDNRTQQVvaIKIIDLE-EAEDEIEDIQQEITVLSQCDSPYVTKYYGSYL-KGTKLWII 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MGFCEGGDLYHRLKQQKgelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDM 160
Cdd:cd06640  81 MEYLGGGSALDLLRAGP---FDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 161 ASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMAtlKHAFNAKDMNSL--VYRIVEGKLPQMPSKYDPQLGELIKR 238
Cdd:cd06640 158 RNTFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELA--KGEPPNSDMHPMrvLFLIPKNNPPTLVGDFSKPFKEFIDA 235
                       250       260
                ....*....|....*....|.
gi 41055987 239 MLCKKPEDRPDVKHILRQPYI 259
Cdd:cd06640 236 CLNKDPSFRPTAKELLKHKFI 256
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
50-256 1.18e-26

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: 110.13  E-value: 1.18e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  50 QEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEGGDLYHRLKqqkGELLPERQVVEWFVQIAMALQYLHEKHI---L 126
Cdd:cd14145  54 QEAKLFAMLKHPNIIALRGVCLKEP-NLCLVMEFARGGPLNRVLS---GKRIPPDILVNWAVQIARGMNYLHCEAIvpvI 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 127 HRDLKTQNIFLTK--------TNIIKVGDLGIARVLENQNDMASTliGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMA 198
Cdd:cd14145 130 HRDLKSSNILILEkvengdlsNKILKITDFGLAREWHRTTKMSAA--GTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELL 207
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 41055987 199 TLKHAFNAKDMNSLVYRIVEGKLP-QMPSKYDPQLGELIKRMLCKKPEDRPDVKHILRQ 256
Cdd:cd14145 208 TGEVPFRGIDGLAVAYGVAMNKLSlPIPSTCPEPFARLMEDCWNPDPHSRPPFTNILDQ 266
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
10-259 1.61e-26

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: 109.71  E-value: 1.61e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKklNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEdCQLYIVMGFCEGGDL 89
Cdd:cd14191  10 LGSGKFGQVFRLVEKKTKKVWAGK--FFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEK-ANIVMVLEMVSGGEL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  90 YHRLKQQKGELlPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIF-LTKTNI-IKVGDLGIARVLENQNDMaSTLIGT 167
Cdd:cd14191  87 FERIIDEDFEL-TERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTkIKLIDFGLARRLENAGSL-KVLFGT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 168 PYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPSKYDP---QLGELIKRMLCKKP 244
Cdd:cd14191 165 PEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEisdDAKDFISNLLKKDM 244
                       250
                ....*....|....*
gi 41055987 245 EDRPDVKHILRQPYI 259
Cdd:cd14191 245 KARLTCTQCLQHPWL 259
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
9-257 1.91e-26

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: 110.09  E-value: 1.91e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   9 VVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEGgD 88
Cdd:cd07848   8 VVGEGAYGVVLKCRHKETKEIVAIKKFKDSEENEEVKETTLRELKMLRTLKQENIVELKEAFRRRG-KLYLVFEYVEK-N 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  89 LYHRLKQQKGELLPERqVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMAST-LIGT 167
Cdd:cd07848  86 MLELLEEMPNGVPPEK-VRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLSEGSNANYTeYVAT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 168 PYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRI--VEGKLP--QM--------------PSKYD 229
Cdd:cd07848 165 RWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQPLFPGESEIDQLFTIqkVLGPLPaeQMklfysnprfhglrfPAVNH 244
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 41055987 230 PQ-------------LGELIKRMLCKKPEDRPDVKHILRQP 257
Cdd:cd07848 245 PQslerrylgilsgvLLDLMKNLLKLNPTDRYLTEQCLNHP 285
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
7-262 1.92e-26

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: 110.50  E-value: 1.92e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   7 VRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRER-RAAEQEAQLLSQLKHPNIVMYRESWEGEDCQlYIVMGFCE 85
Cdd:cd06634  20 LREIGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNEKwQDIIKEVKFLQKLRHPNTIEYRGCYLREHTA-WLVMEYCL 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  86 GG--DLYHRLKQQkgelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNdmasT 163
Cdd:cd06634  99 GSasDLLEVHKKP----LQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGSASIMAPAN----S 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 164 LIGTPYYMSPEL---FSNKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLvYRIVEGKLPQMPS-KYDPQLGELIKR 238
Cdd:cd06634 171 FVGTPYWMAPEVilaMDEGQYDGKVDVWSLGITCIELAERKPPlFNMNAMSAL-YHIAQNESPALQSgHWSEYFRNFVDS 249
                       250       260
                ....*....|....*....|....
gi 41055987 239 MLCKKPEDRPDVKHILRQPYIKHQ 262
Cdd:cd06634 250 CLQKIPQDRPTSDVLLKHRFLLRE 273
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
6-256 2.20e-26

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: 109.72  E-value: 2.20e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   6 FVRVVGKGSYGEVNLVRHK--SDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRE-SWEGEDCQLYIVMG 82
Cdd:cd14205   8 FLQQLGKGNFGSVEMCRYDplQDNTGEVVAVKKLQHSTEEHLRDFEREIEILKSLQHDNIVKYKGvCYSAGRRNLRLIME 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FCEGGDLYHRLKQQKgELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLEnqNDMAS 162
Cdd:cd14205  88 YLPYGSLRDYLQKHK-ERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLP--QDKEY 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 163 TLIGTP-----YYMSPELFSNKPYNYKSDVWALGCCVYEMAT------------LKHAFNAKDMNSLVYRIVE-----GK 220
Cdd:cd14205 165 YKVKEPgespiFWYAPESLTESKFSVASDVWSFGVVLYELFTyieksksppaefMRMIGNDKQGQMIVFHLIEllknnGR 244
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 41055987 221 LPQmPSKYDPQLGELIKRMLCKKPEDRPDVKHILRQ 256
Cdd:cd14205 245 LPR-PDGCPDEIYMIMTECWNNNVNQRPSFRDLALR 279
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
10-258 2.53e-26

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: 108.82  E-value: 2.53e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRErraAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEGGDL 89
Cdd:cd14107  10 IGRGTFGFVKRVTHKGNGECCAAKFIPLRSSTRAR---AFQERDILARLSHRRLTCLLDQFETRK-TLILILELCSSEEL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  90 YHRLkQQKGeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLT--KTNIIKVGDLGIARVLENQNDMASTLiGT 167
Cdd:cd14107  86 LDRL-FLKG-VVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVspTREDIKICDFGFAQEITPSEHQFSKY-GS 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 168 PYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKL----PQMPSKYDpQLGELIKRMLCKK 243
Cdd:cd14107 163 PEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVVswdtPEITHLSE-DAKDFIKRVLQPD 241
                       250
                ....*....|....*
gi 41055987 244 PEDRPDVKHILRQPY 258
Cdd:cd14107 242 PEKRPSASECLSHEW 256
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
11-259 2.94e-26

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: 109.21  E-value: 2.94e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  11 GKGSYGEVNLVRHKSDRKQYVIKKLNLRtSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEGGDLY 90
Cdd:cd14169  12 GEGAFSEVVLAQERGSQRLVALKCIPKK-ALRGKEAMVENEIAVLRRINHENIVSLEDIYESPT-HLYLAMELVTGGELF 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  91 HRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQN-IFLT--KTNIIKVGDLGIARVlENQNdMASTLIGT 167
Cdd:cd14169  90 DRIIERGS--YTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENlLYATpfEDSKIMISDFGLSKI-EAQG-MLSTACGT 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 168 PYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLpQMPSKYDPQLGE----LIKRMLCKK 243
Cdd:cd14169 166 PGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILKAEY-EFDSPYWDDISEsakdFIRHLLERD 244
                       250
                ....*....|....*.
gi 41055987 244 PEDRPDVKHILRQPYI 259
Cdd:cd14169 245 PEKRFTCEQALQHPWI 260
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
6-260 2.96e-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: 2.96e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   6 FVRVVGKGSYGEVNLVRHKSDR---KQYVIKKLNLRTSSRRERRA--AEQEAQLLSQLKH-PNIVMYRESWEgEDCQLYI 79
Cdd:cd05613   4 LLKVLGTGAYGKVFLVRKVSGHdagKLYAMKVLKKATIVQKAKTAehTRTERQVLEHIRQsPFLVTLHYAFQ-TDTKLHL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  80 VMGFCEGGDLYHRLKQQkgELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIAR-VLENQN 158
Cdd:cd05613  83 ILDYINGGELFTHLSQR--ERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKeFLLDEN 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 159 DMASTLIGTPYYMSPELF--SNKPYNYKSDVWALGCCVYEMATLKHAFNA---KDMNSLVYRIVEGKLPQMPSKYDPQLG 233
Cdd:cd05613 161 ERAYSFCGTIEYMAPEIVrgGDSGHDKAVDWWSLGVLMYELLTGASPFTVdgeKNSQAEISRRILKSEPPYPQEMSALAK 240
                       250       260       270
                ....*....|....*....|....*....|..
gi 41055987 234 ELIKRMLCKKPEDR-----PDVKHILRQPYIK 260
Cdd:cd05613 241 DIIQRLLMKDPKKRlgcgpNGADEIKKHPFFQ 272
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
10-259 3.22e-26

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: 108.89  E-value: 3.22e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTS--SRR--ERRAAEQEAQLLSQLKHPNIVMYRESWEGEdCQLYIVMGFCE 85
Cdd:cd14196  13 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSraSRRgvSREEIEREVSILRQVLHPNIITLHDVYENR-TDVVLILELVS 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  86 GGDLYHRLKQQkgELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNI----IKVGDLGIARVLENQNDMA 161
Cdd:cd14196  92 GGELFDFLAQK--ESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIEDGVEFK 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 162 StLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVyriveGKLPQMPSKYDPQL--------G 233
Cdd:cd14196 170 N-IFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETL-----ANITAVSYDFDEEFfshtselaK 243
                       250       260
                ....*....|....*....|....*.
gi 41055987 234 ELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd14196 244 DFIRKLLVKETRKRLTIQEALRHPWI 269
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
6-256 3.55e-26

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: 108.91  E-value: 3.55e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   6 FVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSrrERRAAEQEAQLLSQLK-HPNIVMYRES---------WEgedc 75
Cdd:cd14037   7 IEKYLAEGGFAHVYLVKTSNGGNRAALKRVYVNDEH--DLNVCKREIEIMKRLSgHKNIVGYIDSsanrsgngvYE---- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  76 qLYIVMGFCEGGDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKH--ILHRDLKTQNIFLTKTNIIKVGDLGIA-- 151
Cdd:cd14037  81 -VLLLMEYCKGGGVIDLMNQRLQTGLTESEILKIFCDVCEAVAAMHYLKppLIHRDLKVENVLISDSGNYKLCDFGSAtt 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 152 RVLENQNDMASTLI-------GTPYYMSPE---LFSNKPYNYKSDVWALGCCVYEMATLKHAFNakdmNSLVYRIVEGK- 220
Cdd:cd14037 160 KILPPQTKQGVTYVeedikkyTTLQYRAPEmidLYRGKPITEKSDIWALGCLLYKLCFYTTPFE----ESGQLAILNGNf 235
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 41055987 221 -LPQMPsKYDPQLGELIKRMLCKKPEDRPDVKHILRQ 256
Cdd:cd14037 236 tFPDNS-RYSKRLHKLIRYMLEEDPEKRPNIYQVSYE 271
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
4-259 3.93e-26

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: 110.47  E-value: 3.93e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKL---NLRTSSRRERRaaeqEAQLLSQLKHPNIV--------MYRESWEg 72
Cdd:cd07849   7 YQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKIspfEHQTYCLRTLR----EIKILLRFKHENIIgildiqrpPTFESFK- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  73 edcQLYIVMGFCEGgDLYHRLKQQKgelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIAR 152
Cdd:cd07849  82 ---DVYIVQELMET-DLYKLIKTQH---LSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLAR 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 153 VLENQNDMASTL---IGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKD----------------MNSL 212
Cdd:cd07849 155 IADPEHDHTGFLteyVATRWYRAPEiMLNSKGYTKAIDIWSVGCILAEMLSNRPLFPGKDylhqlnlilgilgtpsQEDL 234
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41055987 213 vYRIVEGK-------LPQMP--------SKYDPQLGELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd07849 235 -NCIISLKarnyiksLPFKPkvpwnklfPNADPKALDLLDKMLTFNPHKRITVEEALAHPYL 295
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
10-197 4.43e-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: 107.96  E-value: 4.43e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTssrrERRAAEQEAQLLSQLKHPNIVMYResweG---EDCQLYIVMGFCEG 86
Cdd:cd14065   1 LGKGFFGEVYKVTHRETGKVMVMKELKRFD----EQRSFLKEVKLMRRLSHPNILRFI----GvcvKDNKLNFITEYVNG 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  87 GDLYHRLKQQKgELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIK---VGDLGIARVL--ENQNDMA 161
Cdd:cd14065  73 GTLEELLKSMD-EQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVREANRGRnavVADFGLAREMpdEKTKKPD 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 41055987 162 S----TLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEM 197
Cdd:cd14065 152 RkkrlTVVGSPYWMAPEMLRGESYDEKVDVFSFGIVLCEI 191
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
2-259 4.87e-26

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: 108.95  E-value: 4.87e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNlrtssRRERRAAEQEAQLLSQLKHPNIVMYRESWEgEDCQLYIVM 81
Cdd:cd14178   3 DGYEIKEDIGIGSYSVCKRCVHKATSTEYAVKIID-----KSKRDPSEEIEILLRYGQHPNIITLKDVYD-DGKFVYLVM 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  82 GFCEGGDLYHRLKQQKgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTN----IIKVGDLGIARVLENQ 157
Cdd:cd14178  77 ELMRGGELLDRILRQK--CFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDESgnpeSIRICDFGFAKQLRAE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 158 NDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEM-ATLKHAFNAKD--MNSLVYRIVEGKLPQMPSKYDP---Q 231
Cdd:cd14178 155 NGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGILLYTMlAGFTPFANGPDdtPEEILARIGSGKYALSGGNWDSisdA 234
                       250       260
                ....*....|....*....|....*...
gi 41055987 232 LGELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd14178 235 AKDIVSKMLHVDPHQRLTAPQVLRHPWI 262
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
7-259 5.46e-26

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 110.30  E-value: 5.46e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987    7 VRVVGKGSYGEVNLVRHKSDRKQYVIKKL--NLRTSSRRErraAEQEAQLLSQLKHPNIV----MYRESWEgedcqLYIV 80
Cdd:PLN00034  79 VNRIGSGAGGTVYKVIHRPTGRLYALKVIygNHEDTVRRQ---ICREIEILRDVNHPNVVkchdMFDHNGE-----IQVL 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   81 MGFCEGGDLYHRlkqqkgELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDM 160
Cdd:PLN00034 151 LEFMDGGSLEGT------HIADEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRILAQTMDP 224
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  161 ASTLIGTPYYMSPE-----LFSNKPYNYKSDVWALGCCVYEMATLKHAF---NAKDMNSLVYRIVEGKLPQMPSKYDPQL 232
Cdd:PLN00034 225 CNSSVGTIAYMSPErintdLNHGAYDGYAGDIWSLGVSILEFYLGRFPFgvgRQGDWASLMCAICMSQPPEAPATASREF 304
                        250       260
                 ....*....|....*....|....*..
gi 41055987  233 GELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:PLN00034 305 RHFISCCLQREPAKRWSAMQLLQHPFI 331
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
9-195 6.47e-26

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


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 107.88  E-value: 6.47e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   9 VVGKGSYGEVNLVRHKSDRKQYVIKKLN-LRTSSRRERRAaEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEGG 87
Cdd:cd14082  10 VLGSGQFGIVYGGKHRKTGRDVAIKVIDkLRFPTKQESQL-RNEVAILQQLSHPGVVNLECMFETPE-RVFVVMEKLHGD 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  88 DLYHRLKQQKGELlPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNI---IKVGDLGIARVLEnQNDMASTL 164
Cdd:cd14082  88 MLEMILSSEKGRL-PERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEPfpqVKLCDFGFARIIG-EKSFRRSV 165
                       170       180       190
                ....*....|....*....|....*....|.
gi 41055987 165 IGTPYYMSPELFSNKPYNYKSDVWALGCCVY 195
Cdd:cd14082 166 VGTPAYLAPEVLRNKGYNRSLDMWSVGVIIY 196
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
8-260 6.65e-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: 109.61  E-value: 6.65e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRER-RAAEQEAQLLS-QLKHPNIVMYRESWEGEDcQLYIVMGFCE 85
Cdd:cd05590   1 RVLGKGSFGKVMLARLKESGRLYAVKVLKKDVILQDDDvECTMTEKRILSlARNHPFLTQLYCCFQTPD-RLFFVMEFVN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  86 GGDLYHRLkqQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLI 165
Cdd:cd05590  80 GGDLMFHI--QKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGIFNGKTTSTFC 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 166 GTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLpQMPSKYDPQLGELIKRMLCKKPE 245
Cdd:cd05590 158 GTPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEV-VYPTWLSQDAVDILKAFMTKNPT 236
                       250       260
                ....*....|....*....|.
gi 41055987 246 DRPDV------KHILRQPYIK 260
Cdd:cd05590 237 MRLGSltlggeEAILRHPFFK 257
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
13-207 7.78e-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: 7.78e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  13 GSYGEVNLVRHKSDRKQYVIKKLNLR--------TSSRrerraaeqEAQLLSQLKHPNIVMYRESWEGEDC-QLYIVMGF 83
Cdd:cd07843  16 GTYGVVYRARDKKTGEIVALKKLKMEkekegfpiTSLR--------EINILLKLQHPNIVTVKEVVVGSNLdKIYMVMEY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGgDLYHRLKQQKGELLPErQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMAST 163
Cdd:cd07843  88 VEH-DLKSLMETMKQPFLQS-EVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLAREYGSPLKPYTQ 165
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 41055987 164 LIGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAFNAK 207
Cdd:cd07843 166 LVVTLWYRAPElLLGAKEYSTAIDMWSVGCIFAELLTKKPLFPGK 210
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
10-197 1.05e-25

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: 107.80  E-value: 1.05e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLK-HPNIVMYRESW-EGEDCqlYIVMGFCeGG 87
Cdd:cd07832   8 IGEGAHGIVFKAKDRETGETVALKKVALRKLEGGIPNQALREIKALQACQgHPYVVKLRDVFpHGTGF--VLVFEYM-LS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  88 DLYHRLKQQKgELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMA-STLIG 166
Cdd:cd07832  85 SLSEVLRDEE-RPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLARLFSEEDPRLySHQVA 163
                       170       180       190
                ....*....|....*....|....*....|..
gi 41055987 167 TPYYMSPELFSNKP-YNYKSDVWALGCCVYEM 197
Cdd:cd07832 164 TRWYRAPELLYGSRkYDEGVDLWAVGCIFAEL 195
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
6-256 1.12e-25

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


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 107.15  E-value: 1.12e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   6 FVRVVGKGSYGEVNLVRHKSDRkQYVIKKLnlrtssrRERRAAE----QEAQLLSQLKHPNIV-MYresweG---EDCQL 77
Cdd:cd05059   8 FLKELGSGQFGVVHLGKWRGKI-DVAIKMI-------KEGSMSEddfiEEAKVMMKLSHPKLVqLY-----GvctKQRPI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  78 YIVMGFCEGGDLYHRLKQQKGELLPErQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIAR-VLEN 156
Cdd:cd05059  75 FIVTEYMANGCLLNYLRERRGKFQTE-QLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLARyVLDD 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 157 QNdMASTliGTPY---YMSPELFSNKPYNYKSDVWALGCCVYEMATL-KHAFNAKDMNSLVYRIVEG-KLPQmPSKYDPQ 231
Cdd:cd05059 154 EY-TSSV--GTKFpvkWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSEgKMPYERFSNSEVVEHISQGyRLYR-PHLAPTE 229
                       250       260
                ....*....|....*....|....*
gi 41055987 232 LGELIKRMLCKKPEDRPDVKHILRQ 256
Cdd:cd05059 230 VYTIMYSCWHEKPEERPTFKILLSQ 254
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
2-243 1.38e-25

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: 110.10  E-value: 1.38e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAA-EQEAQLLSQLKHPNIVMYRESWEGEDcQLYIV 80
Cdd:cd05624  72 DDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRAETACfREERNVLVNGDCQWITTLHYAFQDEN-YLYLV 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MGFCEGGDLYHRLKQQKgELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLG-IARVLENQND 159
Cdd:cd05624 151 MDYYVGGDLLTLLSKFE-DKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFGsCLKMNDDGTV 229
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 160 MASTLIGTPYYMSPELFSNK-----PYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEG----KLPQMPSKYDP 230
Cdd:cd05624 230 QSSVAVGTPDYISPEILQAMedgmgKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHeerfQFPSHVTDVSE 309
                       250
                ....*....|...
gi 41055987 231 QLGELIKRMLCKK 243
Cdd:cd05624 310 EAKDLIQRLICSR 322
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
10-261 1.40e-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: 106.64  E-value: 1.40e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNlrtSSRRERRAAEQEAQLLSQLK-HPNIV-MYRESWEGEDCqlYI-VMGFCEG 86
Cdd:cd13987   1 LGEGTYGKVLLAVHKGSGTKMALKFVP---KPSTKLKDFLREYNISLELSvHPHIIkTYDVAFETEDY--YVfAQEYAPY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  87 GDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNI--IKVGDLGIARvlenqndMASTL 164
Cdd:cd13987  76 GDLFSIIPPQVG--LPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDCrrVKLCDFGLTR-------RVGST 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 165 I----GTPYYMSPELFSNKPY-----NYKSDVWALGCCVYEMATLKHAFN-AKDMNSLVYRIVE---GKLPQMPSKYD-- 229
Cdd:cd13987 147 VkrvsGTIPYTAPEVCEAKKNegfvvDPSIDVWAFGVLLFCCLTGNFPWEkADSDDQFYEEFVRwqkRKNTAVPSQWRrf 226
                       250       260       270
                ....*....|....*....|....*....|...
gi 41055987 230 -PQLGELIKRMLCKKPEDRPDVKHILRqpYIKH 261
Cdd:cd13987 227 tPKALRMFKKLLAPEPERRCSIKEVFK--YLGD 257
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
2-261 1.43e-25

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: 110.09  E-value: 1.43e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLN-LRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEgEDCQLYIV 80
Cdd:cd05622  73 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSkFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQ-DDRYLYMV 151
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MGFCEGGDLYHRLKQQKgelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLeNQNDM 160
Cdd:cd05622 152 MEYMPGGDLVNLMSNYD---VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKM-NKEGM 227
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 161 A--STLIGTPYYMSPELFSNKP----YNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKlPQMPSKYDPQLGE 234
Cdd:cd05622 228 VrcDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHK-NSLTFPDDNDISK 306
                       250       260       270
                ....*....|....*....|....*....|...
gi 41055987 235 LIKRMLCKKPEDRP------DVKHILRQPYIKH 261
Cdd:cd05622 307 EAKNLICAFLTDREvrlgrnGVEEIKRHLFFKN 339
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
1-260 1.80e-25

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: 106.87  E-value: 1.80e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   1 MDGYLFVRVVGKGSYGEVNLVRHKsdrKQYVIKKLNLRTSSRRERRAAE----QEAQLLSQLKHPNIV-MYreSWEGEDC 75
Cdd:cd14117   5 IDDFDIGRPLGKGKFGNVYLAREK---QSKFIVALKVLFKSQIEKEGVEhqlrREIEIQSHLRHPNILrLY--NYFHDRK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  76 QLYIVMGFCEGGDLYHRLkqQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIArvLE 155
Cdd:cd14117  80 RIYLILEYAPRGELYKEL--QKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWS--VH 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 156 NQNDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLpQMPSKYDPQLGEL 235
Cdd:cd14117 156 APSLRRRTMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVDL-KFPPFLSDGSRDL 234
                       250       260
                ....*....|....*....|....*
gi 41055987 236 IKRMLCKKPEDRPDVKHILRQPYIK 260
Cdd:cd14117 235 ISKLLRYHPSERLPLKGVMEHPWVK 259
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
10-254 1.85e-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: 1.85e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDrkqYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEdcQLYIVMGFCEGGDL 89
Cdd:cd14150   8 IGTGSFGTVFRGKWHGD---VAVKILKVTEPTPEQLQAFKNEMQVLRKTRHVNILLFMGFMTRP--NFAIITQWCEGSSL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  90 YHRLK--QQKGELLperQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVL-----ENQNDMAS 162
Cdd:cd14150  83 YRHLHvtETRFDTM---QLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLATVKtrwsgSQQVEQPS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 163 tliGTPYYMSPELF---SNKPYNYKSDVWALGCCVYEM--ATLKHAfNAKDMNSLVYRIVEGKLPQMPSKYDPQLGELIK 237
Cdd:cd14150 160 ---GSILWMAPEVIrmqDTNPYSFQSDVYAYGVVLYELmsGTLPYS-NINNRDQIIFMVGRGYLSPDLSKLSSNCPKAMK 235
                       250       260
                ....*....|....*....|.
gi 41055987 238 RMLCK----KPEDRPDVKHIL 254
Cdd:cd14150 236 RLLIDclkfKREERPLFPQIL 256
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
6-200 2.25e-25

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


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 106.70  E-value: 2.25e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   6 FVRVVGKGSYGEVNLVRHK----SDRKQYVIKKLNlRTSSRRERRAAEQEAQLLSQLKHPNIVMYRE-SWEGEDCQLYIV 80
Cdd:cd05038   8 FIKQLGEGHFGSVELCRYDplgdNTGEQVAVKSLQ-PSGEEQHMSDFKREIEILRTLDHEYIVKYKGvCESPGRRSLRLI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MGFCEGGDLYHRLKQQKGELLpERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQND- 159
Cdd:cd05038  87 MEYLPSGSLRDYLQRHRDQID-LKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAKVLPEDKEy 165
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 41055987 160 -MASTLIGTP-YYMSPELFSNKPYNYKSDVWALGCCVYEMATL 200
Cdd:cd05038 166 yYVKEPGESPiFWYAPECLRESRFSSASDVWSFGVTLYELFTY 208
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
10-260 2.34e-25

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: 107.07  E-value: 2.34e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERR-AAEQEAQLLSQlKHPNIVMYRES--WEGeDCqlYIVMGFCEG 86
Cdd:cd06616  14 IGRGAFGTVNKMLHKPSGTIMAVKRIRSTVDEKEQKRlLMDLDVVMRSS-DCPYIVKFYGAlfREG-DC--WICMELMDI 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  87 G--DLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEK-HILHRDLKTQNIFLTKTNIIKVGDLGIARVLenQNDMAST 163
Cdd:cd06616  90 SldKFYKYVYEVLDSVIPEEILGKIAVATVKALNYLKEElKIIHRDVKPSNILLDRNGNIKLCDFGISGQL--VDSIAKT 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 164 L-IGTPYYMSPELF----SNKPYNYKSDVWALGCCVYEMATLKHAFNAkdMNSL---VYRIVEGKLPQMPS----KYDPQ 231
Cdd:cd06616 168 RdAGCRPYMAPERIdpsaSRDGYDVRSDVWSLGITLYEVATGKFPYPK--WNSVfdqLTQVVKGDPPILSNseerEFSPS 245
                       250       260
                ....*....|....*....|....*....
gi 41055987 232 LGELIKRMLCKKPEDRPDVKHILRQPYIK 260
Cdd:cd06616 246 FVNFVNLCLIKDESKRPKYKELLKHPFIK 274
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
7-258 2.40e-25

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: 106.82  E-value: 2.40e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   7 VRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEG 86
Cdd:cd07860   5 VEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTEN-KLYLVFEFLHQ 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  87 gDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLIG 166
Cdd:cd07860  84 -DLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEVV 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 167 TPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIV--------------------EGKLPQMP 225
Cdd:cd07860 163 TLWYRAPEiLLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFrtlgtpdevvwpgvtsmpdyKPSFPKWA 242
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 41055987 226 ----SKYDPQLGE----LIKRMLCKKPEDRPDVKHILRQPY 258
Cdd:cd07860 243 rqdfSKVVPPLDEdgrdLLSQMLHYDPNKRISAKAALAHPF 283
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
7-247 3.30e-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: 106.34  E-value: 3.30e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   7 VRVVGKGSYGEVNLVRHKSDRKQYVIKKLN---LRTSSRRERRAAEQEaqLLSQLKHPNIVMYRESWEGEDcQLYIVMGF 83
Cdd:cd05609   5 IKLISNGAYGAVYLVRHRETRQRFAMKKINkqnLILRNQIQQVFVERD--ILTFAENPFVVSMYCSFETKR-HLCMVMEY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGGDLYHRLKqqKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARV---------- 153
Cdd:cd05609  82 VEGGDCATLLK--NIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSKIglmslttnly 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 154 -----LENQNDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKL--PQMPS 226
Cdd:cd05609 160 eghieKDTREFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIewPEGDD 239
                       250       260
                ....*....|....*....|.
gi 41055987 227 KYDPQLGELIKRMLCKKPEDR 247
Cdd:cd05609 240 ALPDDAQDLITRLLQQNPLER 260
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
10-260 5.01e-25

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: 106.09  E-value: 5.01e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAeQEAQLLSQLKHPNIVMYRESWEGEDCqLYIVMGFCEGGD- 88
Cdd:cd06622   9 LGKGNYGSVYKVLHRPTGVTMAMKEIRLELDESKFNQII-MELDILHKAVSPYIVDFYGAFFIEGA-VYMCMEYMDAGSl 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  89 --LYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKH-ILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQndMASTLI 165
Cdd:cd06622  87 dkLYAGGVATEG--IPEDVLRRITYAVVKGLKFLKEEHnIIHRDVKPTNVLVNGNGQVKLCDFGVSGNLVAS--LAKTNI 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 166 GTPYYMSPELFS------NKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYR---IVEGKLPQMPSKYDPQLGELI 236
Cdd:cd06622 163 GCQSYMAPERIKsggpnqNPTYTVQSDVWSLGLSILEMALGRYPYPPETYANIFAQlsaIVDGDPPTLPSGYSDDAQDFV 242
                       250       260
                ....*....|....*....|....
gi 41055987 237 KRMLCKKPEDRPDVKHILRQPYIK 260
Cdd:cd06622 243 AKCLNKIPNRRPTYAQLLEHPWLV 266
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
1-261 5.74e-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: 106.93  E-value: 5.74e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   1 MDGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLN---LRTSSRRERRAAEQEAQLLSqLKHPNIVMYRESWEGEDcQL 77
Cdd:cd05619   4 IEDFVLHKMLGKGSFGKVFLAELKGTNQFFAIKALKkdvVLMDDDVECTMVEKRVLSLA-WEHPFLTHLFCTFQTKE-NL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  78 YIVMGFCEGGDLYHRLKQQKGELLPerQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQ 157
Cdd:cd05619  82 FFVMEYLNGGDLMFHIQSCHKFDLP--RATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKENMLG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 158 NDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLvYRIVEGKLPQMPSKYDPQLGELIK 237
Cdd:cd05619 160 DAKTSTFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEEL-FQSIRMDNPFYPRWLEKEAKDILV 238
                       250       260
                ....*....|....*....|....*
gi 41055987 238 RMLCKKPEDRPDVKHILRQ-PYIKH 261
Cdd:cd05619 239 KLFVREPERRLGVRGDIRQhPFFRE 263
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
8-256 5.90e-25

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


Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 105.19  E-value: 5.90e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEV------NLVRHKSDRKQYVIKKLNlRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDCQlYIVM 81
Cdd:cd05044   1 KFLGSGAFGEVfegtakDILGDGSGETKVAVKTLR-KGATDQEKAEFLKEAHLMSNFKHPNILKLLGVCLDNDPQ-YIIL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  82 GFCEGGDLYHRLKQQKGE-----LLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTN----IIKVGDLGIAR 152
Cdd:cd05044  79 ELMEGGDLLSYLRAARPTaftppLLTLKDLLSICVDVAKGCVYLEDMHFVHRDLAARNCLVSSKDyrerVVKIGDFGLAR 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 153 VLEnQNDmastligtpYY------------MSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIV--E 218
Cdd:cd05044 159 DIY-KND---------YYrkegegllpvrwMAPESLVDGVFTTQSDVWAFGVLMWEILTLGQQPYPARNNLEVLHFVraG 228
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 41055987 219 GKLPQMPSKYDpQLGELIKRMLCKKPEDRPDVKHILRQ 256
Cdd:cd05044 229 GRLDQPDNCPD-DLYELMLRCWSTDPEERPSFARILEQ 265
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
9-256 8.84e-25

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: 104.73  E-value: 8.84e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   9 VVGKGSYGEV-------NLVRHKSDRkQYVIKKLNLRTSSRRerraaeQEAQLLSQLKHPNIVMYRESWEgEDCQLYIVM 81
Cdd:cd14147  10 VIGIGGFGKVyrgswrgELVAVKAAR-QDPDEDISVTAESVR------QEARLFAMLAHPNIIALKAVCL-EEPNLCLVM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  82 GFCEGGDLYHRLKqqkGELLPERQVVEWFVQIAMALQYLHEKHI---LHRDLKTQNIFLTKTNI--------IKVGDLGI 150
Cdd:cd14147  82 EYAAGGPLSRALA---GRRVPPHVLVNWAVQIARGMHYLHCEALvpvIHRDLKSNNILLLQPIEnddmehktLKITDFGL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 151 ARVLENQNDMASTliGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLP-QMPSKYD 229
Cdd:cd14147 159 AREWHKTTQMSAA--GTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRGIDCLAVAYGVAVNKLTlPIPSTCP 236
                       250       260
                ....*....|....*....|....*..
gi 41055987 230 PQLGELIKRMLCKKPEDRPDVKHILRQ 256
Cdd:cd14147 237 EPFAQLMADCWAQDPHRRPDFASILQQ 263
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
10-259 9.68e-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: 105.05  E-value: 9.68e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLN-----------LRTSSRRERRAAE-------------QEAQLLSQLKHPNIVM 65
Cdd:cd14199  10 IGKGSYGVVKLAYNEDDNTYYAMKVLSkkklmrqagfpRRPPPRGARAAPEgctqprgpiervyQEIAILKKLDHPNVVK 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  66 YRESWE--GEDcQLYIVMGFCEGGDLyhrLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNII 143
Cdd:cd14199  90 LVEVLDdpSED-HLYMVFELVKQGPV---MEVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLVGEDGHI 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 144 KVGDLGIARVLENQNDMASTLIGTPYYMSPELFSNKPYNYKS---DVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGK 220
Cdd:cd14199 166 KIADFGVSNEFEGSDALLTNTVGTPAFMAPETLSETRKIFSGkalDVWAMGVTLYCFVFGQCPFMDERILSLHSKIKTQP 245
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 41055987 221 LpQMPSKYD--PQLGELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd14199 246 L-EFPDQPDisDDLKDLLFRMLDKNPESRISVPEIKLHPWV 285
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
7-262 1.10e-24

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: 105.90  E-value: 1.10e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   7 VRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRER-RAAEQEAQLLSQLKHPNIVMYRESWEGEDCQlYIVMGFCE 85
Cdd:cd06635  30 LREIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEKwQDIIKEVKFLQRIKHPNSIEYKGCYLREHTA-WLVMEYCL 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  86 GG--DLYHRLKQQkgelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNdmasT 163
Cdd:cd06635 109 GSasDLLEVHKKP----LQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIASPAN----S 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 164 LIGTPYYMSPEL---FSNKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLvYRIVEGKLPQMPS-KYDPQLGELIKR 238
Cdd:cd06635 181 FVGTPYWMAPEVilaMDEGQYDGKVDVWSLGITCIELAERKPPlFNMNAMSAL-YHIAQNESPTLQSnEWSDYFRNFVDS 259
                       250       260
                ....*....|....*....|....
gi 41055987 239 MLCKKPEDRPDVKHILRQPYIKHQ 262
Cdd:cd06635 260 CLQKIPQDRPTSEELLKHMFVLRE 283
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
7-247 1.33e-24

Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The DMPK-like subfamily is composed of DMPK and DMPK-related cell division control protein 42 (Cdc42) binding kinase (MRCK). DMPK is expressed in skeletal and cardiac muscles, and in central nervous tissues. The functional role of DMPK is not fully understood. It may play a role in the signal transduction and homeostasis of calcium. The DMPK gene is implicated in myotonic dystrophy 1 (DM1), an inherited multisystemic disorder with symptoms that include muscle hyperexcitability, progressive muscle weakness and wasting, cataract development, testicular atrophy, and cardiac conduction defects. The genetic basis for DM1 is the mutational expansion of a CTG repeat in the 3'-UTR of DMPK. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. The DMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 105.89  E-value: 1.33e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   7 VRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQE---------AQLLSQLKHpnivmyreSWEGEDcQL 77
Cdd:cd05597   6 LKVIGRGAFGEVAVVKLKSTEKVYAMKILNKWEMLKRAETACFREerdvlvngdRRWITKLHY--------AFQDEN-YL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  78 YIVMGFCEGGDLYHRLKQQkGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLG-IARVLEN 156
Cdd:cd05597  77 YLVMDYYCGGDLLTLLSKF-EDRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFGsCLKLRED 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 157 QNDMASTLIGTPYYMSPELF-----SNKPYNYKSDVWALGCCVYEMATLKHAFNAKdmnSLV--Y-RIVEGK----LPQM 224
Cdd:cd05597 156 GTVQSSVAVGTPDYISPEILqamedGKGRYGPECDWWSLGVCMYEMLYGETPFYAE---SLVetYgKIMNHKehfsFPDD 232
                       250       260
                ....*....|....*....|...
gi 41055987 225 PSKYDPQLGELIKRMLCkKPEDR 247
Cdd:cd05597 233 EDDVSEEAKDLIRRLIC-SRERR 254
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
2-261 1.60e-24

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called 90kDa ribosomal protein S6 kinase 3 or Ribosomal protein S6 kinase alpha-3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK2 is also called p90RSK3, RPS6KA3, S6K-alpha-3, or MAPK-activated protein kinase 1b (MAPKAPK-1b). RSK2 is expressed highly in the regions of the brain with high synaptic activity. It plays a role in the maintenance and consolidation of excitatory synapses. It is a specific modulator of phospholipase D in calcium-regulated exocytosis. Mutations in the RSK2 gene, RPS6KA3, cause Coffin-Lowry syndrome (CLS), a rare syndromic form of X-linked mental retardation characterized by growth and psychomotor retardation and skeletal abnormalities. RSK2 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 105.87  E-value: 1.60e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNlrtssrRERRAAEQEAQLLSQL-KHPNIVMYRESWEgEDCQLYIV 80
Cdd:cd14176  19 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIID------KSKRDPTEEIEILLRYgQHPNIITLKDVYD-DGKYVYVV 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MGFCEGGDLYHRLKQQKgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTN----IIKVGDLGIARVLEN 156
Cdd:cd14176  92 TELMKGGELLDKILRQK--FFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAKQLRA 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 157 QNDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAF-NAKD--MNSLVYRIVEGKLPQMPSKYDP--- 230
Cdd:cd14176 170 ENGLLMTPCYTANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFaNGPDdtPEEILARIGSGKFSLSGGYWNSvsd 249
                       250       260       270
                ....*....|....*....|....*....|.
gi 41055987 231 QLGELIKRMLCKKPEDRPDVKHILRQPYIKH 261
Cdd:cd14176 250 TAKDLVSKMLHVDPHQRLTAALVLRHPWIVH 280
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
9-261 1.66e-24

Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CRIK (also called citron kinase) is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger, and a pleckstrin homology (PH) domain, in addition to other motifs. The CRIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 105.47  E-value: 1.66e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   9 VVGKGSYGEVNLVRHKSDRKQYVIKKLN-LRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEGG 87
Cdd:cd05601   8 VIGRGHFGEVQVVKEKATGDIYAMKVLKkSETLAQEEVSFFEEERDIMAKANSPWITKLQYAFQDSE-NLYLVMEYHPGG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  88 DLYHRLKQQKGeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTL-IG 166
Cdd:cd05601  87 DLLSLLSRYDD-IFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSAAKLSSDKTVTSKMpVG 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 167 TPYYMSPELFSNKPYNYKS------DVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGK----LPQMPsKYDPQLGELI 236
Cdd:cd05601 166 TPDYIAPEVLTSMNGGSKGtygvecDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIMNFKkflkFPEDP-KVSESAVDLI 244
                       250       260
                ....*....|....*....|....*
gi 41055987 237 KRMLCkKPEDRPDVKHILRQPYIKH 261
Cdd:cd05601 245 KGLLT-DAKERLGYEGLCCHPFFSG 268
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
6-240 1.66e-24

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 105.83  E-value: 1.66e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987    6 FVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAE--QEAQLLSQLKHPNIVMYRESWEgEDCQLYIVMGF 83
Cdd:PTZ00426  34 FIRTLGTGSFGRVILATYKNEDFPPVAIKRFEKSKIIKQKQVDHvfSERKILNYINHPFCVNLYGSFK-DESYLYLVLEF 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   84 CEGGDLYHRLKQQKgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQndmAST 163
Cdd:PTZ00426 113 VIGGEFFTFLRRNK--RFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFAKVVDTR---TYT 187
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41055987  164 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLpQMPSKYDPQLGELIKRML 240
Cdd:PTZ00426 188 LCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFYANEPLLIYQKILEGII-YFPKFLDNNCKHLMKKLL 263
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
10-258 1.67e-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: 104.29  E-value: 1.67e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIV-----MYRESwegedcQLYIVMGFC 84
Cdd:cd07835   7 IGEGTYGVVYKARDKLTGEIVALKKIRLETEDEGVPSTAIREISLLKELNHPNIVrlldvVHSEN------KLYLVFEFL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  85 EGgDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARV----LENQNDM 160
Cdd:cd07835  81 DL-DLKKYMDSSPLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLARAfgvpVRTYTHE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 161 ASTLigtpYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRI--------------VEG------ 219
Cdd:cd07835 160 VVTL----WYRAPEiLLGSKHYSTPVDIWSVGCIFAEMVTRRPLFPGDSEIDQLFRIfrtlgtpdedvwpgVTSlpdykp 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 41055987 220 KLPQMPSK--------YDPQLGELIKRMLCKKPEDRPDVKHILRQPY 258
Cdd:cd07835 236 TFPKWARQdlskvvpsLDEDGLDLLSQMLVYDPAKRISAKAALQHPY 282
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
1-259 1.94e-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: 103.43  E-value: 1.94e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   1 MDGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNlrTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEgEDCQLYIV 80
Cdd:cd14114   1 YDHYDILEELGTGAFGVVHRCTERATGNNFAAKFIM--TPHESDKETVRKEIQIMNQLHHPKLINLHDAFE-DDNEMVLI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MGFCEGGDLYHRLKQQkGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLT--KTNIIKVGDLGIARVLeNQN 158
Cdd:cd14114  78 LEFLSGGELFERIAAE-HYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTtkRSNEVKLIDFGLATHL-DPK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 159 DMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRI--VEGKLPQMPSKY-DPQLGEL 235
Cdd:cd14114 156 ESVKVTTGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVksCDWNFDDSAFSGiSEEAKDF 235
                       250       260
                ....*....|....*....|....
gi 41055987 236 IKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd14114 236 IRKLLLADPNKRMTIHQALEHPWL 259
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
8-259 2.66e-24

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: 103.70  E-value: 2.66e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKQYVIKKLnlrtssrRERRAAEQEAQLLSQLK-HPNIV----MYRES--WEGED---CQL 77
Cdd:cd14171  12 QKLGTGISGPVRVCVKKSTGERFALKIL-------LDRPKARTEVRLHMMCSgHPNIVqiydVYANSvqFPGESsprARL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  78 YIVMGFCEGGDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTN---IIKVGDLGIARVl 154
Cdd:cd14171  85 LIVMELMEGGELFDRISQHRH--FTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSedaPIKLCDFGFAKV- 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 155 ENQNDMASTLigTPYYMSPELF---------------SNKPYNY-KS-DVWALGCCVYEMATLKHAFNAKDMNSLVYRIV 217
Cdd:cd14171 162 DQGDLMTPQF--TPYYVAPQVLeaqrrhrkersgiptSPTPYTYdKScDMWSLGVIIYIMLCGYPPFYSEHPSRTITKDM 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 41055987 218 EGKLpqMPSKYD----------PQLGELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd14171 240 KRKI--MTGSYEfpeeewsqisEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
2-275 2.80e-24

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: 104.37  E-value: 2.80e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRA-----AEQEAQLLSQLKHPNIVMYRESWEGEDCQ 76
Cdd:cd14041   6 DRYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIHQLNKNWRDEKKEnyhkhACREYRIHKELDHPRIVKLYDYFSLDTDS 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  77 LYIVMGFCEGGDLYHRLKQQKgeLLPERQVVEWFVQIAMALQYLHEKH--ILHRDLKTQNIFL---TKTNIIKVGDLGIA 151
Cdd:cd14041  86 FCTVLEYCEGNDLDFYLKQHK--LMSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLvngTACGEIKITDFGLS 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 152 RVLENQN-------DMASTLIGTPYYMSPELF--SNKP--YNYKSDVWALGC----CVYEMATLKHAFNAKDM--NSLVY 214
Cdd:cd14041 164 KIMDDDSynsvdgmELTSQGAGTYWYLPPECFvvGKEPpkISNKVDVWSVGVifyqCLYGRKPFGHNQSQQDIlqENTIL 243
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41055987 215 RIVEGKLPQMPSkYDPQLGELIKRMLCKKPEDRPDVKHILRQPYIKHQISMFLEATKEKTA 275
Cdd:cd14041 244 KATEVQFPPKPV-VTPEAKAFIRRCLAYRKEDRIDVQQLACDPYLLPHIRKSVSTSSPAGA 303
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
7-248 2.81e-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: 103.04  E-value: 2.81e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   7 VRVVGKGSYGEVNLVRHKSDRKqYVIKKLNLRTSSRRerrAAEQEAQLLSQLKHPNIVMYRESWEGEdcQLYIVMGFCEG 86
Cdd:cd05067  12 VERLGAGQFGEVWMGYYNGHTK-VAIKSLKQGSMSPD---AFLAEANLMKQLQHQRLVRLYAVVTQE--PIYIITEYMEN 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  87 GDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLIG 166
Cdd:cd05067  86 GSLVDFLKTPSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLIEDNEYTAREGAK 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 167 TPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEG--KLPQmPSKYDPQLGELIKRMLCKK 243
Cdd:cd05067 166 FPIkWTAPEAINYGTFTIKSDVWSFGILLTEIVTHGRIPYPGMTNPEVIQNLERgyRMPR-PDNCPEELYQLMRLCWKER 244

                ....*
gi 41055987 244 PEDRP 248
Cdd:cd05067 245 PEDRP 249
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
4-261 2.98e-24

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: 105.85  E-value: 2.98e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRA-AEQEAQLLSQLKHPNIVMYRESWEgEDCQLYIVMG 82
Cdd:cd05621  54 YDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSAfFWEERDIMAFANSPWVVQLFCAFQ-DDKYLYMVME 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FCEGGDLYHRLKQQKgelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLEnQNDMA- 161
Cdd:cd05621 133 YMPGGDLVNLMSNYD---VPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGTCMKMD-ETGMVh 208
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 162 -STLIGTPYYMSPELFSNKP----YNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGK----LPQmpskyDPQL 232
Cdd:cd05621 209 cDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMDHKnslnFPD-----DVEI 283
                       250       260       270
                ....*....|....*....|....*....|....*
gi 41055987 233 GELIKRMLCKKPEDRP------DVKHILRQPYIKH 261
Cdd:cd05621 284 SKHAKNLICAFLTDREvrlgrnGVEEIKQHPFFRN 318
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
9-255 2.99e-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: 103.20  E-value: 2.99e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   9 VVGKGSYGEVNLVRHKSDrkqYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESwegedC----QLYIVMGFC 84
Cdd:cd14063   7 VIGKGRFGRVHRGRWHGD---VAIKLLNIDYLNEEQLEAFKEEVAAYKNTRHDNLVLFMGA-----CmdppHLAIVTSLC 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  85 EGGDLYHRLKQQKgELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIkVGDLGIARV--LENQNDMAS 162
Cdd:cd14063  79 KGRTLYSLIHERK-EKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLENGRVV-ITDFGLFSLsgLLQPGRRED 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 163 TLI---GTPYYMSPEL----------FSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKlpqMPSKYD 229
Cdd:cd14063 157 TLVipnGWLCYLAPEIiralspdldfEESLPFTKASDVYAFGTVWYELLAGRWPFKEQPAESIIWQVGCGK---KQSLSQ 233
                       250       260       270
                ....*....|....*....|....*....|
gi 41055987 230 PQLGELIKR--MLC--KKPEDRPDVKHILR 255
Cdd:cd14063 234 LDIGREVKDilMQCwaYDPEKRPTFSDLLR 263
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
50-248 3.02e-24

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: 102.75  E-value: 3.02e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  50 QEAQLLSQLKHPNIV-MYRESWEGEdcQLYIVMGFCEGGDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHR 128
Cdd:cd05034  39 QEAQIMKKLRHDKLVqLYAVCSDEE--PIYIVTELMSKGSLLDYLRTGEGRALRLPQLIDMAAQIASGMAYLESRNYIHR 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 129 DLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLIGTPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAK 207
Cdd:cd05034 117 DLAARNILVGENNVCKVADFGLARLIEDDEYTAREGAKFPIkWTAPEAALYGRFTIKSDVWSFGILLYEIVTYGRVPYPG 196
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 41055987 208 DMNSLVYRIVEG--KLPqMPSKYDPQLGELIKRMLCKKPEDRP 248
Cdd:cd05034 197 MTNREVLEQVERgyRMP-KPPGCPDELYDIMLQCWKKEPEERP 238
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
8-259 3.74e-24

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 (also called STK17A) and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. Rabbit DRAK1 has been shown to induce apoptosis in osteoclasts and overexpressio of human DRAK1 induces apoptosis in cultured fibroblast cells. DRAK1 may be involved in apoptotic signaling. The DRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 103.09  E-value: 3.74e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLK-HPNIVMYRESWEGEDcQLYIVMGFCEG 86
Cdd:cd14197  15 RELGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQDCRMEIIHEIAVLELAQaNPWVINLHEVYETAS-EMILVLEYAAG 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  87 GDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNI---IKVGDLGIARVLENQNDMASt 163
Cdd:cd14197  94 GEIFNQCVADREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESPlgdIKIVDFGLSRILKNSEELRE- 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 164 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPSKYDPQLG---ELIKRML 240
Cdd:cd14197 173 IMGTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQMNVSYSEEEFEHLSEsaiDFIKTLL 252
                       250
                ....*....|....*....
gi 41055987 241 CKKPEDRPDVKHILRQPYI 259
Cdd:cd14197 253 IKKPENRATAEDCLKHPWL 271
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
10-260 4.85e-24

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: 104.19  E-value: 4.85e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRA---AEQEAQLLSQLKH-PNIVMYRESWEgEDCQLYIVMGFCE 85
Cdd:cd05586   1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVAKKEVAhtiGERNILVRTALDEsPFIVGLKFSFQ-TPTDLYLVTDYMS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  86 GGDLYHRLkqQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLI 165
Cdd:cd05586  80 GGELFWHL--QKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSKADLTDNKTTNTFC 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 166 GTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLpQMPSKYDPQLG-ELIKRMLCKK 243
Cdd:cd05586 158 GTTEYLAPEvLLDEKGYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKV-RFPKDVLSDEGrSFVKGLLNRN 236
                       250       260
                ....*....|....*....|.
gi 41055987 244 PEDR----PDVKHILRQPYIK 260
Cdd:cd05586 237 PKHRlgahDDAVELKEHPFFA 257
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
4-258 5.11e-24

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2, group 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 102.37  E-value: 5.11e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLnlrtsSRRERRAAEQEAQLLSQ--LKHPNIVMYRESWEgEDCQLYIVM 81
Cdd:cd14665   2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYI-----ERGEKIDENVQREIINHrsLRHPNIVRFKEVIL-TPTHLAIVM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  82 GFCEGGDLYHRLKQqkGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNI--IKVGDLGIAR--VLENQ 157
Cdd:cd14665  76 EYAAGGELFERICN--AGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAprLKICDFGYSKssVLHSQ 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 158 ndmASTLIGTPYYMSPELFSNKPYNYK-SDVWALGCCVYEMATLKHAF----NAKDMNSLVYRI--VEGKLPQMpSKYDP 230
Cdd:cd14665 154 ---PKSTVGTPAYIAPEVLLKKEYDGKiADVWSCGVTLYVMLVGAYPFedpeEPRNFRKTIQRIlsVQYSIPDY-VHISP 229
                       250       260
                ....*....|....*....|....*...
gi 41055987 231 QLGELIKRMLCKKPEDRPDVKHILRQPY 258
Cdd:cd14665 230 ECRHLISRIFVADPATRITIPEIRNHEW 257
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
6-247 5.26e-24

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: 104.23  E-value: 5.26e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   6 FVRVVGKGSYGEVNLVRH------------KSDRKQYVIKKLNLRTSSRRERRAAEQEAQllsqlkHPNIVMYRESWEgE 73
Cdd:cd05614   4 LLKVLGTGAYGKVFLVRKvsghdanklyamKVLRKAALVQKAKTVEHTRTERNVLEHVRQ------SPFLVTLHYAFQ-T 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  74 DCQLYIVMGFCEGGDLYHRLKQQkgELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIAR- 152
Cdd:cd05614  77 DAKLHLILDYVSGGELFTHLYQR--DHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSKe 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 153 VLENQNDMASTLIGTPYYMSPELFSNKPYNYKS-DVWALGCCVYEMATLKHAFN---AKDMNSLVYRIVEGKLPQMPSKY 228
Cdd:cd05614 155 FLTEEKERTYSFCGTIEYMAPEIIRGKSGHGKAvDWWSLGILMFELLTGASPFTlegEKNTQSEVSRRILKCDPPFPSFI 234
                       250
                ....*....|....*....
gi 41055987 229 DPQLGELIKRMLCKKPEDR 247
Cdd:cd05614 235 GPVARDLLQKLLCKDPKKR 253
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
7-243 6.75e-24

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


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 105.10  E-value: 6.75e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   7 VRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAA-EQEAQLLSQLKHPNIVMYRESWEgEDCQLYIVMGFCE 85
Cdd:cd05623  77 LKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAETACfREERDVLVNGDSQWITTLHYAFQ-DDNNLYLVMDYYV 155
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  86 GGDLYHRLKQQKgELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLG-IARVLENQNDMASTL 164
Cdd:cd05623 156 GGDLLTLLSKFE-DRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGsCLKLMEDGTVQSSVA 234
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 165 IGTPYYMSPELFS-----NKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGK----LPQMPSKYDPQLGEL 235
Cdd:cd05623 235 VGTPDYISPEILQamedgKGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKerfqFPTQVTDVSENAKDL 314

                ....*...
gi 41055987 236 IKRMLCKK 243
Cdd:cd05623 315 IRRLICSR 322
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
8-260 7.12e-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: 103.49  E-value: 7.12e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKQYVIKKLN---LRTSSRRERRAAEQEAQLLSqLKHPNIVMYRESWEGEDcQLYIVMGFC 84
Cdd:cd05620   1 KVLGKGSFGKVLLAELKGKGEYFAVKALKkdvVLIDDDVECTMVEKRVLALA-WENPFLTHLYCTFQTKE-HLFFVMEFL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  85 EGGDLYHRLkQQKGELLPERQVVeWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTL 164
Cdd:cd05620  79 NGGDLMFHI-QDKGRFDLYRATF-YAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKENVFGDNRASTF 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 165 IGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLvYRIVEGKLPQMPSKYDPQLGELIKRMLCKKP 244
Cdd:cd05620 157 CGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDEL-FESIRVDTPHYPRWITKESKDILEKLFERDP 235
                       250
                ....*....|....*..
gi 41055987 245 EDRPDVKHILR-QPYIK 260
Cdd:cd05620 236 TRRLGVVGNIRgHPFFK 252
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
4-260 1.21e-23

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: 103.02  E-value: 1.21e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKL-----NlRTSSRRERRaaeqEAQLLSQLK-HPNIV----MYRESwegE 73
Cdd:cd07852   9 YEILKKLGKGAYGIVWKAIDKKTGEVVALKKIfdafrN-ATDAQRTFR----EIMFLQELNdHPNIIkllnVIRAE---N 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  74 DCQLYIVMGFCEGgDLYHRLKqqKGELLP-ERQVVEWfvQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIAR 152
Cdd:cd07852  81 DKDIYLVFEYMET-DLHAVIR--ANILEDiHKQYIMY--QLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGLAR 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 153 VLENQNDMASTLIGTPY-----YMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAF-NAKDMNSLVyRIVEG------ 219
Cdd:cd07852 156 SLSQLEEDDENPVLTDYvatrwYRAPEiLLGSTRYTKGVDMWSVGCILGEMLLGKPLFpGTSTLNQLE-KIIEVigrpsa 234
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41055987 220 ------------------------KLPQMPSKYDPQLGELIKRMLCKKPEDRPDVKHILRQPYIK 260
Cdd:cd07852 235 ediesiqspfaatmleslppsrpkSLDELFPKASPDALDLLKKLLVFNPNKRLTAEEALRHPYVA 299
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
4-258 1.31e-23

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: 101.73  E-value: 1.31e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEgEDCQLYIVMGF 83
Cdd:cd07861   2 YTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIRLESEEEGVPSTAIREISLLKELQHPNIVCLEDVLM-QENRLYLVFEF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGgDLYHRLKQ-QKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMAS 162
Cdd:cd07861  81 LSM-DLKKYLDSlPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARAFGIPVRVYT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 163 TLIGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVE-------------GKLPQMPSKY 228
Cdd:cd07861 160 HEVVTLWYRAPEvLLGSPRYSTPVDIWSIGTIFAEMATKKPLFHGDSEIDQLFRIFRilgtptediwpgvTSLPDYKNTF 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 41055987 229 D-----------PQLGE----LIKRMLCKKPEDRPDVKHILRQPY 258
Cdd:cd07861 240 PkwkkgslrtavKNLDEdgldLLEKMLIYDPAKRISAKKALVHPY 284
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
50-248 1.45e-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: 100.88  E-value: 1.45e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  50 QEAQLLSQLKHPNIVmyreswegedcQLY---------IVMGFCEGGDLYHRLKQQKGELLPERqVVEWFVQIAMALQYL 120
Cdd:cd05040  47 KEVNAMHSLDHPNLI-----------RLYgvvlssplmMVTELAPLGSLLDRLRKDQGHFLIST-LCDYAVQIANGMAYL 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 121 HEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMastligtpYYMS-----------PELFSNKPYNYKSDVWA 189
Cdd:cd05040 115 ESKRFIHRDLAARNILLASKDKVKIGDFGLMRALPQNEDH--------YVMQehrkvpfawcaPESLKTRKFSHASDVWM 186
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41055987 190 LGCCVYEMATLKH----AFNAKDMNSLVYRivEGKLPQMPSKYDPQLGELIKRMLCKKPEDRP 248
Cdd:cd05040 187 FGVTLWEMFTYGEepwlGLNGSQILEKIDK--EGERLERPDDCPQDIYNVMLQCWAHKPADRP 247
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
2-197 2.24e-23

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: 102.46  E-value: 2.24e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAA-EQEAQLLSQLKHPNIVMYRESWEgEDCQLYIV 80
Cdd:cd05596  26 EDFDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSKFEMIKRSDSAFfWEERDIMAHANSEWIVQLHYAFQ-DDKYLYMV 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MGFCEGGDLYHRLKQQKgelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIA-RVLENQND 159
Cdd:cd05596 105 MDYMPGGDLVNLMSNYD---VPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFGTCmKMDKDGLV 181
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 41055987 160 MASTLIGTPYYMSPELFSNKP----YNYKSDVWALGCCVYEM 197
Cdd:cd05596 182 RSDTAVGTPDYISPEVLKSQGgdgvYGRECDWWSVGVFLYEM 223
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
4-263 2.30e-23

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: 100.71  E-value: 2.30e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSsrrERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGF 83
Cdd:cd14104   2 YMIAEELGRGQFGIVHRCVETSSKKTYMAKFVKVKGA---DQVLVKKEISILNIARHRNILRLHESFESHE-ELVMIFEF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGGDLYHRLKQQKGELlPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLT--KTNIIKVGDLGIARVLEnQNDMA 161
Cdd:cd14104  78 ISGVDIFERITTARFEL-NEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCtrRGSYIKIIEFGQSRQLK-PGDKF 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 162 STLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPSKYDP---QLGELIKR 238
Cdd:cd14104 156 RLQYTSAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAEYAFDDEAFKNisiEALDFVDR 235
                       250       260
                ....*....|....*....|....*
gi 41055987 239 MLCKKPEDRPDVKHILRQPYIKHQI 263
Cdd:cd14104 236 LLVKERKSRMTAQEALNHPWLKQGM 260
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
22-254 2.35e-23

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: 101.32  E-value: 2.35e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  22 RHKSDRKQYVIKKLNLRTSSRR----ERRAAEqEAQLLSQLKHPNIVMYRESWEGEDCQLYIVMGFCE---GGDLYHRLK 94
Cdd:cd14001  23 RGGSSRSPWAVKKINSKCDKGQrslyQERLKE-EAKILKSLNHPNIVGFRAFTKSEDGSLCLAMEYGGkslNDLIEERYE 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  95 QQKGElLPERQVVEWFVQIAMALQYLH-EKHILHRDLKTQNIfLTKTN--IIKVGDLGIA----RVLENQNDMASTLIGT 167
Cdd:cd14001 102 AGLGP-FPAATILKVALSIARALEYLHnEKKILHGDIKSGNV-LIKGDfeSVKLCDFGVSlpltENLEVDSDPKAQYVGT 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 168 PYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLK--H-------------AFNAKDMNSLVYrivEGKLPQMPSKYDPQ 231
Cdd:cd14001 180 EPWKAKEaLEEGGVITDKADIFAYGLVLWEMMTLSvpHlnlldiedddedeSFDEDEEDEEAY---YGTLGTRPALNLGE 256
                       250       260       270
                ....*....|....*....|....*....|
gi 41055987 232 LGELIKRML-----C--KKPEDRPDVKHIL 254
Cdd:cd14001 257 LDDSYQKVIelfyaCtqEDPKDRPSAAHIV 286
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
6-253 2.39e-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: 100.50  E-value: 2.39e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   6 FVRVVGKGSYGEVNLVRHKSDRKqYVIKKLNLRTSSRRerrAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCE 85
Cdd:cd05072  11 LVKKLGAGQFGEVWMGYYNNSTK-VAVKTLKPGTMSVQ---AFLEEANLMKTLQHDKLVRLYAVVTKEE-PIYIITEYMA 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  86 GGDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLI 165
Cdd:cd05072  86 KGSLLDFLKSDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIEDNEYTAREGA 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 166 GTPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATL-KHAFNAKDMNSLVYRIVEG-KLPQMPSKYDpQLGELIKRMLCK 242
Cdd:cd05072 166 KFPIkWTAPEAINFGSFTIKSDVWSFGILLYEIVTYgKIPYPGMSNSDVMSALQRGyRMPRMENCPD-ELYDIMKTCWKE 244
                       250
                ....*....|.
gi 41055987 243 KPEDRPDVKHI 253
Cdd:cd05072 245 KAEERPTFDYL 255
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
9-195 2.72e-23

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK2 (or MYLK2) phosphorylates myosin regulatory light chain and controls the contraction of skeletal muscles. MLCK2 contains a single kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site. The MLCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 100.38  E-value: 2.72e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   9 VVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSsrRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEGGD 88
Cdd:cd14190  11 VLGGGKFGKVHTCTEKRTGLKLAAKVINKQNS--KDKEMVLLEIQVMNQLNHRNLIQLYEAIETPN-EIVLFMEYVEGGE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  89 LYHRLKQQKGELLPERQVVewFV-QIAMALQYLHEKHILHRDLKTQNIFLTKT--NIIKVGDLGIARVLeNQNDMASTLI 165
Cdd:cd14190  88 LFERIVDEDYHLTEVDAMV--FVrQICEGIQFMHQMRVLHLDLKPENILCVNRtgHQVKIIDFGLARRY-NPREKLKVNF 164
                       170       180       190
                ....*....|....*....|....*....|
gi 41055987 166 GTPYYMSPELFSNKPYNYKSDVWALGCCVY 195
Cdd:cd14190 165 GTPEFLSPEVVNYDQVSFPTDMWSMGVITY 194
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
6-256 3.04e-23

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: 100.02  E-value: 3.04e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   6 FVRVVGKGSYGEVNLVRHKSDRKqYVIKklNLRTSSRRERRAAEqEAQLLSQLKHPNIV-MYRESWEgeDCQLYIVMGFC 84
Cdd:cd05112   8 FVQEIGSGQFGLVHLGYWLNKDK-VAIK--TIREGAMSEEDFIE-EAEVMMKLSHPKLVqLYGVCLE--QAPICLVFEFM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  85 EGGDLYHRLKQQKGeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTl 164
Cdd:cd05112  82 EHGCLSDYLRTQRG-LFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTRFVLDDQYTSST- 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 165 iGTPY---YMSPELFSNKPYNYKSDVWALGCCVYEM-ATLKHAFNAKDMNSLVYRIVEGKLPQMPSKYDPQLGELIKRML 240
Cdd:cd05112 160 -GTKFpvkWSSPEVFSFSRYSSKSDVWSFGVLMWEVfSEGKIPYENRSNSEVVEDINAGFRLYKPRLASTHVYEIMNHCW 238
                       250
                ....*....|....*.
gi 41055987 241 CKKPEDRPDVKHILRQ 256
Cdd:cd05112 239 KERPEDRPSFSLLLRQ 254
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
7-213 3.11e-23

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: 100.04  E-value: 3.11e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   7 VRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRtsSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEG 86
Cdd:cd14192   9 HEVLGGGRFGQVHKCTELSTGLTLAAKIIKVK--GAKEREEVKNEINIMNQLNHVNLIQLYDAFESKT-NLTLIMEYVDG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  87 GDLYHRLKQQKGELlPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKT--NIIKVGDLGIARVLENQNDMASTL 164
Cdd:cd14192  86 GELFDRITDESYQL-TELDAILFTRQICEGVHYLHQHYILHLDLKPENILCVNStgNQIKIIDFGLARRYKPREKLKVNF 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 41055987 165 iGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAF----NAKDMNSLV 213
Cdd:cd14192 165 -GTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFlgetDAETMNNIV 216
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
2-247 3.47e-23

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: 101.62  E-value: 3.47e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRA---AEQEaqLLSQLKHPNIVMYRESWEGEDCqLY 78
Cdd:cd05598   1 SMFEKIKTIGVGAFGEVSLVRKKDTNALYAMKTLRKKDVLKRNQVAhvkAERD--ILAEADNEWVVKLYYSFQDKEN-LY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  79 IVMGFCEGGDLYHRLkqQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQN 158
Cdd:cd05598  78 FVMDYIPGGDLMSLL--IKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTH 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 159 D----MASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIV----EGKLPQMPsKYDP 230
Cdd:cd05598 156 DskyyLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAQTPAETQLKVInwrtTLKIPHEA-NLSP 234
                       250
                ....*....|....*..
gi 41055987 231 QLGELIKRmLCKKPEDR 247
Cdd:cd05598 235 EAKDLILR-LCCDAEDR 250
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
10-198 3.93e-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: 100.20  E-value: 3.93e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEGgDL 89
Cdd:cd07839   8 IGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEGVPSSALREICLLKELKHKNIVRLYDVLHSDK-KLTLVFEYCDQ-DL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  90 YHRLKQQKGEllPERQVVEWFV-QIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLIGTP 168
Cdd:cd07839  86 KKYFDSCNGD--IDPEIVKSFMfQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARAFGIPVRCYSAEVVTL 163
                       170       180       190
                ....*....|....*....|....*....|.
gi 41055987 169 YYMSPE-LFSNKPYNYKSDVWALGCCVYEMA 198
Cdd:cd07839 164 WYRPPDvLFGAKLYSTSIDMWSAGCIFAELA 194
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
10-199 4.10e-23

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: 100.91  E-value: 4.10e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRE-------SWEGEDCQLYIVMG 82
Cdd:cd07865  20 IGQGTFGEVFKARHRKTGQIVALKKVLMENEKEGFPITALREIKILQLLKHENVVNLIEicrtkatPYNRYKGSIYLVFE 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FCEGgDLYHRLKQQKGEL-LPERQVVewFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVL----ENQ 157
Cdd:cd07865 100 FCEH-DLAGLLSNKNVKFtLSEIKKV--MKMLLNGLYYIHRNKILHRDMKAANILITKDGVLKLADFGLARAFslakNSQ 176
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 41055987 158 NDMASTLIGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMAT 199
Cdd:cd07865 177 PNRYTNRVVTLWYRPPElLLGERDYGPPIDMWGAGCIMAEMWT 219
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
10-273 4.84e-23

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type IV; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKIV is found predominantly in neurons and immune cells. It is activated by the binding of calcium/CaM and phosphorylation by CaMKK (alpha or beta). The CaMKK-CaMKIV cascade participates in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors. It also is implicated in T-cell development and signaling, cytokine secretion, and signaling through Toll-like receptors, and is thus, pivotal in immune response and inflammation. The CaMKIV subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 100.28  E-value: 4.84e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNlRTSsrrERRAAEQEAQLLSQLKHPNIVMYRESWEgEDCQLYIVMGFCEGGDL 89
Cdd:cd14085  11 LGRGATSVVYRCRQKGTQKPYAVKKLK-KTV---DKKIVRTEIGVLLRLSHPNIIKLKEIFE-TPTEISLVLELVTGGEL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  90 YHRLkQQKGeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKT---NIIKVGDLGIARVLENQNDMaSTLIG 166
Cdd:cd14085  86 FDRI-VEKG-YYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPapdAPLKIADFGLSKIVDQQVTM-KTVCG 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 167 TPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVY-RIVEGKLPQMPSKYDP---QLGELIKRMLCK 242
Cdd:cd14085 163 TPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYDERGDQYMFkRILNCDYDFVSPWWDDvslNAKDLVKKLIVL 242
                       250       260       270
                ....*....|....*....|....*....|...
gi 41055987 243 KPEDRPDVKHILRQPYIKHQISMF--LEATKEK 273
Cdd:cd14085 243 DPKKRLTTQQALQHPWVTGKAANFahMDTAQKK 275
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
10-197 5.66e-23

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: 99.09  E-value: 5.66e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDrKQYVIKKLNLRTSSRRERRaaeQEAQLLSQLKHPNIV--MYRESWEGedcQLYIVMGFCEGG 87
Cdd:cd14155   1 IGSGFFSEVYKVRHRTS-GQVMALKMNTLSSNRANML---REVQLMNRLSHPNILrfMGVCVHQG---QLHALTEYINGG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  88 DLYhrlkqqkgELLPERQVVEWFVQ------IAMALQYLHEKHILHRDLKTQNIFLTKTN---IIKVGDLGIARVLENQN 158
Cdd:cd14155  74 NLE--------QLLDSNEPLSWTVRvklaldIARGLSYLHSKGIFHRDLTSKNCLIKRDEngyTAVVGDFGLAEKIPDYS 145
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 41055987 159 DMASTL--IGTPYYMSPELFSNKPYNYKSDVWALGCCVYEM 197
Cdd:cd14155 146 DGKEKLavVGSPYWMAPEVLRGEPYNEKADVFSYGIILCEI 186
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
4-259 6.42e-23

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: 100.13  E-value: 6.42e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRA-----AEQEAQLLSQLKHPNIVMYRESWEGEDCQLY 78
Cdd:cd14040   8 YLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKEnyhkhACREYRIHKELDHPRIVKLYDYFSLDTDTFC 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  79 IVMGFCEGGDLYHRLKQQKgeLLPERQVVEWFVQIAMALQYLHE--KHILHRDLKTQNIFL---TKTNIIKVGDLGIARV 153
Cdd:cd14040  88 TVLEYCEGNDLDFYLKQHK--LMSEKEARSIVMQIVNALRYLNEikPPIIHYDLKPGNILLvdgTACGEIKITDFGLSKI 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 154 LENQN------DMASTLIGTPYYMSPELF--SNKP--YNYKSDVWALGC----CVYEMATLKHAFNAKDM--NSLVYRIV 217
Cdd:cd14040 166 MDDDSygvdgmDLTSQGAGTYWYLPPECFvvGKEPpkISNKVDVWSVGViffqCLYGRKPFGHNQSQQDIlqENTILKAT 245
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 41055987 218 EGKLPQMPSkYDPQLGELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd14040 246 EVQFPVKPV-VSNEAKAFIRRCLAYRKEDRFDVHQLASDPYL 286
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
7-257 7.28e-23

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: 99.40  E-value: 7.28e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   7 VRVVGKGSYGEVNLVRHKSDRKQYVIKKlnlrtsSRRERRAAEQEAQLLSQL-------KHPNIVMYRESWeGEDCQLYI 79
Cdd:cd14051   5 VEKIGSGEFGSVYKCINRLDGCVYAIKK------SKKPVAGSVDEQNALNEVyahavlgKHPHVVRYYSAW-AEDDHMII 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  80 VMGFCEGGDLYHRLK--QQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNII-------------- 143
Cdd:cd14051  78 QNEYCNGGSLADAISenEKAGERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFISRTPNPvsseeeeedfegee 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 144 ----------KVGDLGIArvlenqndmasTLIGTPY-------YMSPEL----FSNKPynyKSDVWALGCCVYEMA---T 199
Cdd:cd14051 158 dnpesnevtyKIGDLGHV-----------TSISNPQveegdcrFLANEIlqenYSHLP---KADIFALALTVYEAAgggP 223
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 41055987 200 LKHafNAKDMnslvYRIVEGKLPQMPSkYDPQLGELIKRMLCKKPEDRPDVKHILRQP 257
Cdd:cd14051 224 LPK--NGDEW----HEIRQGNLPPLPQ-CSPEFNELLRSMIHPDPEKRPSAAALLQHP 274
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
48-258 7.84e-23

Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), is an ER-localized type I transmembrane protein with kinase and endoribonuclease domains in the cytoplasmic side. It acts as an ER stress sensor and is the oldest and most conserved component of the unfolded protein response (UPR) in eukaryotes. The UPR is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. During ER stress, IRE1 dimerizes and forms oligomers, allowing the kinase domain to undergo trans-autophosphorylation. This leads to a conformational change that stimulates its endoribonuclease activity and results in the cleavage of its mRNA substrate, HAC1 in yeast and XBP1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. Mammals contain two IRE1 proteins, IRE1alpha (or ERN1) and IRE1beta (or ERN2). The Ire1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 98.88  E-value: 7.84e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  48 AEQEAQLLSQL-KHPNIVMY--REswegEDCQ-LYIVMGFCEGG--DLYHRLKQQKGELLPERQVVEWFVQIAMALQYLH 121
Cdd:cd13982  41 ADREVQLLRESdEHPNVIRYfcTE----KDRQfLYIALELCAASlqDLVESPRESKLFLRPGLEPVRLLRQIASGLAHLH 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 122 EKHILHRDLKTQNIFLTKTNI-----IKVGDLGIARVLenqNDMASTLI------GTPYYMSPELFSNKPYN---YKSDV 187
Cdd:cd13982 117 SLNIVHRDLKPQNILISTPNAhgnvrAMISDFGLCKKL---DVGRSSFSrrsgvaGTSGWIAPEMLSGSTKRrqtRAVDI 193
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41055987 188 WALGCCVYEMATL-KHAFNAK---DMNslvyrIVEGK--LPQMPSK--YDPQLGELIKRMLCKKPEDRPDVKHILRQPY 258
Cdd:cd13982 194 FSLGCVFYYVLSGgSHPFGDKlerEAN-----ILKGKysLDKLLSLgeHGPEAQDLIERMIDFDPEKRPSAEEVLNHPF 267
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
6-261 8.66e-23

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: 100.45  E-value: 8.66e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   6 FVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRR--------ERRAAEqeaqLLSQLKHPNIVMYRESWEGEDcQL 77
Cdd:cd05589   3 CIAVLGRGHFGKVLLAEYKPTGELFAIKALKKGDIIARdeveslmcEKRIFE----TVNSARHPFLVNLFACFQTPE-HV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  78 YIVMGFCEGGDLYHRLKQqkgELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQ 157
Cdd:cd05589  78 CFVMEYAAGGDLMMHIHE---DVFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGF 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 158 NDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIV--EGKLPQMPSkydPQLGEL 235
Cdd:cd05589 155 GDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVndEVRYPRFLS---TEAISI 231
                       250       260       270
                ....*....|....*....|....*....|.
gi 41055987 236 IKRMLCKKPEDR-----PDVKHILRQPYIKH 261
Cdd:cd05589 232 MRRLLRKNPERRlgaseRDAEDVKKQPFFRN 262
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
8-259 8.93e-23

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: 98.91  E-value: 8.93e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAqllsqlKHPNIV----MYRESWEGEDCqLYIVMGF 83
Cdd:cd14172  10 QVLGLGVNGKVLECFHRRTGQKCALKLLYDSPKARREVEHHWRAS------GGPHIVhildVYENMHHGKRC-LLIIMEC 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGGDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLT---KTNIIKVGDLGIARVLENQNDM 160
Cdd:cd14172  83 MEGGELFSRIQERGDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTskeKDAVLKLTDFGFAKETTVQNAL 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 161 aSTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLV----YRIVEGKLpQMP----SKYDPQL 232
Cdd:cd14172 163 -QTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTGQAISpgmkRRIRMGQY-GFPnpewAEVSEEA 240
                       250       260
                ....*....|....*....|....*..
gi 41055987 233 GELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd14172 241 KQLIRHLLKTDPTERMTITQFMNHPWI 267
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
8-283 9.40e-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: 100.26  E-value: 9.40e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKQYVIKKLN---LRTSSRRERRAAEQEAQLLSQlKHPNIVMYRESWEGEDcQLYIVMGFC 84
Cdd:cd05591   1 KVLGKGSFGKVMLAERKGTDEVYAIKVLKkdvILQDDDVDCTMTEKRILALAA-KHPFLTALHSCFQTKD-RLFFVMEYV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  85 EGGDLYHRLkqQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTL 164
Cdd:cd05591  79 NGGDLMFQI--QRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGKTTTTF 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 165 IGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKL--PQMPSKydpQLGELIKRMLCK 242
Cdd:cd05591 157 CGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVlyPVWLSK---EAVSILKAFMTK 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 41055987 243 KPEDR-------PDVKHILRQPYIKHQISMFLEATKEKTA-----KSRKNAAN 283
Cdd:cd05591 234 NPAKRlgcvasqGGEDAIRQHPFFREIDWEALEQRKVKPPfkpkiKTKRDANN 286
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
10-191 9.40e-23

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


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 98.73  E-value: 9.40e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNlrTSSRRERRAAEQEAQLLSQLKHPNI-----VMYReswegeDCQLYIVMGFC 84
Cdd:cd14154   1 LGKGFFGQAIKVTHRETGEVMVMKELI--RFDEEAQRNFLKEVKVMRSLDHPNVlkfigVLYK------DKKLNLITEYI 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  85 EGGDLYHRLKQqKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARV-----LENQND 159
Cdd:cd14154  73 PGGTLKDVLKD-MARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLARLiveerLPSGNM 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 41055987 160 MAS---------------TLIGTPYYMSPELFSNKPYNYKSDVWALG 191
Cdd:cd14154 152 SPSetlrhlkspdrkkryTVVGNPYWMAPEMLNGRSYDEKVDIFSFG 198
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
10-261 1.19e-22

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: 98.99  E-value: 1.19e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNlRTSSRRERRaaeqeaQLLSQLkhpNIVMyreswEGEDCQlYIV--------- 80
Cdd:cd06618  23 IGSGTCGQVYKMRHKKTGHVMAVKQMR-RSGNKEENK------RILMDL---DVVL-----KSHDCP-YIVkcygyfitd 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 ---------MGFCeggdlYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKH-ILHRDLKTQNIFLTKTNIIKVGDLGI 150
Cdd:cd06618  87 sdvficmelMSTC-----LDKLLKRIQGPIPEDILGKMTVSIVKALHYLKEKHgVIHRDVKPSNILLDESGNVKLCDFGI 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 151 A-RVLEnqnDMAST-LIGTPYYMSPELFS--NKP-YNYKSDVWALGCCVYEMATLKHAFNAKDMN-SLVYRIVEGKLPQM 224
Cdd:cd06618 162 SgRLVD---SKAKTrSAGCAAYMAPERIDppDNPkYDIRADVWSLGISLVELATGQFPYRNCKTEfEVLTKILNEEPPSL 238
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 41055987 225 PSK--YDPQLGELIKRMLCKKPEDRPDVKHILRQPYIKH 261
Cdd:cd06618 239 PPNegFSPDFCSFVDLCLTKDHRYRPKYRELLQHPFIRR 277
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
9-260 1.49e-22

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: 99.05  E-value: 1.49e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   9 VVGKGSYGEVNLVRHKSD-----RKqyvIKKLNLRTSSRRErraAEQEAQLLSQLKHPNIVMYRESWEgEDCQLYIVMGF 83
Cdd:cd06615   8 ELGAGNGGVVTKVLHRPSglimaRK---LIHLEIKPAIRNQ---IIRELKVLHECNSPYIVGFYGAFY-SDGEISICMEH 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGGDLYHRLKqqKGELLPERQVVEWFVQIAMALQYLHEKH-ILHRDLKTQNIFLTKTNIIKVGDLGIARVLenQNDMAS 162
Cdd:cd06615  81 MDGGSLDQVLK--KAGRIPENILGKISIAVLRGLTYLREKHkIMHRDVKPSNILVNSRGEIKLCDFGVSGQL--IDSMAN 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 163 TLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMAT------------LKHAFNAKD----------------MNS--- 211
Cdd:cd06615 157 SFVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIgrypipppdakeLEAMFGRPVsegeakeshrpvsghpPDSprp 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 41055987 212 -----LVYRIVEGKLPQMPSK-YDPQLGELIKRMLCKKPEDRPDVKHILRQPYIK 260
Cdd:cd06615 237 maifeLLDYIVNEPPPKLPSGaFSDEFQDFVDKCLKKNPKERADLKELTKHPFIK 291
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
4-258 1.53e-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: 100.12  E-value: 1.53e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIV----MYRESWEGED-CQLY 78
Cdd:cd07878  17 YQNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLSRPFQSLIHARRTYRELRLLKHMKHENVIglldVFTPATSIENfNEVY 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  79 IVMGFCeGGDLYHRLKQQKgelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARvleNQN 158
Cdd:cd07878  97 LVTNLM-GADLNNIVKCQK---LSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLAR---QAD 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 159 DMASTLIGTPYYMSPELFSN-KPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVE------------------- 218
Cdd:cd07878 170 DEMTGYVATRWYRAPEIMLNwMHYNQTVDIWSVGCIMAELLKGKALFPGNDYIDQLKRIMEvvgtpspevlkkissehar 249
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 41055987 219 ---GKLPQMPSK--------YDPQLGELIKRMLCKKPEDRPDVKHILRQPY 258
Cdd:cd07878 250 kyiQSLPHMPQQdlkkifrgANPLAIDLLEKMLVLDSDKRISASEALAHPY 300
pknD PRK13184
serine/threonine-protein kinase PknD;
1-287 1.70e-22

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 103.70  E-value: 1.70e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987    1 MDGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKL--NLRTSSRRERRAAeQEAQLLSQLKHPNIV-MYRESWEGEdcQL 77
Cdd:PRK13184   1 MQRYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIreDLSENPLLKKRFL-REAKIAADLIHPGIVpVYSICSDGD--PV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   78 YIVMGFCEGGDLYHRLKQ--QKGEL---LPERQVVEWFV----QIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDL 148
Cdd:PRK13184  78 YYTMPYIEGYTLKSLLKSvwQKESLskeLAEKTSVGAFLsifhKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDW 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  149 GIARVLENQND------------MASTL------IGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMN 210
Cdd:PRK13184 158 GAAIFKKLEEEdlldidvderniCYSSMtipgkiVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRKKGR 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  211 SLVYR-IVEGklPQMPSKY---DPQLGELIKRMLCKKPEDRPDVKHILR---QPYIKHQISMFleatkEKTAKSRKNAAN 283
Cdd:PRK13184 238 KISYRdVILS--PIEVAPYreiPPFLSQIAMKALAVDPAERYSSVQELKqdlEPHLQGSPEWT-----VKATLMTKKKSC 310

                 ....
gi 41055987  284 GKLN 287
Cdd:PRK13184 311 WKFY 314
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
11-219 1.81e-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: 98.91  E-value: 1.81e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  11 GKGSYGEVNLVRHKSDRKQYVIKKLnlrtsSRRERraAEQEAQLLSQLK-HPNIVMYRESWEGEdCQLYIVMGFCEGGDL 89
Cdd:cd14092  15 GDGSFSVCRKCVHKKTGQEFAVKIV-----SRRLD--TSREVQLLRLCQgHPNIVKLHEVFQDE-LHTYLVMELLRGGEL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  90 YHRLKQQKgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTN---IIKVGDLGIARVLENQNDMaSTLIG 166
Cdd:cd14092  87 LERIRKKK--RFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDddaEIKIVDFGFARLKPENQPL-KTPCF 163
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41055987 167 TPYYMSPELFSNKP----YNYKSDVWALGCCVYEMATLKHAFNAKDMN----SLVYRIVEG 219
Cdd:cd14092 164 TLPYAAPEVLKQALstqgYDESCDLWSLGVILYTMLSGQVPFQSPSRNesaaEIMKRIKSG 224
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
43-259 2.21e-22

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: 97.30  E-value: 2.21e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  43 RERRAAEQEAQLLSQLKHPNIVMYRESWEGEDCqLYIVMGFCEGGDLYHRLKQQKgeLLPERQVVEWFVQIAMALQYLHE 122
Cdd:cd14110  41 EDKQLVLREYQVLRRLSHPRIAQLHSAYLSPRH-LVLIEELCSGPELLYNLAERN--SYSEAEVTDYLWQILSAVDYLHS 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 123 KHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLIGtpYY---MSPELFSNKPYNYKSDVWALGCCVYEMAT 199
Cdd:cd14110 118 RRILHLDLRSENMIITEKNLLKIVDLGNAQPFNQGKVLMTDKKG--DYvetMAPELLEGQGAGPQTDIWAIGVTAFIMLS 195
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41055987 200 LKHAFNAkDMNSLVYRIVEGKLPQMPSKYdPQLGE----LIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd14110 196 ADYPVSS-DLNWERDRNIRKGKVQLSRCY-AGLSGgavnFLKSTLCAKPWGRPTASECLQNPWL 257
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
8-251 2.24e-22

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: 97.51  E-value: 2.24e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKsDRKQYVIKKLnlRTSSRRERRAAEQEAQLLSQLKHPNIV-MYRESWEGEdcQLYIVMGFCEG 86
Cdd:cd05148  12 RKLGSGYFGEVWEGLWK-NRVRVAIKIL--KSDDLLKQQDFQKEVQALKRLRHKHLIsLFAVCSVGE--PVYIITELMEK 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  87 GDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMAS-TLI 165
Cdd:cd05148  87 GSLLAFLRSPEGQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLARLIKEDVYLSSdKKI 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 166 gtPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVY-RIVEG-KLPQmPSKYDPQLGELIKRMLCK 242
Cdd:cd05148 167 --PYkWTAPEAASHGTFSTKSDVWSFGILLYEMFTYGQVPYPGMNNHEVYdQITAGyRMPC-PAKCPQEIYKIMLECWAA 243

                ....*....
gi 41055987 243 KPEDRPDVK 251
Cdd:cd05148 244 EPEDRPSFK 252
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
1-217 4.51e-22

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: 97.39  E-value: 4.51e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   1 MDGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRtssrRERRA---AEQEAQLLSQLKHPNIVMYRESWEGEDCqL 77
Cdd:cd07871   4 LETYVKLDKLGEGTYATVFKGRSKLTENLVALKEIRLE----HEEGApctAIREVSLLKNLKHANIVTLHDIIHTERC-L 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  78 YIVMGFCEGgDLYHRLkQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQ 157
Cdd:cd07871  79 TLVFEYLDS-DLKQYL-DNCGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLARAKSVP 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41055987 158 NDMASTLIGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAF---NAKDMNSLVYRIV 217
Cdd:cd07871 157 TKTYSNEVVTLWYRPPDvLLGSTEYSTPIDMWGVGCILYEMATGRPMFpgsTVKEELHLIFRLL 220
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
10-254 4.70e-22

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: 97.02  E-value: 4.70e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDrkqYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcqLYIVMGFCEGGDL 89
Cdd:cd14149  20 IGSGSFGTVYKGKWHGD---VAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMTKDN--LAIVTQWCEGSSL 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  90 YHRLKQQKGELlPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLE--NQNDMASTLIGT 167
Cdd:cd14149  95 YKHLHVQETKF-QMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSrwSGSQQVEQPTGS 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 168 PYYMSPELF---SNKPYNYKSDVWALGCCVYEMATLKHAFN-AKDMNSLVYRIVEGKLPQMPSKYDPQLGELIKRMLC-- 241
Cdd:cd14149 174 ILWMAPEVIrmqDNNPFSFQSDVYSYGIVLYELMTGELPYShINNRDQIIFMVGRGYASPDLSKLYKNCPKAMKRLVAdc 253
                       250
                ....*....|....*
gi 41055987 242 --KKPEDRPDVKHIL 254
Cdd:cd14149 254 ikKVKEERPLFPQIL 268
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
8-253 4.83e-22

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: 96.63  E-value: 4.83e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKqYVIKKLNLRTSSRRerrAAEQEAQLLSQLKHPNIVMYRESWEGEdcQLYIVMGFCEGG 87
Cdd:cd05073  17 KKLGAGQFGEVWMATYNKHTK-VAVKTMKPGSMSVE---AFLAEANVMKTLQHDKLVKLHAVVTKE--PIYIITEFMAKG 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  88 DLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLIGT 167
Cdd:cd05073  91 SLLDFLKSDEGSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVIEDNEYTAREGAKF 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 168 PY-YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPSKYDPQ-LGELIKRMLCKKPE 245
Cdd:cd05073 171 PIkWTAPEAINFGSFTIKSDVWSFGILLMEIVTYGRIPYPGMSNPEVIRALERGYRMPRPENCPEeLYNIMMRCWKNRPE 250

                ....*...
gi 41055987 246 DRPDVKHI 253
Cdd:cd05073 251 ERPTFEYI 258
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
10-249 5.21e-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: 96.44  E-value: 5.21e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVnlVRHKSDRKQYVIKKLNLRT-SSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDCQLYIVMGFCEGGD 88
Cdd:cd14064   1 IGSGSFGKV--YKGRCRNKIVAIKRYRANTyCSKSDVDMFCREVSILCRLNHPCVIQFVGACLDDPSQFAIVTQYVSGGS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  89 LYHRLKQQKGELLPERQVVeWFVQIAMALQYLHE--KHILHRDLKTQNIFLTKTNIIKVGDLGIARVLEN-QNDMASTLI 165
Cdd:cd14064  79 LFSLLHEQKRVIDLQSKLI-IAVDVAKGMEYLHNltQPIIHRDLNSHNILLYEDGHAVVADFGESRFLQSlDEDNMTKQP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 166 GTPYYMSPELFS-NKPYNYKSDVWALGCCVYEMAT-------LKHAFNAKDMnslVYRIVEgklPQMPSKYDPQLGELIK 237
Cdd:cd14064 158 GNLRWMAPEVFTqCTRYSIKADVFSYALCLWELLTgeipfahLKPAAAAADM---AYHHIR---PPIGYSIPKPISSLLM 231
                       250
                ....*....|..
gi 41055987 238 RMLCKKPEDRPD 249
Cdd:cd14064 232 RGWNAEPESRPS 243
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
8-279 6.58e-22

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


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 97.03  E-value: 6.58e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIvmYRESWEGEDCqLYIVMGFCEGG 87
Cdd:cd14170   8 QVLGLGINGKVLQIFNKRTQEKFALKMLQDCPKARREVELHWRASQCPHIVRIVDV--YENLYAGRKC-LLIVMECLDGG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  88 DLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTK---TNIIKVGDLGIARVLENQNDMASTL 164
Cdd:cd14170  85 ELFSRIQDRGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSkrpNAILKLTDFGFAKETTSHNSLTTPC 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 165 IgTPYYMSPELFSNKPYNYKSDVWALGC------CVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMP-SKYDPQLGELIK 237
Cdd:cd14170 165 Y-TPYYVAPEVLGPEKYDKSCDMWSLGVimyillCGYPPFYSNHGLAISPGMKTRIRMGQYEFPNPEwSEVSEEVKMLIR 243
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 41055987 238 RMLCKKPEDRPDVKHILRQPYIKHqiSMFLEATKEKTAKSRK 279
Cdd:cd14170 244 NLLKTEPTQRMTITEFMNHPWIMQ--STKVPQTPLHTSRVLK 283
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
6-256 1.18e-21

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: 95.31  E-value: 1.18e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   6 FVRVVGKGSYGEVNLVRHKSdrkQYVIKKLNLRTSSRRERRAAEqEAQLLSQLKHPNIV-MYRESWEGEdcQLYIVMGFC 84
Cdd:cd05114   8 FMKELGSGLFGVVRLGKWRA---QYKVAIKAIREGAMSEEDFIE-EAKVMMKLTHPKLVqLYGVCTQQK--PIYIVTEFM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  85 EGGDLYHRLKQQKGELLPErQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIAR-VLENQNDMAST 163
Cdd:cd05114  82 ENGCLLNYLRQRRGKLSRD-MLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRyVLDDQYTSSSG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 164 LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATL-KHAFNAKDMNSLVYRIVEGKLPQMPSKYDPQLGELIKRMLCK 242
Cdd:cd05114 161 AKFPVKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTEgKMPFESKSNYEVVEMVSRGHRLYRPKLASKSVYEVMYSCWHE 240
                       250
                ....*....|....
gi 41055987 243 KPEDRPDVKHILRQ 256
Cdd:cd05114 241 KPEGRPTFADLLRT 254
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
6-225 1.45e-21

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: 95.56  E-value: 1.45e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   6 FVRVVGKGSYGEVnlvrHKS------DRKQY--VIKKLnLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDCQL 77
Cdd:cd05057  11 KGKVLGSGAFGTV----YKGvwipegEKVKIpvAIKVL-REETGPKANEEILDEAYVMASVDHPHLVRLLGICLSSQVQL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  78 yiVMGFCEGGDLYHRLKQQKGELLPeRQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQ 157
Cdd:cd05057  86 --ITQLMPLGCLLDYVRNHRDNIGS-QLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGLAKLLDVD 162
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41055987 158 NDMASTLIG-TPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATLK----HAFNAKDMNSLVyrIVEGKLPQMP 225
Cdd:cd05057 163 EKEYHAEGGkVPIkWMALESIQYRIYTHKSDVWSYGVTVWELMTFGakpyEGIPAVEIPDLL--EKGERLPQPP 234
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
8-254 1.46e-21

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 95.49  E-value: 1.46e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEV------NLVrhKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVmyreswegedcQLY--- 78
Cdd:cd05032  12 RELGQGSFGMVyeglakGVV--KGEPETRVAIKTVNENASMRERIEFLNEASVMKEFNCHHVV-----------RLLgvv 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  79 -------IVMGFCEGGDLYHRLKQQKGE--------LLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNII 143
Cdd:cd05032  79 stgqptlVVMELMAKGDLKSYLRSRRPEaennpglgPPTLQKFIQMAAEIADGMAYLAAKKFVHRDLAARNCMVAEDLTV 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 144 KVGDLGIARVLENQNdmastligtpYY------------MSPELFSNKPYNYKSDVWALGCCVYEMATL-KHAFNAKDMN 210
Cdd:cd05032 159 KIGDFGMTRDIYETD----------YYrkggkgllpvrwMAPESLKDGVFTTKSDVWSFGVVLWEMATLaEQPYQGLSNE 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 41055987 211 SLVYRIVEGKLPQMPSKYDPQLGELIKRMLCKKPEDRPDVKHIL 254
Cdd:cd05032 229 EVLKFVIDGGHLDLPENCPDKLLELMRMCWQYNPKMRPTFLEIV 272
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
8-208 1.80e-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: 96.26  E-value: 1.80e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERraaEQEAQLLSQlKHPNIVMYRESWEgEDCQLYIVMGFCEGG 87
Cdd:cd14179  13 KPLGEGSFSICRKCLHKKTNQEYAVKIVSKRMEANTQR---EIAALKLCE-GHPNIVKLHEVYH-DQLHTFLVMELLKGG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  88 DLYHRLKQQKgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNI---IKVGDLGIARVLENQNDMASTL 164
Cdd:cd14179  88 ELLERIKKKQ--HFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESDnseIKIIDFGFARLKPPDNQPLKTP 165
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 41055987 165 IGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKD 208
Cdd:cd14179 166 CFTLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQCHD 209
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
5-253 1.81e-21

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: 95.23  E-value: 1.81e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   5 LFVRVVGKGSYGEVNL-----VRHKSDRKQYVIKKLNlRTSSRRERRAAEQEAQLLSQLKHPNIV-MYRESWEGEdcQLY 78
Cdd:cd05049   8 VLKRELGEGAFGKVFLgecynLEPEQDKMLVAVKTLK-DASSPDARKDFEREAELLTNLQHENIVkFYGVCTEGD--PLL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  79 IVMGFCEGGDLYHRLK-------------QQKGELLPErQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKV 145
Cdd:cd05049  85 MVFEYMEHGDLNKFLRshgpdaaflasedSAPGELTLS-QLLHIAVQIASGMVYLASQHFVHRDLATRNCLVGTNLVVKI 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 146 GDLGIARvlenqnDMAStligTPYY------------MSPELFSNKPYNYKSDVWALGCCVYEMATL-KHAFNAKDMNSL 212
Cdd:cd05049 164 GDFGMSR------DIYS----TDYYrvgghtmlpirwMPPESILYRKFTTESDVWSFGVVLWEIFTYgKQPWFQLSNTEV 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 41055987 213 VYRIVEGKLPQMPSKYDPQLGELIKRMLCKKPEDRPDVKHI 253
Cdd:cd05049 234 IECITQGRLLQRPRTCPSEVYAVMLGCWKREPQQRLNIKDI 274
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
10-258 2.14e-21

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: 95.24  E-value: 2.14e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLrTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEGgDL 89
Cdd:cd07836   8 LGEGTYATVYKGRNRTTGEIVALKEIHL-DAEEGTPSTAIREISLMKELKHENIVRLHDVIHTEN-KLMLVFEYMDK-DL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  90 --YHRLKQQKGELLPerQVVEWFV-QIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLIG 166
Cdd:cd07836  85 kkYMDTHGVRGALDP--NTVKSFTyQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARAFGIPVNTFSNEVV 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 167 TPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAF---NAKDMNSLVYRIV------------------------- 217
Cdd:cd07836 163 TLWYRAPDvLLGSRTYSTSIDIWSVGCIMAEMITGRPLFpgtNNEDQLLKIFRIMgtptestwpgisqlpeykptfpryp 242
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 41055987 218 EGKLPQMPSKYDPQLGELIKRMLCKKPEDRPDVKHILRQPY 258
Cdd:cd07836 243 PQDLQQLFPHADPLGIDLLHRLLQLNPELRISAHDALQHPW 283
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
9-256 2.25e-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: 94.30  E-value: 2.25e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   9 VVGKGSYGEVnlvrhksdRKQYVIKKLNLRTSSRRERRAAE------QEAQLLSQLKHPNIVmyreSWEGEDCQ---LYI 79
Cdd:cd05085   3 LLGKGNFGEV--------YKGTLKDKTPVAVKTCKEDLPQElkikflSEARILKQYDHPNIV----KLIGVCTQrqpIYI 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  80 VMGFCEGGDLYHRLKQQKGELlPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQND 159
Cdd:cd05085  71 VMELVPGGDFLSFLRKKKDEL-KTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSRQEDDGVY 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 160 MASTLIGTPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVE-GKLPQMPSKYDPQLGELIK 237
Cdd:cd05085 150 SSSGLKQIPIkWTAPEALNYGRYSSESDVWSFGILLWETFSLGVCPYPGMTNQQAREQVEkGYRMSAPQRCPEDIYKIMQ 229
                       250
                ....*....|....*....
gi 41055987 238 RMLCKKPEDRPDVKHILRQ 256
Cdd:cd05085 230 RCWDYNPENRPKFSELQKE 248
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
6-253 2.25e-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: 95.63  E-value: 2.25e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   6 FVRVVGKGSYGEV-NLVRHKSDRKQYVIK---KLNLRTSSRRERRAAEQEAQLLSQL-KHPNIVMYRESwegedCQ---- 76
Cdd:cd05055  39 FGKTLGAGAFGKVvEATAYGLSKSDAVMKvavKMLKPTAHSSEREALMSELKIMSHLgNHENIVNLLGA-----CTiggp 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  77 LYIVMGFCEGGDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLEN 156
Cdd:cd05055 114 ILVITEYCCYGDLLNFLRRKRESFLTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTHGKIVKICDFGLARDIMN 193
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 157 QNDMASTliGTPY----YMSPELFSNKPYNYKSDVWALGCCVYEMATLK-HAFNAKDMNSLVYRIVEGKLPQMPSKYDPQ 231
Cdd:cd05055 194 DSNYVVK--GNARlpvkWMAPESIFNCVYTFESDVWSYGILLWEIFSLGsNPYPGMPVDSKFYKLIKEGYRMAQPEHAPA 271
                       250       260
                ....*....|....*....|...
gi 41055987 232 -LGELIKRMLCKKPEDRPDVKHI 253
Cdd:cd05055 272 eIYDIMKTCWDADPLKRPTFKQI 294
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
4-269 2.85e-21

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also called ERK4) and 6 (also called ERK3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK4 (also called ERK4 or p63MAPK) and MAPK6 (also called ERK3 or p97MAPK) are atypical MAPKs that are not regulated by MAPK kinases. MAPK6 is expressed ubiquitously with highest amounts in brain and skeletal muscle. It may be involved in the control of cell differentiation by negatively regulating cell cycle progression in certain conditions. It may also play a role in glucose-induced insulin secretion. MAPK6 and MAPK4 cooperate to regulate the activity of MAPK-activated protein kinase 5 (MK5), leading to its relocation to the cytoplasm and exclusion from the nucleus. The MAPK6/MK5 and MAPK4/MK5 pathways may play critical roles in embryonic and post-natal development. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 96.00  E-value: 2.85e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRtsSRRERRAAEQEAQLLSQLKHPNIV-MY-----RESWEGEDCQ- 76
Cdd:cd07854   7 YMDLRPLGCGSNGLVFSAVDSDCDKRVAVKKIVLT--DPQSVKHALREIKIIRRLDHDNIVkVYevlgpSGSDLTEDVGs 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  77 ------LYIVMGFCEGgDLYHRLKQQkgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFL-TKTNIIKVGDLG 149
Cdd:cd07854  85 ltelnsVYIVQEYMET-DLANVLEQG---PLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFInTEDLVLKIGDFG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 150 IARVL----ENQNDMASTLIgTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEgklpQM 224
Cdd:cd07854 161 LARIVdphySHKGYLSEGLV-TKWYRSPRlLLSPNNYTKAIDMWAAGCIFAEMLTGKPLFAGAHELEQMQLILE----SV 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 41055987 225 PSKYDPQLGELIKRMLCKKPEDRPDVKHILRQ--PYIKHQISMFLEA 269
Cdd:cd07854 236 PVVREEDRNELLNVIPSFVRNDGGEPRRPLRDllPGVNPEALDFLEQ 282
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
4-249 2.89e-21

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: 95.70  E-value: 2.89e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRE--------------- 68
Cdd:cd13977   2 YSLIREVGRGSYGVVYEAVVRRTGARVAVKKIRCNAPENVELALREFWALSSIQRQHPNVIQLEEcvlqrdglaqrmshg 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  69 -------------SWEGE-------DCQLYIVMGFCEGGDLYHRLKQQKgellPERQVVEWFV-QIAMALQYLHEKHILH 127
Cdd:cd13977  82 ssksdlylllvetSLKGErcfdprsACYLWFVMEFCDGGDMNEYLLSRR----PDRQTNTSFMlQLSSALAFLHRNQIVH 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 128 RDLKTQNIFLTK---TNIIKVGDLGIARVL--------ENQN---DMASTLIGTPYYMSPELFSNKpYNYKSDVWALGCC 193
Cdd:cd13977 158 RDLKPDNILISHkrgEPILKVADFGLSKVCsgsglnpeEPANvnkHFLSSACGSDFYMAPEVWEGH-YTAKADIFALGII 236
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41055987 194 VYEMA---TLKHAFNAKDMnsLVYRIVEGK--LP-------------QMPSKYDPQLGE----LIKRMLCKKPEDRPD 249
Cdd:cd13977 237 IWAMVeriTFRDGETKKEL--LGTYIQQGKeiVPlgeallenpklelQIPLKKKKSMNDdmkqLLRDMLAANPQERPD 312
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
4-258 3.88e-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: 93.68  E-value: 3.88e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNlrtssrRERRAAEQEAQLL---SQLKHPNIVMYRESWEgEDCQLYIV 80
Cdd:cd14662   2 YELVKDIGSGNFGVARLMRNKETKELVAVKYIE------RGLKIDENVQREIinhRSLRHPNIIRFKEVVL-TPTHLAIV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MGFCEGGDLYHRLkQQKGELlPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFL--TKTNIIKVGDLGIAR--VLEN 156
Cdd:cd14662  75 MEYAAGGELFERI-CNAGRF-SEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLdgSPAPRLKICDFGYSKssVLHS 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 157 QndmASTLIGTPYYMSPELFSNKPYNYK-SDVWALGCCVYEMATLKHAF----NAKDMNSLVYRI--VEGKLPQMpSKYD 229
Cdd:cd14662 153 Q---PKSTVGTPAYIAPEVLSRKEYDGKvADVWSCGVTLYVMLVGAYPFedpdDPKNFRKTIQRImsVQYKIPDY-VRVS 228
                       250       260
                ....*....|....*....|....*....
gi 41055987 230 PQLGELIKRMLCKKPEDRPDVKHILRQPY 258
Cdd:cd14662 229 QDCRHLLSRIFVANPAKRITIPEIKNHPW 257
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
51-249 4.04e-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: 93.57  E-value: 4.04e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  51 EAQLLSQLKHPNIVMYRESWEGEdcQLYIVMGFCEGGDLyHRLKQQKGELlPERQVVEWFVQIAMALQYLHEKHILHRDL 130
Cdd:cd05060  46 EASVMAQLDHPCIVRLIGVCKGE--PLMLVMELAPLGPL-LKYLKKRREI-PVSDLKELAHQVAMGMAYLESKHFVHRDL 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 131 KTQNIFLTKTNIIKVGDLGIARVLENQNDmastligtpYYMS------------PELFSNKPYNYKSDVWALGCCVYEMA 198
Cdd:cd05060 122 AARNVLLVNRHQAKISDFGMSRALGAGSD---------YYRAttagrwplkwyaPECINYGKFSSKSDVWSYGVTLWEAF 192
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 41055987 199 TLKHAFNAKDMNSLVYRIVEG--KLPQmPSKYDPQLGELIKRMLCKKPEDRPD 249
Cdd:cd05060 193 SYGAKPYGEMKGPEVIAMLESgeRLPR-PEECPQEIYSIMLSCWKYRPEDRPT 244
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
4-259 4.30e-21

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: 93.87  E-value: 4.30e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVnlVR-HKSDRKQYV-IKKLNlrtSSRRERRAAEQEAQLLSQLK------HPNIV------MYREs 69
Cdd:cd14133   1 YEVLEVLGKGTFGQV--VKcYDLLTGEEVaLKIIK---NNKDYLDQSLDEIRLLELLNkkdkadKYHIVrlkdvfYFKN- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  70 wegedcQLYIVmgfCE--GGDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLT--KTNIIKV 145
Cdd:cd14133  75 ------HLCIV---FEllSQNLYEFLKQNKFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLAsySRCQIKI 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 146 GDLGIARVLenqNDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVE--GKLPQ 223
Cdd:cd14133 146 IDFGSSCFL---TQRLYSYIQSRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGtiGIPPA 222
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 41055987 224 ----MPSKYDPQLGELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd14133 223 hmldQGKADDELFVDFLKKLLEIDPKERPTASQALSHPWL 262
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
10-253 4.81e-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: 93.64  E-value: 4.81e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRaaeQEAQLLSQLKHPNIVMY-----RESwegedcQLYIVMGFC 84
Cdd:cd05052  14 LGGGQYGEVYEGVWKKYNLTVAVKTLKEDTMEVEEFL---KEAAVMKEIKHPNLVQLlgvctREP------PFYIITEFM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  85 EGGDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLenQNDMASTL 164
Cdd:cd05052  85 PYGNLLDYLRECNREELNAVVLLYMATQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLM--TGDTYTAH 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 165 IGTPY---YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMnSLVYRIVE-GKLPQMPSKYDPQLGELIKRM 239
Cdd:cd05052 163 AGAKFpikWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSpYPGIDL-SQVYELLEkGYRMERPEGCPPKVYELMRAC 241
                       250
                ....*....|....
gi 41055987 240 LCKKPEDRPDVKHI 253
Cdd:cd05052 242 WQWNPSDRPSFAEI 255
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
10-262 4.89e-21

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


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 94.31  E-value: 4.89e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNlrtssrRERRAAEQEAQLLSQL-KHPNIVMYRESWEgEDCQLYIVMGFCEGGD 88
Cdd:cd14177  12 IGVGSYSVCKRCIHRATNMEFAVKIID------KSKRDPSEEIEILMRYgQHPNIITLKDVYD-DGRYVYLVTELMKGGE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  89 LYHRLKQQKgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFL----TKTNIIKVGDLGIARVLENQNDMASTL 164
Cdd:cd14177  85 LLDRILRQK--FFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYmddsANADSIRICDFGFAKQLRGENGLLLTP 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 165 IGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFnAKDMN----SLVYRIVEGKLPQMPSKYDP---QLGELIK 237
Cdd:cd14177 163 CYTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPF-ANGPNdtpeEILLRIGSGKFSLSGGNWDTvsdAAKDLLS 241
                       250       260
                ....*....|....*....|....*
gi 41055987 238 RMLCKKPEDRPDVKHILRQPYIKHQ 262
Cdd:cd14177 242 HMLHVDPHQRYTAEQVLKHSWIACR 266
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
9-258 4.99e-21

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: 93.88  E-value: 4.99e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   9 VVGKGSYGEVNLVRHKSDRKQYVIKKLNLrTSSRRE-------RRAAEQEAQLLSQLK-HPNIVMYRESWEGEDCqLYIV 80
Cdd:cd14181  17 VIGRGVSSVVRRCVHRHTGQEFAVKIIEV-TAERLSpeqleevRSSTLKEIHILRQVSgHPSIITLIDSYESSTF-IFLV 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MGFCEGGDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLEnQNDM 160
Cdd:cd14181  95 FDLMRRGELFDYLTEKVT--LSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFSCHLE-PGEK 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 161 ASTLIGTPYYMSPELF------SNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPSKYDPQ--- 231
Cdd:cd14181 172 LRELCGTPGYLAPEILkcsmdeTHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIMEGRYQFSSPEWDDRsst 251
                       250       260
                ....*....|....*....|....*..
gi 41055987 232 LGELIKRMLCKKPEDRPDVKHILRQPY 258
Cdd:cd14181 252 VKDLISRLLVVDPEIRLTAEQALQHPF 278
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
10-256 5.15e-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: 93.57  E-value: 5.15e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHksdRKQYV-IKKLnlrtssRRERRAAEQ---EAQLLSQLKHPNIVMYResweG---EDCQLYIVMG 82
Cdd:cd05039  14 IGKGEFGDVMLGDY---RGQKVaVKCL------KDDSTAAQAflaEASVMTTLRHPNLVQLL----GvvlEGNGLYIVTE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FCEGGDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVlENQNDMAS 162
Cdd:cd05039  81 YMAKGSLVDYLRSRGRAVITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAKE-ASSNQDGG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 163 TLigtPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLVYRIVEGKLPQMPSKYDPQLGELIKRML 240
Cdd:cd05039 160 KL---PIkWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVpYPRIPLKDVVPHVEKGYRMEAPEGCPPEVYKVMKNCW 236
                       250
                ....*....|....*.
gi 41055987 241 CKKPEDRPDVKHILRQ 256
Cdd:cd05039 237 ELDPAKRPTFKQLREK 252
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
9-259 5.50e-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: 93.44  E-value: 5.50e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   9 VVGKGSYGEVNLVRHKSDRKQYVIKKLnlRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEGGD 88
Cdd:cd14193  11 ILGGGRFGQVHKCEEKSSGLKLAAKII--KARSQKEKEEVKNEIEVMNQLNHANLIQLYDAFESRN-DIVLVMEYVDGGE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  89 LYHRLKQQKGELlPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLT--KTNIIKVGDLGIARVLENQNDMASTLiG 166
Cdd:cd14193  88 LFDRIIDENYNL-TELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVsrEANQVKIIDFGLARRYKPREKLRVNF-G 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 167 TPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQMPSKYD---PQLGELIKRMLCKK 243
Cdd:cd14193 166 TPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILACQWDFEDEEFAdisEEAKDFISKLLIKE 245
                       250
                ....*....|....*.
gi 41055987 244 PEDRPDVKHILRQPYI 259
Cdd:cd14193 246 KSWRMSASEALKHPWL 261
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
4-260 6.24e-21

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: 94.85  E-value: 6.24e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLN-----LRTSSRRERraaeqEAQLLSQLKHPNIV-----MYRESwEGE 73
Cdd:cd07859   2 YKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKINdvfehVSDATRILR-----EIKLLRLLRHPDIVeikhiMLPPS-RRE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  74 DCQLYIVMGFCEGgDLyHRLKQQKGELLPERQVVeWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARV 153
Cdd:cd07859  76 FKDIYVVFELMES-DL-HQVIKANDDLTPEHHQF-FLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLARV 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 154 leNQNDMASTLIGTPY-----YMSPEL---FSNKpYNYKSDVWALGCCVYEMATLKHAFNAKD-------MNSL------ 212
Cdd:cd07859 153 --AFNDTPTAIFWTDYvatrwYRAPELcgsFFSK-YTPAIDIWSIGCIFAEVLTGKPLFPGKNvvhqldlITDLlgtpsp 229
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41055987 213 --VYRI-----------VEGKLP-QMPSKY---DPQLGELIKRMLCKKPEDRPDVKHILRQPYIK 260
Cdd:cd07859 230 etISRVrnekarrylssMRKKQPvPFSQKFpnaDPLALRLLERLLAFDPKDRPTAEEALADPYFK 294
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
16-258 6.24e-21

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


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 93.57  E-value: 6.24e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  16 GEVNLVR---HKSDRKQYVIKKLNLRTSSRRE------RRAAEQEAQLLSQL-KHPNIVMYRESWEgEDCQLYIVMGFCE 85
Cdd:cd14093  14 GVSSTVRrciEKETGQEFAVKIIDITGEKSSEneaeelREATRREIEILRQVsGHPNIIELHDVFE-SPTFIFLVFELCR 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  86 GGDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLEnQNDMASTLI 165
Cdd:cd14093  93 KGELFDYLTEVVT--LSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATRLD-EGEKLRELC 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 166 GTPYYMSPEL-----FSNKP-YNYKSDVWALGCCVYemaTLKHAF----NAKDMNSLvYRIVEGKLpQMPSkydPQLGE- 234
Cdd:cd14093 170 GTPGYLAPEVlkcsmYDNAPgYGKEVDMWACGVIMY---TLLAGCppfwHRKQMVML-RNIMEGKY-EFGS---PEWDDi 241
                       250       260       270
                ....*....|....*....|....*....|
gi 41055987 235 ------LIKRMLCKKPEDRPDVKHILRQPY 258
Cdd:cd14093 242 sdtakdLISKLLVVDPKKRLTAEEALEHPF 271
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
10-200 6.81e-21

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: 92.89  E-value: 6.81e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLrTSSRRERRAAEQEAQLLSQLKHPNIV-MYRESWEGEdcQLYIVMGFCEGGD 88
Cdd:cd05041   3 IGRGNFGDVYRGVLKPDNTEVAVKTCRE-TLPPDLKRKFLQEARILKQYDHPNIVkLIGVCVQKQ--PIMIVMELVPGGS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  89 LYHRLKQQKGELlPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARvlENQNDMASTLIGT- 167
Cdd:cd05041  80 LLTFLRKKGARL-TVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSR--EEEDGEYTVSDGLk 156
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 41055987 168 --PY-YMSPELFSNKPYNYKSDVWALGCCVYEMATL 200
Cdd:cd05041 157 qiPIkWTAPEALNYGRYTSESDVWSFGILLWEIFSL 192
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
8-248 6.83e-21

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: 93.33  E-value: 6.83e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIV-MYRESWEgedcQLYIVMGFCEG 86
Cdd:cd14025   2 EKVGSGGFGQVYKVRHKHWKTWLAIKCPPSLHVDDSERMELLEEAKKMEMAKFRHILpVYGICSE----PVGLVMEYMET 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  87 GDLYHRLKQqkgELLPERQVVEWFVQIAMALQYLH--EKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDM---A 161
Cdd:cd14025  78 GSLEKLLAS---EPLPWELRFRIIHETAVGMNFLHcmKPPLLHLDLKPANILLDAHYHVKISDFGLAKWNGLSHSHdlsR 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 162 STLIGTPYYMSPELF--SNKPYNYKSDVWALGCCVYEMATLKHAFNA-KDMNSLVYRIVEGKLPQMP--SKYDP----QL 232
Cdd:cd14025 155 DGLRGTIAYLPPERFkeKNRCPDTKHDVYSFAIVIWGILTQKKPFAGeNNILHIMVKVVKGHRPSLSpiPRQRPsecqQM 234
                       250
                ....*....|....*.
gi 41055987 233 GELIKRMLCKKPEDRP 248
Cdd:cd14025 235 ICLMKRCWDQDPRKRP 250
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
51-259 7.05e-21

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


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 92.96  E-value: 7.05e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  51 EAQLLSQLKHPNIVMYRESWEGEDCQLYIVMGFCEGGDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDL 130
Cdd:cd14109  46 EVDIHNSLDHPNIVQMHDAYDDEKLAVTVIDNLASTIELVRDNLLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDL 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 131 KTQNIFLtKTNIIKVGDLGIARVLENQNdMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMN 210
Cdd:cd14109 126 RPEDILL-QDDKLKLADFGQSRRLLRGK-LTTLIYGSPEFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDR 203
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 41055987 211 SLVYRIVEGKLPQMPSKYDP---QLGELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd14109 204 ETLTNVRSGKWSFDSSPLGNisdDARDFIKKLLVYIPESRLTVDEALNHPWF 255
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
6-248 1.19e-20

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: 92.47  E-value: 1.19e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   6 FVRVVGKGSYGEV-----NlvrhksDRKQYVIKKLNLRTSSRRERRAaeqEAQLLSQLKHPNIV-MYRESWEGEdcQLYI 79
Cdd:cd05068  12 LLRKLGSGQFGEVweglwN------NTTPVAVKTLKPGTMDPEDFLR---EAQIMKKLRHPKLIqLYAVCTLEE--PIYI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  80 VMGFCEGGDLYHRLkQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQND 159
Cdd:cd05068  81 ITELMKHGSLLEYL-QGKGRSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFGLARVIKVEDE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 160 MASTlIGTPY---YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEG--KLPQmPSKYDPQLGE 234
Cdd:cd05068 160 YEAR-EGAKFpikWTAPEAANYNRFSIKSDVWSFGILLTEIVTYGRIPYPGMTNAEVLQQVERgyRMPC-PPNCPPQLYD 237
                       250
                ....*....|....
gi 41055987 235 LIKRMLCKKPEDRP 248
Cdd:cd05068 238 IMLECWKADPMERP 251
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
1-260 1.37e-20

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 92.96  E-value: 1.37e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987    1 MDGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDCqLYIV 80
Cdd:PLN00009   1 MDQYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQEDEGVPSTAIREISLLKEMQHGNIVRLQDVVHSEKR-LYLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   81 MGFCEgGDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTK-TNIIKVGDLGIARVLENQND 159
Cdd:PLN00009  80 FEYLD-LDLKKHMDSSPDFAKNPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRrTNALKLADFGLARAFGIPVR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  160 MASTLIGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAFNA-KDMNSL--VYRIV-----------------E 218
Cdd:PLN00009 159 TFTHEVVTLWYRAPEiLLGSRHYSTPVDIWSVGCIFAEMVNQKPLFPGdSEIDELfkIFRILgtpneetwpgvtslpdyK 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 41055987  219 GKLPQMPSK--------YDPQLGELIKRMLCKKPEDRPDVKHILRQPYIK 260
Cdd:PLN00009 239 SAFPKWPPKdlatvvptLEPAGVDLLSKMLRLDPSKRITARAALEHEYFK 288
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
4-283 1.57e-20

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


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 94.18  E-value: 1.57e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQY---VIKKLNLRTSSRRERRAAEQEAQLLSqlKHPNIVMYRESWEGEDcQLYIV 80
Cdd:cd05610   6 FVIVKPISRGAFGKVYLGRKKNNSKLYavkVVKKADMINKNMVHQVQAERDALALS--KSPFIVHLYYSLQSAN-NVYLV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MGFCEGGDLYHRLKQQKgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQ--- 157
Cdd:cd05610  83 MEYLIGGDVKSLLHIYG--YFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKVTLNReln 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 158 --------------NDMAST------------------------------------LIGTPYYMSPELFSNKPYNYKSDV 187
Cdd:cd05610 161 mmdilttpsmakpkNDYSRTpgqvlslisslgfntptpyrtpksvrrgaarvegerILGTPDYLAPELLLGKPHGPAVDW 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 188 WALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKL--PQMPSKYDPQLGELIKRMLCKKPEDRPDVKHILRQPY------- 258
Cdd:cd05610 241 WALGVCLFEFLTGIPPFNDETPQQVFQNILNRDIpwPEGEEELSVNAQNAIEILLTMDPTKRAGLKELKQHPLfhgvdwe 320
                       330       340
                ....*....|....*....|....*.
gi 41055987 259 -IKHQISMFLEATKEKTAKSRKNAAN 283
Cdd:cd05610 321 nLQNQTMPFIPQPDDETDTSYFEARN 346
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
2-261 1.57e-20

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: 93.58  E-value: 1.57e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRReRRAAEQEAQLLSQLKHPNIVMYRESWEgEDCQLYIVM 81
Cdd:cd06650   5 DDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAI-RNQIIRELQVLHECNSPYIVGFYGAFY-SDGEISICM 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  82 GFCEGGDLYHRLKqqKGELLPERQVVEWFVQIAMALQYLHEKH-ILHRDLKTQNIFLTKTNIIKVGDLGIARVLenQNDM 160
Cdd:cd06650  83 EHMDGGSLDQVLK--KAGRIPEQILGKVSIAVIKGLTYLREKHkIMHRDVKPSNILVNSRGEIKLCDFGVSGQL--IDSM 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 161 ASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAF---NAKDMNSLVYRIVEGKL---------------- 221
Cdd:cd06650 159 ANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIpppDAKELELMFGCQVEGDAaetpprprtpgrplss 238
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41055987 222 -----------------------PQMPS-KYDPQLGELIKRMLCKKPEDRPDVKHILRQPYIKH 261
Cdd:cd06650 239 ygmdsrppmaifelldyivneppPKLPSgVFSLEFQDFVNKCLIKNPAERADLKQLMVHAFIKR 302
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
4-259 1.59e-20

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: 93.38  E-value: 1.59e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVR-HKsDRKQYVIKKLNlrtSSRRERRAAEQEAQLLSQLKH------PNIVMYRES--WEGED 74
Cdd:cd14210  15 YEVLSVLGKGSFGQVVKCLdHK-TGQLVAIKIIR---NKKRFHQQALVEVKILKHLNDndpddkHNIVRYKDSfiFRGHL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  75 CqlyIVMgfcE--GGDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLT---KTNiIKVGDLG 149
Cdd:cd14210  91 C---IVF---EllSINLYELLKSNNFQGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKqpsKSS-IKVIDFG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 150 IArVLENQndMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVE----------- 218
Cdd:cd14210 164 SS-CFEGE--KVYTYIQSRFYRAPEVILGLPYDTAIDMWSLGCILAELYTGYPLFPGENEEEQLACIMEvlgvppkslid 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41055987 219 ------------------------------GKLPQMPSKYDPQLGELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd14210 241 kasrrkkffdsngkprpttnskgkkrrpgsKSLAQVLKCDDPSFLDFLKKCLRWDPSERMTPEEALQHPWI 311
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
13-261 2.05e-20

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 91.84  E-value: 2.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   13 GSYGEVNLVRHKSDRKQYVIKKLNLRTSSrrerraaEQE---AQLLSqlKHPNIV-MYrESWEGEDCQLyIVMGFCEGGD 88
Cdd:PHA03390  27 GKFGKVSVLKHKPTQKLFVQKIIKAKNFN-------AIEpmvHQLMK--DNPNFIkLY-YSVTTLKGHV-LIMDYIKDGD 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   89 LYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNI-IKVGDLGIARVlENQndmASTLIGT 167
Cdd:PHA03390  96 LFDLLKKEGK--LSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRAKDrIYLCDYGLCKI-IGT---PSCYDGT 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  168 PYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAF---NAKDMN--SLVYRIvEGKLPqMPSKYDPQLGELIKRMLCK 242
Cdd:PHA03390 170 LDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFkedEDEELDleSLLKRQ-QKKLP-FIKNVSKNANDFVQSMLKY 247
                        250       260
                 ....*....|....*....|
gi 41055987  243 KPEDR-PDVKHILRQPYIKH 261
Cdd:PHA03390 248 NINYRlTNYNEIIKHPFLKI 267
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
10-259 2.24e-20

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


Pssm-ID: 270843 [Multi-domain]  Cd Length: 328  Bit Score: 93.02  E-value: 2.24e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDCQLYIVMGFcEGGDL 89
Cdd:cd07856  18 VGMGAFGLVCSARDQLTGQNVAVKKIMKPFSTPVLAKRTYRELKLLKHLRHENIISLSDIFISPLEDIYFVTEL-LGTDL 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  90 yHRLKQQKgellP-ERQVVEWFV-QIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQndmASTLIGT 167
Cdd:cd07856  97 -HRLLTSR----PlEKQFIQYFLyQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLARIQDPQ---MTGYVST 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 168 PYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKD-------------------------------MNSLVYR 215
Cdd:cd07856 169 RYYRAPEiMLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDhvnqfsiitellgtppddvinticsentlrfVQSLPKR 248
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 41055987 216 iveGKLP--QMPSKYDPQLGELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd07856 249 ---ERVPfsEKFKNADPDAIDLLEKMLVFDPKKRISAAEALAHPYL 291
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
7-255 2.32e-20

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


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 92.30  E-value: 2.32e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   7 VRVVGKGSYGEVNLVRH--KSDRKQYVIKKLNLRTSSRRERRA-AEQEAQLLSQLKHPNIVMYRE-SWEGEDCQLYIVMG 82
Cdd:cd05079   9 IRDLGEGHFGKVELCRYdpEGDNTGEQVAVKSLKPESGGNHIAdLKKEIEILRNLYHENIVKYKGiCTEDGGNGIKLIME 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FCEGGDLYHRLKQQKGELlPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLEN------ 156
Cdd:cd05079  89 FLPSGSLKEYLPRNKNKI-NLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETdkeyyt 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 157 -QNDMASTLigtpYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAK---------------DMNSLVYRIVEGK 220
Cdd:cd05079 168 vKDDLDSPV----FWYAPECLIQSKFYIASDVWSFGVTLYELLTYCDSESSPmtlflkmigpthgqmTVTRLVRVLEEGK 243
                       250       260       270
                ....*....|....*....|....*....|....*
gi 41055987 221 LPQMPSKYDPQLGELIKRMLCKKPEDRPDVKHILR 255
Cdd:cd05079 244 RLPRPPNCPEEVYQLMRKCWEFQPSKRTTFQNLIE 278
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
40-254 2.61e-20

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: 91.27  E-value: 2.61e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  40 SSRRERRAAEQEAQLLSQLKHPNIVMY-----RESWEGEDCQLYIVMGFCEGGDLyHRLKQQKGELlPERQVVEWFVQIA 114
Cdd:cd14012  37 NGKKQIQLLEKELESLKKLRHPNLVSYlafsiERRGRSDGWKVYLLTEYAPGGSL-SELLDSVGSV-PLDTARRWTLQLL 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 115 MALQYLHEKHILHRDLKTQNIFLTK---TNIIKVGDLGIARVLENQNDMAS-TLIGTPYYMSPELF-SNKPYNYKSDVWA 189
Cdd:cd14012 115 EALEYLHRNGVVHKSLHAGNVLLDRdagTGIVKLTDYSLGKTLLDMCSRGSlDEFKQTYWLPPELAqGSKSPTRKTDVWD 194
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41055987 190 LGCCVYEMATLKHAFNAKDMNSLVyrivegklpQMPSKYDPQLGELIKRMLCKKPEDRPDVKHIL 254
Cdd:cd14012 195 LGLLFLQMLFGLDVLEKYTSPNPV---------LVSLDLSASLQDFLSKCLSLDPKKRPTALELL 250
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
10-207 2.64e-20

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: 92.63  E-value: 2.64e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLnlrtsSRRERRAAEQEAQLLSQLK-HPNIVMYRESWEgEDCQLYIVMGFCEGGD 88
Cdd:cd14180  14 LGEGSFSVCRKCRHRQSGQEYAVKII-----SRRMEANTQREVAALRLCQsHPNIVALHEVLH-DQYHTYLVMELLRGGE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  89 LYHRLKQQKgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFL---TKTNIIKVGDLGIARVLENQNDMASTLI 165
Cdd:cd14180  88 LLDRIKKKA--RFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYadeSDGAVLKVIDFGFARLRPQGSRPLQTPC 165
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 41055987 166 GTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAK 207
Cdd:cd14180 166 FTLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSK 207
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
7-256 3.05e-20

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: 91.88  E-value: 3.05e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   7 VRVVGKGSYGEVNLVRH---KSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESW-EGEDCQLYIVMG 82
Cdd:cd05080   9 IRDLGEGHFGKVSLYCYdptNDGTGEMVAVKALKADCGPQHRSGWKQEIDILKTLYHENIVKYKGCCsEQGGKSLQLIME 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FCEGGDLYHRLKQQKGELlpeRQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIA----------R 152
Cdd:cd05080  89 YVPLGSLRDYLPKHSIGL---AQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAkavpegheyyR 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 153 VLENQNDMAstligtpYYMSPELFSNKPYNYKSDVWALGCCVYEMATlkHAFNAKDMNSLVYRIVEGKLPQMPSKYDPQL 232
Cdd:cd05080 166 VREDGDSPV-------FWYAPECLKEYKFYYASDVWSFGVTLYELLT--HCDSSQSPPTKFLEMIGIAQGQMTVVRLIEL 236
                       250       260
                ....*....|....*....|....*
gi 41055987 233 GELIKRMLCkkPEDRP-DVKHILRQ 256
Cdd:cd05080 237 LERGERLPC--PDKCPqEVYHLMKN 259
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
10-248 4.06e-20

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


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 90.76  E-value: 4.06e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKklnlrtsSRRERRAAE------QEAQLLSQLKHPNIVmyreSWEGEDCQ---LYIV 80
Cdd:cd05084   4 IGRGNFGEVFSGRLRADNTPVAVK-------SCRETLPPDlkakflQEARILKQYSHPNIV----RLIGVCTQkqpIYIV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MGFCEGGDLYHRLkQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARvlENQNDM 160
Cdd:cd05084  73 MELVQGGDFLTFL-RTEGPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSR--EEEDGV 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 161 ASTLIGTPY----YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVE--GKLPqMPSKYDPQLGE 234
Cdd:cd05084 150 YAATGGMKQipvkWTAPEALNYGRYSSESDVWSFGILLWETFSLGAVPYANLSNQQTREAVEqgVRLP-CPENCPDEVYR 228
                       250
                ....*....|....
gi 41055987 235 LIKRMLCKKPEDRP 248
Cdd:cd05084 229 LMEQCWEYDPRKRP 242
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
7-199 4.39e-20

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: 90.89  E-value: 4.39e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   7 VRVVGKGSYGEVNLVRHKSDRKQYV---IKKLNlRTSSRRERRAAEQEAQLLSQLKHPNIVmYRESWEGEDCQLYIVMGF 83
Cdd:cd05033   9 EKVIGGGEFGEVCSGSLKLPGKKEIdvaIKTLK-SGYSDKQRLDFLTEASIMGQFDHPNVI-RLEGVVTKSRPVMIVTEY 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGGDLYHRLKQQKGELLPErQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMAST 163
Cdd:cd05033  87 MENGSLDKFLRENDGKFTVT-QLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLSRRLEDSEATYTT 165
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 41055987 164 LIG-TPY-YMSPELFSNKPYNYKSDVWALGCCVYEMAT 199
Cdd:cd05033 166 KGGkIPIrWTAPEAIAYRKFTSASDVWSFGIVMWEVMS 203
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
10-258 4.50e-20

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: 91.16  E-value: 4.50e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQ--YVIKKLNLRTSsRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcqLYIVMGFCEGG 87
Cdd:cd05115  12 LGSGNFGCVKKGVYKMRKKQidVAIKVLKQGNE-KAVRDEMMREAQIMHQLDNPYIVRMIGVCEAEA--LMLVMEMASGG 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  88 DLyHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLIGT 167
Cdd:cd05115  89 PL-NKFLSGKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLSKALGADDSYYKARSAG 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 168 PY---YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVE-GKLPQMPSKYDPQLGELIKRMLCKK 243
Cdd:cd05115 168 KWplkWYAPECINFRKFSSRSDVWSYGVTMWEAFSYGQKPYKKMKGPEVMSFIEqGKRMDCPAECPPEMYALMSDCWIYK 247
                       250
                ....*....|....*...
gi 41055987 244 PEDRPD---VKHILRQPY 258
Cdd:cd05115 248 WEDRPNfltVEQRMRTYY 265
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
10-258 6.92e-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: 92.02  E-value: 6.92e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRE------SWEgEDCQLYIVMGF 83
Cdd:cd07877  25 VGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDvftparSLE-EFNDVYLVTHL 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CeGGDLYHRLKQQKgelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARvleNQNDMAST 163
Cdd:cd07877 104 M-GADLNNIVKCQK---LTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLAR---HTDDEMTG 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 164 LIGTPYYMSPELFSN-KPYNYKSDVWALGCCVYEMATLKHAFNAKD----------------------MNSLVYRIVEGK 220
Cdd:cd07877 177 YVATRWYRAPEIMLNwMHYNQTVDIWSVGCIMAELLTGRTLFPGTDhidqlklilrlvgtpgaellkkISSESARNYIQS 256
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 41055987 221 LPQMPSK--------YDPQLGELIKRMLCKKPEDRPDVKHILRQPY 258
Cdd:cd07877 257 LTQMPKMnfanvfigANPLAVDLLEKMLVLDSDKRITAAQALAHAY 302
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
4-258 9.73e-20

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: 90.48  E-value: 9.73e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYV-IKKLNLRTSSRRERRAAEQEAQLLSQLK---HPNIVMYRE----SWEGEDC 75
Cdd:cd07862   3 YECVAEIGEGAYGKVFKARDLKNGGRFVaLKRVRVQTGEEGMPLSTIREVAVLRHLEtfeHPNVVRLFDvctvSRTDRET 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  76 QLYIVMGFCEGgDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLE 155
Cdd:cd07862  83 KLTLVFEHVDQ-DLTTYLDKVPEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLARIYS 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 156 NQNDMASTLIgTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAK-DMNSL--VYRIV----------EGKLP 222
Cdd:cd07862 162 FQMALTSVVV-TLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFRGSsDVDQLgkILDVIglpgeedwprDVALP 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 41055987 223 QMP---------SKYDPQLGELIKRMLCK----KPEDRPDVKHILRQPY 258
Cdd:cd07862 241 RQAfhsksaqpiEKFVTDIDELGKDLLLKcltfNPAKRISAYSALSHPY 289
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
10-260 1.19e-19

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: 91.26  E-value: 1.19e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRReRRAAEQEAQLLSQLKHPNIVMYRESWEgEDCQLYIVMGFCEGGDL 89
Cdd:cd06649  13 LGAGNGGVVTKVQHKPSGLIMARKLIHLEIKPAI-RNQIIRELQVLHECNSPYIVGFYGAFY-SDGEISICMEHMDGGSL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  90 YHRLKQQKgeLLPERQVVEWFVQIAMALQYLHEKH-ILHRDLKTQNIFLTKTNIIKVGDLGIARVLenQNDMASTLIGTP 168
Cdd:cd06649  91 DQVLKEAK--RIPEEILGKVSIAVLRGLAYLREKHqIMHRDVKPSNILVNSRGEIKLCDFGVSGQL--IDSMANSFVGTR 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 169 YYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAF---NAKDMNSLVYR------------------------------ 215
Cdd:cd06649 167 SYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYPIpppDAKELEAIFGRpvvdgeegephsisprprppgrpvsghgmd 246
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 41055987 216 -------------IVEGKLPQMPSK-YDPQLGELIKRMLCKKPEDRPDVKHILRQPYIK 260
Cdd:cd06649 247 srpamaifelldyIVNEPPPKLPNGvFTPDFQEFVNKCLIKNPAERADLKMLMNHTFIK 305
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
9-197 1.28e-19

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: 89.54  E-value: 1.28e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   9 VVGKGSYGEV--NLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVmYRESWEGEDCQLYIVMGFCEG 86
Cdd:cd05065  11 VIGAGEFGEVcrGRLKLPGKREIFVAIKTLKSGYTEKQRRDFLSEASIMGQFDHPNII-HLEGVVTKSRPVMIITEFMEN 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  87 GDLYHRLKQQKGELLPeRQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQND---MAST 163
Cdd:cd05065  90 GALDSFLRQNDGQFTV-IQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLEDDTSdptYTSS 168
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 41055987 164 LIGT-PY-YMSPELFSNKPYNYKSDVWALGCCVYEM 197
Cdd:cd05065 169 LGGKiPIrWTAPEAIAYRKFTSASDVWSYGIVMWEV 204
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
10-197 1.34e-19

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: 89.12  E-value: 1.34e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKlnlrTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEgEDCQLYIVMGFCEGGDL 89
Cdd:cd14156   1 IGSGFFSKVYKVTHGATGKVMVVKI----YKNDVDQHKIVREISLLQKLSHPNIVRYLGICV-KDEKLHPILEYVSGGCL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  90 YHRLKQQkgEL-LPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIK---VGDLGIARVL----ENQNDMA 161
Cdd:cd14156  76 EELLARE--ELpLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGReavVTDFGLAREVgempANDPERK 153
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 41055987 162 STLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEM 197
Cdd:cd14156 154 LSLVGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEI 189
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
10-253 1.39e-19

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


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 89.21  E-value: 1.39e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKqYVIKKLNLRTSSRRerrAAEQEAQLLSQLKHPNIVMYRESWEGEdcQLYIVMGFCEGGDL 89
Cdd:cd14203   3 LGQGCFGEVWMGTWNGTTK-VAIKTLKPGTMSPE---AFLEEAQIMKKLRHDKLVQLYAVVSEE--PIYIVTEFMSKGSL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  90 YHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLIGTPY 169
Cdd:cd14203  77 LDFLKDGEGKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQGAKFPI 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 170 -YMSPELFSNKPYNYKSDVWALGCCVYEMATlKHAFNAKDMNS--LVYRIVEGKLPQMPSKYDPQLGELIKRMLCKKPED 246
Cdd:cd14203 157 kWTAPEAALYGRFTIKSDVWSFGILLTELVT-KGRVPYPGMNNreVLEQVERGYRMPCPPGCPESLHELMCQCWRKDPEE 235

                ....*..
gi 41055987 247 RPDVKHI 253
Cdd:cd14203 236 RPTFEYL 242
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
10-226 1.59e-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: 90.24  E-value: 1.59e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNlRTSSRRERRAAEQEAQLLSQLKHPNIV-MYRESWEGEDCQLYIVMGFCEGGD 88
Cdd:cd13988   1 LGQGATANVFRGRHKKTGDLYAVKVFN-NLSFMRPLDVQMREFEVLKKLNHKNIVkLFAIEEELTTRHKVLVMELCPCGS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  89 LYHRLKQQKGEL-LPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLT----KTNIIKVGDLGIARVLENQNDMASt 163
Cdd:cd13988  80 LYTVLEEPSNAYgLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMRVigedGQSVYKLTDFGAARELEDDEQFVS- 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41055987 164 LIGTPYYMSPELF--------SNKPYNYKSDVWALGCCVYEMATLKHAF----NAKDMNSLVYRIVEGKLPQMPS 226
Cdd:cd13988 159 LYGTEEYLHPDMYeravlrkdHQKKYGATVDLWSIGVTFYHAATGSLPFrpfeGPRRNKEVMYKIITGKPSGAIS 233
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
2-195 1.64e-19

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: 89.31  E-value: 1.64e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLnLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVM 81
Cdd:cd14088   1 DRYDLGQVIKTEEFCEIFRAKDKTTGKLYTCKKF-LKRDGRKVRKAAKNEINILKMVKHPNILQLVDVFETRK-EYFIFL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  82 GFCEGGDLYHRLKQQKgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFL---TKTNIIKVGDLGIARVlenQN 158
Cdd:cd14088  79 ELATGREVFDWILDQG--YYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYynrLKNSKIVISDFHLAKL---EN 153
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 41055987 159 DMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVY 195
Cdd:cd14088 154 GLIKEPCGTPEYLAPEVVGRQRYGRPVDCWAIGVIMY 190
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
10-253 2.14e-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: 89.36  E-value: 2.14e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVnLVRHKSDRKQYVIKKLNLRTSSRRerrAAEQEAQLLSQLKHPNIVMYRESWEGEdcQLYIVMGFCEGGDL 89
Cdd:cd05071  17 LGQGCFGEV-WMGTWNGTTRVAIKTLKPGTMSPE---AFLQEAQVMKKLRHEKLVQLYAVVSEE--PIYIVTEYMSKGSL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  90 YHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLIGTPY 169
Cdd:cd05071  91 LDFLKGEMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAKFPI 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 170 -YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVE-GKLPQMPSKYDPQLGELIKRMLCKKPEDR 247
Cdd:cd05071 171 kWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVErGYRMPCPPECPESLHDLMCQCWRKEPEER 250

                ....*.
gi 41055987 248 PDVKHI 253
Cdd:cd05071 251 PTFEYL 256
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
6-256 2.18e-19

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: 88.50  E-value: 2.18e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   6 FVRVVGKGSYGEVNLVRHKSdrKQYVIKKLNLRTSSRrerrAAEQEAQLLSQLKHPNIVMYRESWEGEDCQLYIVMGFCE 85
Cdd:cd05082  10 LLQTIGKGEFGDVMLGDYRG--NKVAVKCIKNDATAQ----AFLAEASVMTQLRHSNLVQLLGVIVEEKGGLYIVTEYMA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  86 GGDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLI 165
Cdd:cd05082  84 KGSLVDYLRSRGRSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEASSTQDTGKLPV 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 166 GtpyYMSPELFSNKPYNYKSDVWALGCCVYEMATL-KHAFNAKDMNSLVYRIVEGKLPQMPSKYDPQLGELIKRMLCKKP 244
Cdd:cd05082 164 K---WTAPEALREKKFSTKSDVWSFGILLWEIYSFgRVPYPRIPLKDVVPRVEKGYKMDAPDGCPPAVYDVMKNCWHLDA 240
                       250
                ....*....|..
gi 41055987 245 EDRPDVKHILRQ 256
Cdd:cd05082 241 AMRPSFLQLREQ 252
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
11-248 3.04e-19

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: 88.09  E-value: 3.04e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  11 GKGSYGevNLVRHKSDRKQYVIKKLNLRTSSRRERraaeQEAQLLSQLKHPNIVMYRESweGEDCQLyIVMGFCEGGDLY 90
Cdd:cd14068   3 GDGGFG--SVYRAVYRGEDVAVKIFNKHTSFRLLR----QELVVLSHLHHPSLVALLAA--GTAPRM-LVMELAPKGSLD 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  91 HRLKQQKGELLPERQVvEWFVQIAMALQYLHEKHILHRDLKTQNI--FLTKTN---IIKVGDLGIARVLENQNdmASTLI 165
Cdd:cd14068  74 ALLQQDNASLTRTLQH-RIALHVADGLRYLHSAMIIYRDLKPHNVllFTLYPNcaiIAKIADYGIAQYCCRMG--IKTSE 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 166 GTPYYMSPELF-SNKPYNYKSDVWALGCCVYEMATL--KHAFNAKDMNSLVYRIVEGKLPQMPSKYD----PQLGELIKR 238
Cdd:cd14068 151 GTPGFRAPEVArGNVIYNQQADVYSFGLLLYDILTCgeRIVEGLKFPNEFDELAIQGKLPDPVKEYGcapwPGVEALIKD 230
                       250
                ....*....|
gi 41055987 239 MLCKKPEDRP 248
Cdd:cd14068 231 CLKENPQCRP 240
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
10-195 3.24e-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: 88.04  E-value: 3.24e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTssrRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDCqLYIVMGFCEGGDL 89
Cdd:cd14108  10 IGRGAFSYLRRVKEKSSDLSFAAKFIPVRA---KKKTSARRELALLAELDHKSIVRFHDAFEKRRV-VIIVTELCHEELL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  90 YHRLKQQKgelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFL--TKTNIIKVGDLGIARVLeNQNDMASTLIGT 167
Cdd:cd14108  86 ERITKRPT---VCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMadQKTDQVRICDFGNAQEL-TPNEPQYCKYGT 161
                       170       180
                ....*....|....*....|....*...
gi 41055987 168 PYYMSPELFSNKPYNYKSDVWALGCCVY 195
Cdd:cd14108 162 PEFVAPEIVNQSPVSKVTDIWPVGVIAY 189
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
10-197 3.43e-19

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: 90.48  E-value: 3.43e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRhKSDRKQYV-IKKLNLRTSSRR-ERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEGG 87
Cdd:cd05600  19 VGQGGYGSVFLAR-KKDTGEICaLKIMKKKVLFKLnEVNHVLTERDILTTTNSPWLVKLLYAFQDPE-NVYLAMEYVPGG 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  88 DlYHRLKQQKGeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIAR--------------- 152
Cdd:cd05600  97 D-FRTLLNNSG-ILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGLASgtlspkkiesmkirl 174
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41055987 153 ----------------------VLENQNDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEM 197
Cdd:cd05600 175 eevkntafleltakerrniyraMRKEDQNYANSVVGSPDYMAPEVLRGEGYDLTVDYWSLGCILFEC 241
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
4-258 4.52e-19

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: 89.58  E-value: 4.52e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESW----EGEDCQ-LY 78
Cdd:cd07879  17 YTSLKQVGSGAYGSVCSAIDKRTGEKVAIKKLSRPFQSEIFAKRAYRELTLLKHMQHENVIGLLDVFtsavSGDEFQdFY 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  79 IVMGFceggdLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARvlENQN 158
Cdd:cd07879  97 LVMPY-----MQTDLQKIMGHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGLAR--HADA 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 159 DMASTLIgTPYYMSPELFSN-KPYNYKSDVWALGCCVYEMATLKHAFNAKD----------------------MNSLVYR 215
Cdd:cd07879 170 EMTGYVV-TRWYRAPEVILNwMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDyldqltqilkvtgvpgpefvqkLEDKAAK 248
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 41055987 216 IVEGKLPQMPSK--------YDPQLGELIKRMLCKKPEDRPDVKHILRQPY 258
Cdd:cd07879 249 SYIKSLPKYPRKdfstlfpkASPQAVDLLEKMLELDVDKRLTATEALEHPY 299
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
9-197 5.23e-19

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


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 88.24  E-value: 5.23e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   9 VVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERraAEQEAQLLSQLK-HPNIVMYRESWEgEDCQLYIVMGFCEGG 87
Cdd:cd14090   9 LLGEGAYASVQTCINLYTGKEYAVKIIEKHPGHSRSR--VFREVETLHQCQgHPNILQLIEYFE-DDERFYLVFEKMRGG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  88 DLYHRLKQQKgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNII---KVGDLGIAR-VLENQNDMA-- 161
Cdd:cd14090  86 PLLSHIEKRV--HFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKVspvKICDFDLGSgIKLSSTSMTpv 163
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 41055987 162 -----STLIGTPYYMSPE---LFSNKPYNY--KSDVWALGCCVYEM 197
Cdd:cd14090 164 ttpelLTPVGSAEYMAPEvvdAFVGEALSYdkRCDLWSLGVILYIM 209
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
2-196 5.41e-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: 89.91  E-value: 5.41e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLnLRTSSRRERRAAEQEAQ--LLSQLKHPNIVMYRESWegEDCQ-LY 78
Cdd:cd05629   1 EDFHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTL-LKSEMFKKDQLAHVKAErdVLAESDSPWVVSLYYSF--QDAQyLY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  79 IVMGFCEGGDLYHRLKqqKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQN 158
Cdd:cd05629  78 LIMEFLPGGDLMTMLI--KYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGLSTGFHKQH 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 159 D-----------------------------------------------MASTLIGTPYYMSPELFSNKPYNYKSDVWALG 191
Cdd:cd05629 156 DsayyqkllqgksnknridnrnsvavdsinltmsskdqiatwkknrrlMAYSTVGTPDYIAPEIFLQQGYGQECDWWSLG 235

                ....*
gi 41055987 192 CCVYE 196
Cdd:cd05629 236 AIMFE 240
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
4-201 5.87e-19

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: 88.53  E-value: 5.87e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIV-----MYRESWEGEDCQ-- 76
Cdd:cd07866  10 YEILGKLGEGTFGEVYKARQIKTGRVVALKKILMHNEKDGFPITALREIKILKKLKHPNVVplidmAVERPDKSKRKRgs 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  77 LYIVMGFCEGgDLYHRLKQQKGELLPErQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLEN 156
Cdd:cd07866  90 VYMVTPYMDH-DLSGLLENPSVKLTES-QIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADFGLARPYDG 167
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41055987 157 ----------QNDMAST-LIGTPYYMSPEL-FSNKPYNYKSDVWALGCCVYEMATLK 201
Cdd:cd07866 168 pppnpkggggGGTRKYTnLVVTRWYRPPELlLGERRYTTAVDIWGIGCVFAEMFTRR 224
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
3-259 7.15e-19

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: 88.62  E-value: 7.15e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   3 GYLFVRVVGKGSYGEVNLVRHK--SDRKQYVIKKL-NLRTSSRRERRAAeQEAQLLSQLK-HPNIVMYRES---WEGEDC 75
Cdd:cd07857   1 RYELIKELGQGAYGIVCSARNAetSEEETVAIKKItNVFSKKILAKRAL-RELKLLRHFRgHKNITCLYDMdivFPGNFN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  76 QLYIVMGFCEGgDLYHRLKQqkGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVL- 154
Cdd:cd07857  80 ELYLYEELMEA-DLHQIIRS--GQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLARGFs 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 155 ----ENQNDMaSTLIGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKD----MNSLVY----------- 214
Cdd:cd07857 157 enpgENAGFM-TEYVATRWYRAPEiMLSFQSYTKAIDVWSVGCILAELLGRKPVFKGKDyvdqLNQILQvlgtpdeetls 235
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 215 RIVEGK-------LPQMPSK--------YDPQLGELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd07857 236 RIGSPKaqnyirsLPNIPKKpfesifpnANPLALDLLEKLLAFDPTKRISVEEALEHPYL 295
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
9-256 8.15e-19

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: 87.40  E-value: 8.15e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   9 VVGKGSYGEVNLVRHKSD--RKQYVIKKLNlRTSSRRERRAAEQEAQLLSQL-KHPNIVMYRESWEGEDcQLYIVMGFCE 85
Cdd:cd05047   2 VIGEGNFGQVLKARIKKDglRMDAAIKRMK-EYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRG-YLYLAIEYAP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  86 GGDLYHRLKQQK--------------GELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIA 151
Cdd:cd05047  80 HGNLLDFLRKSRvletdpafaianstASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 152 RVLENQndMASTLIGTPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLVYRIVEGKLPQMPSKYD 229
Cdd:cd05047 160 RGQEVY--VKKTMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTpYCGMTCAELYEKLPQGYRLEKPLNCD 237
                       250       260
                ....*....|....*....|....*..
gi 41055987 230 PQLGELIKRMLCKKPEDRPDVKHILRQ 256
Cdd:cd05047 238 DEVYDLMRQCWREKPYERPSFAQILVS 264
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
6-199 9.57e-19

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: 87.26  E-value: 9.57e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   6 FVRVVGKGSYGEVNLVRHK--SDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRE-SWEGEDCQLYIVMG 82
Cdd:cd05081   8 YISQLGKGNFGSVELCRYDplGDNTGALVAVKQLQHSGPDQQRDFQREIQILKALHSDFIVKYRGvSYGPGRRSLRLVME 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FCEGGDLYHRLKQQKGELLPeRQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMas 162
Cdd:cd05081  88 YLPSGCLRDFLQRHRARLDA-SRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLLPLDKDY-- 164
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 41055987 163 TLIGTP-----YYMSPELFSNKPYNYKSDVWALGCCVYEMAT 199
Cdd:cd05081 165 YVVREPgqspiFWYAPESLSDNIFSRQSDVWSFGVVLYELFT 206
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
2-216 1.01e-18

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-1 is widely expressed except in the spleen and thymus. It is highly expressed in the brain, heart, pancreas, testis, and ovary, and is localized in the cytoplasm. It is regulated by cyclin D3 and is inhibited by the p21 cell cycle inhibitor. It has also been shown to interact with the membrane-associated cyclin Y, which recruits the protein to the plasma membrane. PFTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 87.83  E-value: 1.01e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAeQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVM 81
Cdd:cd07869   5 DSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTAI-REASLLKGLKHANIVLLHDIIHTKE-TLTLVF 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  82 GFCEGgDLYHRLKQQKGELLPErQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMA 161
Cdd:cd07869  83 EYVHT-DLCQYMDKHPGGLHPE-NVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARAKSVPSHTY 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41055987 162 STLIGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAF-NAKDMNSLVYRI 216
Cdd:cd07869 161 SNEVVTLWYRPPDvLLGSTEYSTCLDMWGVGCIFVEMIQGVAAFpGMKDIQDQLERI 217
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
8-197 1.02e-18

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: 86.84  E-value: 1.02e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKQYV---IKKLNLrTSSRRERRAAEQEAQLLSQLKHPNIVmYRESWEGEDCQLYIVMGFC 84
Cdd:cd05066  10 KVIGAGEFGEVCSGRLKLPGKREIpvaIKTLKA-GYTEKQRRDFLSEASIMGQFDHPNII-HLEGVVTRSKPVMIVTEYM 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  85 EGGDLYHRLKQQKGELLPeRQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTL 164
Cdd:cd05066  88 ENGSLDAFLRKHDGQFTV-IQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDPEAAYTT 166
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 41055987 165 IGTPY---YMSPELFSNKPYNYKSDVWALGCCVYEM 197
Cdd:cd05066 167 RGGKIpirWTAPEAIAYRKFTSASDVWSYGIVMWEV 202
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
4-264 1.04e-18

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: 88.20  E-value: 1.04e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNL----RTSSRRERRaaeqEAQLLSQLKHPNIV--------MYRESWE 71
Cdd:cd07858   7 YVPIKPIGRGAYGIVCSAKNSETNEKVAIKKIANafdnRIDAKRTLR----EIKLLRHLDHENVIaikdimppPHREAFN 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  72 gedcQLYIVMGFCEGgDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIA 151
Cdd:cd07858  83 ----DVYIVYELMDT-DLHQIIRSSQT--LSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 152 RVLENQNDMASTLIGTPYYMSPELFSN-KPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVE------------ 218
Cdd:cd07858 156 RTTSEKGDFMTEYVVTRWYRAPELLLNcSEYTTAIDVWSVGCIFAELLGRKPLFPGKDYVHQLKLITEllgspseedlgf 235
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41055987 219 ----------GKLPQMP--------SKYDPQLGELIKRMLCKKPEDRPDVKHILRQPYIK--HQIS 264
Cdd:cd07858 236 irnekarryiRSLPYTPrqsfarlfPHANPLAIDLLEKMLVFDPSKRITVEEALAHPYLAslHDPS 301
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
11-257 1.15e-18

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: 86.90  E-value: 1.15e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  11 GKGSYGEVNLVRHKSdrKQYVIKKLNLRTSSRRER-------------------RAAEQEAQLLSQLKHPNIVMYRESWE 71
Cdd:cd14000   3 GDGGFGSVYRASYKG--EPVAVKIFNKHTSSNFANvpadtmlrhlratdamknfRLLRQELTVLSHLHHPSIVYLLGIGI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  72 GEDCqlyIVMGFCEGGDLYHRLKQQK------GELLPERQVVewfvQIAMALQYLHEKHILHRDLKTQNIFLTKTN---- 141
Cdd:cd14000  81 HPLM---LVLELAPLGSLDHLLQQDSrsfaslGRTLQQRIAL----QVADGLRYLHSAMIIYRDLKSHNVLVWTLYpnsa 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 142 -IIKVGDLGIARvlENQNDMASTLIGTPYYMSPELFS-NKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEG 219
Cdd:cd14000 154 iIIKIADYGISR--QCCRMGAKGSEGTPGFRAPEIARgNVIYNEKVDVFSFGMLLYEILSGGAPMVGHLKFPNEFDIHGG 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 41055987 220 KLP---QMPSKYDPQLGELIKRMLCKKPEDRP---DVKHILRQP 257
Cdd:cd14000 232 LRPplkQYECAPWPEVEVLMKKCWKENPQQRPtavTVVSILNSP 275
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
10-197 1.18e-18

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: 86.92  E-value: 1.18e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLnLRTSSRRERRAAeQEAQLLSQLKHPNI-----VMYReswegeDCQLYIVMGFC 84
Cdd:cd14222   1 LGKGFFGQAIKVTHKATGKVMVMKEL-IRCDEETQKTFL-TEVKVMRSLDHPNVlkfigVLYK------DKRLNLLTEFI 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  85 EGGDLYHRLKQQkgELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVL---------- 154
Cdd:cd14222  73 EGGTLKDFLRAD--DPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveekkkpppd 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 41055987 155 ----------ENQNDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEM 197
Cdd:cd14222 151 kpttkkrtlrKNDRKKRYTVVGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCEI 203
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
10-248 1.50e-18

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


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 86.17  E-value: 1.50e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAE--QEAQLLSQLKHPNIVMYRESWEGEDCQLyiVMGFCEGG 87
Cdd:cd05116   3 LGSGNFGTVKKGYYQMKKVVKTVAVKILKNEANDPALKDEllREANVMQQLDNPYIVRMIGICEAESWML--VMEMAELG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  88 DLYHRLkqQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVL---ENQNDMASTL 164
Cdd:cd05116  81 PLNKFL--QKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKALradENYYKAQTHG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 165 IGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATL-KHAFNAKDMNSLVYRIVEGKLPQMPSKYDPQLGELIKRMLCKK 243
Cdd:cd05116 159 KWPVKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSYgQKPYKGMKGNEVTQMIEKGERMECPAGCPPEMYDLMKLCWTYD 238

                ....*
gi 41055987 244 PEDRP 248
Cdd:cd05116 239 VDERP 243
PK_NRBP1_like cd13984
Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The ...
40-257 1.78e-18

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: 86.05  E-value: 1.78e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  40 SSRRERRAAEQEA----QLLSQLKHPNIVMYRESW---EGEDCQLYIVMGFCEGGDLYHRLKQQK--GELLPERQVVEWF 110
Cdd:cd13984  30 SERKIFKAQEEKIravfDNLIQLDHPNIVKFHRYWtdvQEEKARVIFITEYMSSGSLKQFLKKTKknHKTMNEKSWKRWC 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 111 VQIAMALQYLH--EKHILHRDLKTQNIFLTKTNIIKVGDLgIARVLENQNDMASTLIGTPYYMSPELFSNKPYNYKSDVW 188
Cdd:cd13984 110 TQILSALSYLHscDPPIIHGNLTCDTIFIQHNGLIKIGSV-APDAIHNHVKTCREEHRNLHFFAPEYGYLEDVTTAVDIY 188
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41055987 189 ALGCCVYEMATLKhafnAKDMNSLVYRIVEGKLPQMPSKYDPQLGELIKRMLCKKPEDRPDVKHILRQP 257
Cdd:cd13984 189 SFGMCALEMAALE----IQSNGEKVSANEEAIIRAIFSLEDPLQKDFIRKCLSVAPQDRPSARDLLFHP 253
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
8-256 1.78e-18

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: 86.78  E-value: 1.78e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSdrKQYVIKKLN--LRTSSRRERRAAEQEAQLLSQLKHPNIV-MYRESWEGED-CQLYIVMgf 83
Cdd:cd14158  21 NKLGEGGFGVVFKGYIND--KNVAVKKLAamVDISTEDLTKQFEQEIQVMAKCQHENLVeLLGYSCDGPQlCLVYTYM-- 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 cEGGDLYHRLKQQKGEL-LPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLE--NQNDM 160
Cdd:cd14158  97 -PNGSLLDRLACLNDTPpLSWHMRCKIAQGTANGINYLHENNHIHRDIKSANILLDETFVPKISDFGLARASEkfSQTIM 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 161 ASTLIGTPYYMSPELFSNKpYNYKSDVWALGCCVYEMAT--------------LKHAFNAKDMNSLVYRIVEGKLPQMPS 226
Cdd:cd14158 176 TERIVGTTAYMAPEALRGE-ITPKSDIFSFGVVLLEIITglppvdenrdpqllLDIKEEIEDEEKTIEDYVDKKMGDWDS 254
                       250       260       270
                ....*....|....*....|....*....|
gi 41055987 227 KYDPQLGELIKRMLCKKPEDRPDVKHILRQ 256
Cdd:cd14158 255 TSIEAMYSVASQCLNDKKNRRPDIAKVQQL 284
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
1-206 1.89e-18

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: 86.78  E-value: 1.89e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   1 MDGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRE---------SWE 71
Cdd:cd07864   6 VDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLNHRSVVNLKEivtdkqdalDFK 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  72 GEDCQLYIV--------MGFCEGGdLYHrlkqqkgelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNII 143
Cdd:cd07864  86 KDKGAFYLVfeymdhdlMGLLESG-LVH---------FSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQI 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41055987 144 KVGDLGIARVLENQNDMAST-LIGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAFNA 206
Cdd:cd07864 156 KLADFGLARLYNSEESRPYTnKVITLWYRPPElLLGEERYGPAIDVWSCGCILGELFTKKPIFQA 220
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
9-259 2.04e-18

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: 86.47  E-value: 2.04e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   9 VVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAeQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEGG- 87
Cdd:cd06619   8 ILGHGNGGTVYKAYHLLTRRILAVKVIPLDITVELQKQIM-SELEILYKCDSPYIIGFYGAFFVEN-RISICTEFMDGGs 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  88 -DLYHRLkqqkgellPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLenQNDMASTLIG 166
Cdd:cd06619  86 lDVYRKI--------PEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQL--VNSIAKTYVG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 167 TPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMN-------SLVYRIVEGKLPQMP-SKYDPQLGELIKR 238
Cdd:cd06619 156 TNAYMAPERISGEQYGIHSDVWSLGISFMELALGRFPYPQIQKNqgslmplQLLQCIVDEDPPVLPvGQFSEKFVHFITQ 235
                       250       260
                ....*....|....*....|.
gi 41055987 239 MLCKKPEDRPDVKHILRQPYI 259
Cdd:cd06619 236 CMRKQPKERPAPENLMDHPFI 256
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
9-247 2.29e-18

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: 86.34  E-value: 2.29e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   9 VVGKGSYGEVNLVRHKSDRKQYVIKKLNL-RTSSRRERRAAEQEAQLLSQLKH----PNIVMYRESWEGEDcQLYIVMGF 83
Cdd:cd05606   1 IIGRGGFGEVYGCRKADTGKMYAMKCLDKkRIKMKQGETLALNERIMLSLVSTggdcPFIVCMTYAFQTPD-KLCFILDL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGGDLYHRLKQQKgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASt 163
Cdd:cd05606  80 MNGGDLHYHLSQHG--VFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLACDFSKKKPHAS- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 164 lIGTPYYMSPELFSN-KPYNYKSDVWALGCCVYEMATLKHAF---NAKDMNSlVYRIVEGKLPQMPSKYDPQLGELIKRM 239
Cdd:cd05606 157 -VGTHGYMAPEVLQKgVAYDSSADWFSLGCMLYKLLKGHSPFrqhKTKDKHE-IDRMTLTMNVELPDSFSPELKSLLEGL 234

                ....*...
gi 41055987 240 LCKKPEDR 247
Cdd:cd05606 235 LQRDVSKR 242
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
9-260 3.26e-18

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: 85.29  E-value: 3.26e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   9 VVGKGSYGEVNLVRHKSDRKQYVIKKLN----LRTSSRRERRAAEQEAQLLSQL----KHPNIVMYRESWEGEDCQLYIV 80
Cdd:cd14101   7 LLGKGGFGTVYAGHRISDGLQVAIKQISrnrvQQWSKLPGVNPVPNEVALLQSVgggpGHRGVIRLLDWFEIPEGFLLVL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MGFCEGGDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFL-TKTNIIKVGDLGIARVLenQND 159
Cdd:cd14101  87 ERPQHCQDLFDYITERGA--LDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVdLRTGDIKLIDFGSGATL--KDS 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 160 MASTLIGTPYYMSPELFSNKPYN-YKSDVWALGCCVYEMATLKHAFNaKDMNslvyrIVEGKlPQMPSKYDPQLGELIKR 238
Cdd:cd14101 163 MYTDFDGTRVYSPPEWILYHQYHaLPATVWSLGILLYDMVCGDIPFE-RDTD-----ILKAK-PSFNKRVSNDCRSLIRS 235
                       250       260
                ....*....|....*....|..
gi 41055987 239 MLCKKPEDRPDVKHILRQPYIK 260
Cdd:cd14101 236 CLAYNPSDRPSLEQILLHPWMM 257
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
10-254 3.33e-18

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


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 86.22  E-value: 3.33e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLV------RHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQL-KHPNIVMYRESWEgEDCQLYIVMG 82
Cdd:cd05098  21 LGEGCFGQVVLAeaigldKDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIgKHKNIINLLGACT-QDGPLYVIVE 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FCEGGDL--YHRLKQQKG------------ELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDL 148
Cdd:cd05098 100 YASKGNLreYLQARRPPGmeycynpshnpeEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIADF 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 149 GIARVLENQNDMASTLIGT-PY-YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLVYRIVEGKLPQMP 225
Cdd:cd05098 180 GLARDIHHIDYYKKTTNGRlPVkWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSpYPGVPVEELFKLLKEGHRMDKP 259
                       250       260
                ....*....|....*....|....*....
gi 41055987 226 SKYDPQLGELIKRMLCKKPEDRPDVKHIL 254
Cdd:cd05098 260 SNCTNELYMMMRDCWHAVPSQRPTFKQLV 288
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
10-253 3.36e-18

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: 85.89  E-value: 3.36e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKqYVIKKLNLRTSSRRerrAAEQEAQLLSQLKHPNIVMYRESWEGEdcQLYIVMGFCEGGDL 89
Cdd:cd05069  20 LGQGCFGEVWMGTWNGTTK-VAIKTLKPGTMMPE---AFLQEAQIMKKLRHDKLVPLYAVVSEE--PIYIVTEFMGKGSL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  90 YHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLIGTPY 169
Cdd:cd05069  94 LDFLKEGDGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQGAKFPI 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 170 -YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVE-GKLPQMPSKYDPQLGELIKRMLCKKPEDR 247
Cdd:cd05069 174 kWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMVNREVLEQVErGYRMPCPQGCPESLHELMKLCWKKDPDER 253

                ....*.
gi 41055987 248 PDVKHI 253
Cdd:cd05069 254 PTFEYI 259
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
2-258 4.57e-18

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: 86.54  E-value: 4.57e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDC-----Q 76
Cdd:cd07880  15 DRYRDLKQVGSGAYGTVCSALDRRTGAKVAIKKLYRPFQSELFAKRAYRELRLLKHMKHENVIGLLDVFTPDLSldrfhD 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  77 LYIVMGFCeGGDLYHRLKQQKgelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARvlEN 156
Cdd:cd07880  95 FYLVMPFM-GTDLGKLMKHEK---LSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLAR--QT 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 157 QNDMASTLIgTPYYMSPELFSN-KPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVE----------------- 218
Cdd:cd07880 169 DSEMTGYVV-TRWYRAPEVILNwMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHLDQLMEIMKvtgtpskefvqklqsed 247
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 41055987 219 -----GKLPQMPSK--------YDPQLGELIKRMLCKKPEDRPDVKHILRQPY 258
Cdd:cd07880 248 aknyvKKLPRFRKKdfrsllpnANPLAVNVLEKMLVLDAESRITAAEALAHPY 300
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
4-204 4.69e-18

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: 85.40  E-value: 4.69e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAeQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGF 83
Cdd:cd07870   2 YLNLEKLGEGSYATVYKGISRINGQLVALKVISMKTEEGVPFTAI-REASLLKGLKHANIVLLHDIIHTKE-TLTFVFEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGgDLYHRLKQQKGELLPeRQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMAST 163
Cdd:cd07870  80 MHT-DLAQYMIQHPGGLHP-YNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLARAKSIPSQTYSS 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 41055987 164 LIGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAF 204
Cdd:cd07870 158 EVVTLWYRPPDvLLGATDYSSALDIWGAGCIFIEMLQGQPAF 199
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
10-197 5.09e-18

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: 85.01  E-value: 5.09e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLnLRTSSRRERRAAeQEAQLLSQLKHPNI-----VMYRESwegedcQLYIVMGFC 84
Cdd:cd14221   1 LGKGCFGQAIKVTHRETGEVMVMKEL-IRFDEETQRTFL-KEVKVMRCLEHPNVlkfigVLYKDK------RLNFITEYI 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  85 EGGDLYHRLKQQKGELlPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMAS-- 162
Cdd:cd14221  73 KGGTLRGIIKSMDSHY-PWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLARLMVDEKTQPEgl 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 41055987 163 ------------TLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEM 197
Cdd:cd14221 152 rslkkpdrkkryTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEI 198
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
10-257 6.13e-18

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: 85.07  E-value: 6.13e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQL-KHPNIVMYRESWeGEDCQLYIVMGFCEGGD 88
Cdd:cd14138  13 IGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLgQHSHVVRYYSAW-AEDDHMLIQNEYCNGGS 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  89 LYHRLKQ--QKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTN-------------------IIKVGD 147
Cdd:cd14138  92 LADAISEnyRIMSYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFISRTSipnaaseegdedewasnkvIFKIGD 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 148 LG-IARVLENQNDMastliGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMnslVYRIVEGKLPQMP 225
Cdd:cd14138 172 LGhVTRVSSPQVEE-----GDSRFLANEvLQENYTHLPKADIFALALTVVCAAGAEPLPTNGDQ---WHEIRQGKLPRIP 243
                       250       260       270
                ....*....|....*....|....*....|..
gi 41055987 226 SKYDPQLGELIKRMLCKKPEDRPDVKHILRQP 257
Cdd:cd14138 244 QVLSQEFLDLLKVMIHPDPERRPSAVALVKHS 275
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
6-271 6.94e-18

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: 85.05  E-value: 6.94e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   6 FVRVVGKGSYGEV--NLVRHKSDRKQYVIKKLNlRTSSRRERRAAEQEAQLLSQL-KHPNIVMYRESWEGEDcQLYIVMG 82
Cdd:cd05089   6 FEDVIGEGNFGQVikAMIKKDGLKMNAAIKMLK-EFASENDHRDFAGELEVLCKLgHHPNIINLLGACENRG-YLYIAIE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FCEGGDLYHRLKQQK--------------GELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDL 148
Cdd:cd05089  84 YAPYGNLLDFLRKSRvletdpafakehgtASTLTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVSKIADF 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 149 GIARVLENQndMASTLIGTPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLVYRIVEGKLPQMPS 226
Cdd:cd05089 164 GLSRGEEVY--VKKTMGRLPVrWMAIESLNYSVYTTKSDVWSFGVLLWEIVSLGGTpYCGMTCAELYEKLPQGYRMEKPR 241
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 41055987 227 KYDPQLGELIKRMLCKKPEDRPDVKHilrqpyIKHQISMFLEATK 271
Cdd:cd05089 242 NCDDEVYELMRQCWRDRPYERPPFSQ------ISVQLSRMLEARK 280
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
10-207 7.92e-18

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: 85.50  E-value: 7.92e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHK--SDRKQYVIKKLNLRTSSRrerrAAEQEAQLLSQLKHPNIVMYRESW-EGEDCQLYIVMGFCEG 86
Cdd:cd07867  10 VGRGTYGHVYKAKRKdgKDEKEYALKQIEGTGISM----SACREIALLRELKHPNVIALQKVFlSHSDRKVWLLFDYAEH 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  87 gDLYHRLK-------QQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLT----KTNIIKVGDLGIARV-- 153
Cdd:cd07867  86 -DLWHIIKfhraskaNKKPMQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMgegpERGRVKIADMGFARLfn 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41055987 154 --LENQNDMASTLIgTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAFNAK 207
Cdd:cd07867 165 spLKPLADLDPVVV-TFWYRAPElLLGARHYTKAIDIWAIGCIFAELLTSEPIFHCR 220
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
4-204 1.09e-17

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: 84.24  E-value: 1.09e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLK---HPNIVMYRE----SWEGEDCQ 76
Cdd:cd07863   2 YEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVQTNEDGLPLSTVREVALLKRLEafdHPNIVRLMDvcatSRTDRETK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  77 LYIVMGFCEGgDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLEN 156
Cdd:cd07863  82 VTLVFEHVDQ-DLRTYLDKVPPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLARIYSC 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 41055987 157 QndMAST-LIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAF 204
Cdd:cd07863 161 Q--MALTpVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLF 207
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
9-259 1.33e-17

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


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 84.31  E-value: 1.33e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   9 VVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERraAEQEAQLLSQLK-HPNIVMYRESWEGEDcQLYIVM-GFCEG 86
Cdd:cd14173   9 VLGEGAYARVQTCINLITNKEYAVKIIEKRPGHSRSR--VFREVEMLYQCQgHRNVLELIEFFEEED-KFYLVFeKMRGG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  87 GDLYHRLKQQKGELLPERQVVEwfvQIAMALQYLHEKHILHRDLKTQNIFLTKTNII---KVGDLGIARVLENQNDMAS- 162
Cdd:cd14173  86 SILSHIHRRRHFNELEASVVVQ---DIASALDFLHNKGIAHRDLKPENILCEHPNQVspvKICDFDLGSGIKLNSDCSPi 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 163 ------TLIGTPYYMSPEL---FSNKP--YNYKSDVWALGCCVYEMATLKHAFNAK---------------DMNSLVYRI 216
Cdd:cd14173 163 stpellTPCGSAEYMAPEVveaFNEEAsiYDKRCDLWSLGVILYIMLSGYPPFVGRcgsdcgwdrgeacpaCQNMLFESI 242
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 41055987 217 VEGKLpQMPSK----YDPQLGELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd14173 243 QEGKY-EFPEKdwahISCAAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
1-204 1.37e-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: 84.28  E-value: 1.37e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   1 MDGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRtssrRERRA---AEQEAQLLSQLKHPNIVMYRESWEGEDcQL 77
Cdd:cd07873   1 LETYIKLDKLGEGTYATVYKGRSKLTDNLVALKEIRLE----HEEGApctAIREVSLLKDLKHANIVTLHDIIHTEK-SL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  78 YIVMGFCEGgDLYHRLkQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQ 157
Cdd:cd07873  76 TLVFEYLDK-DLKQYL-DDCGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSIP 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 41055987 158 NDMASTLIGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAF 204
Cdd:cd07873 154 TKTYSNEVVTLWYRPPDiLLGSTDYSTQIDMWGVGCIFYEMSTGRPLF 201
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
9-248 1.98e-17

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: 83.28  E-value: 1.98e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   9 VVGKGSYGEVNLVRHK----SDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIV-MYRESWEGEdcQLYIVMGF 83
Cdd:cd05046  12 TLGRGEFGEVFLAKAKgieeEGGETLVLVKALQKTKDENLQSEFRRELDMFRKLSHKNVVrLLGLCREAE--PHYMILEY 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGGDLYHRLKQQKGELLPER-------QVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLEN 156
Cdd:cd05046  90 TDLGDLKQFLRATKSKDEKLKppplstkQKVALCTQIALGMDHLSNARFVHRDLAARNCLVSSQREVKVSLLSLSKDVYN 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 157 QN--DMASTLIgtPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATL-KHAFNAKDMNSLVYRIVEGKLP-QMPSKYDPQ 231
Cdd:cd05046 170 SEyyKLRNALI--PLrWLAPEAVQEDDFSTKSDVWSFGVLMWEVFTQgELPFYGLSDEEVLNRLQAGKLElPVPEGCPSR 247
                       250
                ....*....|....*..
gi 41055987 232 LGELIKRMLCKKPEDRP 248
Cdd:cd05046 248 LYKLMTRCWAVNPKDRP 264
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
5-253 2.09e-17

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


Pssm-ID: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 83.55  E-value: 2.09e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   5 LFVRVVGKGSYGEVNLVRHKS---DRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIV-MYRESWEGEdcQLYIV 80
Cdd:cd05093   8 VLKRELGEGAFGKVFLAECYNlcpEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVkFYGVCVEGD--PLIMV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MGFCEGGDLYHRLK------------QQKGELlPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDL 148
Cdd:cd05093  86 FEYMKHGDLNKFLRahgpdavlmaegNRPAEL-TQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDF 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 149 GIARVLENQN--DMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATL-KHAFNAKDMNSLVYRIVEGKLPQMP 225
Cdd:cd05093 165 GMSRDVYSTDyyRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYgKQPWYQLSNNEVIECITQGRVLQRP 244
                       250       260
                ....*....|....*....|....*...
gi 41055987 226 SKYDPQLGELIKRMLCKKPEDRPDVKHI 253
Cdd:cd05093 245 RTCPKEVYDLMLGCWQREPHMRLNIKEI 272
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
10-247 2.32e-17

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: 82.94  E-value: 2.32e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRtssrrerRAAEQEAQLLSQLKHPNIV-MYRESWEGEdcQLYIVMGFCEGGD 88
Cdd:cd13991  14 IGRGSFGEVHRMEDKQTGFQCAVKKVRLE-------VFRAEELMACAGLTSPRVVpLYGAVREGP--WVNIFMDLKEGGS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  89 LYHRLKQQKgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKT-NIIKVGDLGIARVLENQNDMASTLI-- 165
Cdd:cd13991  85 LGQLIKEQG--CLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDgSDAFLCDFGHAECLDPDGLGKSLFTgd 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 166 ---GTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLP--QMPSKYDPQLGELIKRML 240
Cdd:cd13991 163 yipGTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPWTQYYSGPLCLKIANEPPPlrEIPPSCAPLTAQAIQAGL 242

                ....*..
gi 41055987 241 CKKPEDR 247
Cdd:cd13991 243 RKEPVHR 249
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
9-260 2.46e-17

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: 83.54  E-value: 2.46e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   9 VVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERraAEQEAQLLSQLK-HPNIVMYRESWEgEDCQLYIVMGFCEGG 87
Cdd:cd14174   9 LLGEGAYAKVQGCVSLQNGKEYAVKIIEKNAGHSRSR--VFREVETLYQCQgNKNILELIEFFE-DDTRFYLVFEKLRGG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  88 DLYHRLKQQKgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNI---FLTKTNIIKVGDLGIARVLENQNdmASTL 164
Cdd:cd14174  86 SILAHIQKRK--HFNEREASRVVRDIASALDFLHTKGIAHRDLKPENIlceSPDKVSPVKICDFDLGSGVKLNS--ACTP 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 165 IGTP---------YYMSP---ELFSNKP--YNYKSDVWALGCCVYEMATLKHAFNAK---------------DMNSLVYR 215
Cdd:cd14174 162 ITTPelttpcgsaEYMAPevvEVFTDEAtfYDKRCDLWSLGVILYIMLSGYPPFVGHcgtdcgwdrgevcrvCQNKLFES 241
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 41055987 216 IVEGKLpQMPSKYDPQLG----ELIKRMLCKKPEDRPDVKHILRQPYIK 260
Cdd:cd14174 242 IQEGKY-EFPDKDWSHISseakDLISKLLVRDAKERLSAAQVLQHPWVQ 289
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
1-247 2.59e-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: 84.34  E-value: 2.59e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   1 MDGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNL-RTSSRRERRAAEQEAQLLSQLKH---PNIVMYRESWEGEDcQ 76
Cdd:cd05633   4 MNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKkRIKMKQGETLALNERIMLSLVSTgdcPFIVCMTYAFHTPD-K 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  77 LYIVMGFCEGGDLYHRLKQQKgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLEN 156
Cdd:cd05633  83 LCFILDLMNGGDLHYHLSQHG--VFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACDFSK 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 157 QNDMAStlIGTPYYMSPELFSN-KPYNYKSDVWALGCCVYEMATLKHAF---NAKDMNSlVYRIVEGKLPQMPSKYDPQL 232
Cdd:cd05633 161 KKPHAS--VGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFrqhKTKDKHE-IDRMTLTVNVELPDSFSPEL 237
                       250
                ....*....|....*
gi 41055987 233 GELIKRMLCKKPEDR 247
Cdd:cd05633 238 KSLLEGLLQRDVSKR 252
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
8-240 2.66e-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: 83.94  E-value: 2.66e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKQYVIKKLNL-RTSSRRERRAAEQEAQLLSQLKH---PNIVMYRESWEGEDcQLYIVMGF 83
Cdd:cd14223   6 RIIGRGGFGEVYGCRKADTGKMYAMKCLDKkRIKMKQGETLALNERIMLSLVSTgdcPFIVCMSYAFHTPD-KLSFILDL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGGDLYHRLKQQKgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASt 163
Cdd:cd14223  85 MNGGDLHYHLSQHG--VFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLACDFSKKKPHAS- 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 164 lIGTPYYMSPELFSNK-PYNYKSDVWALGCCVYEMATLKHAF---NAKDMNSlVYRIVEGKLPQMPSKYDPQLGELIKRM 239
Cdd:cd14223 162 -VGTHGYMAPEVLQKGvAYDSSADWFSLGCMLFKLLRGHSPFrqhKTKDKHE-IDRMTLTMAVELPDSFSPELRSLLEGL 239

                .
gi 41055987 240 L 240
Cdd:cd14223 240 L 240
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
7-254 2.88e-17

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: 82.82  E-value: 2.88e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   7 VRVVGKGSYGEV--NLVRHKSDRK---QYVIKKLNlRTSSRRERRAAEQEAQLLSQLKHPNIVmyreSWEGEDCQL---Y 78
Cdd:cd05036  11 IRALGQGAFGEVyeGTVSGMPGDPsplQVAVKTLP-ELCSEQDEMDFLMEALIMSKFNHPNIV----RCIGVCFQRlprF 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  79 IVMGFCEGGDL-----YHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKT---NIIKVGDLGI 150
Cdd:cd05036  86 ILLELMAGGDLksflrENRPRPEQPSSLTMLDLLQLAQDVAKGCRYLEENHFIHRDIAARNCLLTCKgpgRVAKIGDFGM 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 151 ARVLENQNdmastligtpYY------------MSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVE 218
Cdd:cd05036 166 ARDIYRAD----------YYrkggkamlpvkwMPPEAFLDGIFTSKTDVWSFGVLLWEIFSLGYMPYPGKSNQEVMEFVT 235
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 41055987 219 GKLPQMPSKYDPqlGELIKRML-C--KKPEDRPDVKHIL 254
Cdd:cd05036 236 SGGRMDPPKNCP--GPVYRIMTqCwqHIPEDRPNFSTIL 272
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
8-199 2.89e-17

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: 82.71  E-value: 2.89e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEV-NLVRHKSDRKQYVIKKLNLRTS-SRRERRAAEQEAQLLSQLKHPNIVMYrESWEGEDCQLYIVMGFCE 85
Cdd:cd05063  11 KVIGAGEFGEVfRGILKMPGRKEVAVAIKTLKPGyTEKQRQDFLSEASIMGQFSHHNIIRL-EGVVTKFKPAMIITEYME 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  86 GGDLYHRLKQQKGELLPeRQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTLI 165
Cdd:cd05063  90 NGALDKYLRDHDGEFSS-YQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRVLEDDPEGTYTTS 168
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 41055987 166 GTPY---YMSPELFSNKPYNYKSDVWALGCCVYEMAT 199
Cdd:cd05063 169 GGKIpirWTAPEAIAYRKFTSASDVWSFGIVMWEVMS 205
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
10-257 3.09e-17

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: 82.54  E-value: 3.09e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRhKSDRKQYVIKKLNlRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDCQL--YIVMGFCEGG 87
Cdd:cd14664   1 IGRGGAGTVYKGV-MPNGTLVAVKRLK-GEGTQGGDHGFQAEIQTLGMIRHRNIVRLRGYCSNPTTNLlvYEYMPNGSLG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  88 DLYHRLKQQKGEL-LPERQVVEwfVQIAMALQYLHEK---HILHRDLKTQNIFLTKTNIIKVGDLGIARVLE-NQNDMAS 162
Cdd:cd14664  79 ELLHSRPESQPPLdWETRQRIA--LGSARGLAYLHHDcspLIIHRDVKSNNILLDEEFEAHVADFGLAKLMDdKDSHVMS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 163 TLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNA---KDMNSLVyRIVEGKLPQ--MPSKYDPQLGELIK 237
Cdd:cd14664 157 SVAGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRPFDEaflDDGVDIV-DWVRGLLEEkkVEALVDPDLQGVYK 235
                       250       260       270
                ....*....|....*....|....*....|....*
gi 41055987 238 R----------MLC--KKPEDRP---DVKHILRQP 257
Cdd:cd14664 236 LeeveqvfqvaLLCtqSSPMERPtmrEVVRMLEGD 270
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
10-204 3.46e-17

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 83.66  E-value: 3.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   10 VGKGSYGEVNLVRHKSDRKQYVIKKL------NLRTSSRRE------RRAAEQEAQLLSQLKHPNIVMYRESWEGEDCqL 77
Cdd:PTZ00024  17 LGEGTYGKVEKAYDTLTGKIVAIKKVkiieisNDVTKDRQLvgmcgiHFTTLRELKIMNEIKHENIMGLVDVYVEGDF-I 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   78 YIVMGFCEGgDLyHRLKQQKgELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIAR----- 152
Cdd:PTZ00024  96 NLVMDIMAS-DL-KKVVDRK-IRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLARrygyp 172
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41055987  153 ----VLENQNDMASTLIGTP-----YYMSPELF--SNKpYNYKSDVWALGCCVYEMATLKHAF 204
Cdd:PTZ00024 173 pysdTLSKDETMQRREEMTSkvvtlWYRAPELLmgAEK-YHFAVDMWSVGCIFAELLTGKPLF 234
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
7-199 3.69e-17

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: 82.70  E-value: 3.69e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   7 VRVVGKGSYGEVN----LVRHKSDRKQYVIKKLNLRtSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDCQLyiVMG 82
Cdd:cd05111  12 LKVLGSGVFGTVHkgiwIPEGDSIKIPVAIKVIQDR-SGRQSFQAVTDHMLAIGSLDHAYIVRLLGICPGASLQL--VTQ 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FCEGGDLYHRLKQQKGELLPERqVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVL-ENQNDMA 161
Cdd:cd05111  89 LLPLGSLLDHVRQHRGSLGPQL-LLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLKSPSQVQVADFGVADLLyPDDKKYF 167
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 41055987 162 STLIGTPY-YMSPELFSNKPYNYKSDVWALGCCVYEMAT 199
Cdd:cd05111 168 YSEAKTPIkWMALESIHFGKYTHQSDVWSYGVTVWEMMT 206
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
8-249 4.09e-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: 82.68  E-value: 4.09e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEV---NLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIV----MYRESWEGEDCQLYIV 80
Cdd:cd14204  13 KVLGEGEFGSVmegELQQPDGTNHKVAVKTMKLDNFSQREIEEFLSEAACMKDFNHPNVIrllgVCLEVGSQRIPKPMVI 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MGFCEGGDLYHRLKQQKGEL----LPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLEN 156
Cdd:cd14204  93 LPFMKYGDLHSFLLRSRLGSgpqhVPLQTLLKFMIDIALGMEYLSSRNFLHRDLAARNCMLRDDMTVCVADFGLSKKIYS 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 157 -----QNDMASTLIGtpyYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYR-IVEGKLPQMPSKYDP 230
Cdd:cd14204 173 gdyyrQGRIAKMPVK---WIAVESLADRVYTVKSDVWAFGVTMWEIATRGMTPYPGVQNHEIYDyLLHGHRLKQPEDCLD 249
                       250
                ....*....|....*....
gi 41055987 231 QLGELIKRMLCKKPEDRPD 249
Cdd:cd14204 250 ELYDIMYSCWRSDPTDRPT 268
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
13-253 4.27e-17

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: 82.16  E-value: 4.27e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  13 GSYGEVNLVRHKSdrKQYVIKKLNLRTSSRRERRAAE-QEAQLLSQLKHPNIVMYResweG---EDCQLYIVMGFCEGGD 88
Cdd:cd14027   4 GGFGKVSLCFHRT--QGLVVLKTVYTGPNCIEHNEALlEEGKMMNRLRHSRVVKLL----GvilEEGKYSLVMEYMEKGN 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  89 LYHRLKQQKGELLPERQVVewfVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIA-------------RVLE 155
Cdd:cd14027  78 LMHVLKKVSVPLSVKGRII---LEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwskltkeehNEQR 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 156 NQNDMASTLIGTPYYMSPELFSN---KPYNyKSDVWALGCCVYEMATLKHAF-NAKDMNSLVYRIVEGKLP---QMPSKY 228
Cdd:cd14027 155 EVDGTAKKNAGTLYYMAPEHLNDvnaKPTE-KSDVYSFAIVLWAIFANKEPYeNAINEDQIIMCIKSGNRPdvdDITEYC 233
                       250       260
                ....*....|....*....|....*
gi 41055987 229 DPQLGELIKRMLCKKPEDRPDVKHI 253
Cdd:cd14027 234 PREIIDLMKLCWEANPEARPTFPGI 258
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
2-253 4.44e-17

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: 82.42  E-value: 4.44e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLFVRVVGKGSYGEVNLVRHKSDRKqYVIKKLNLRTSSRRerrAAEQEAQLLSQLKHPNIVMYRESWEGEdcQLYIVM 81
Cdd:cd05070   9 ESLQLIKRLGNGQFGEVWMGTWNGNTK-VAIKTLKPGTMSPE---SFLEEAQIMKKLKHDKLVQLYAVVSEE--PIYIVT 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  82 GFCEGGDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMA 161
Cdd:cd05070  83 EYMSKGSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEYTA 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 162 STLIGTPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATlKHAFNAKDMNS--LVYRIVEGKLPQMPSKYDPQLGELIKR 238
Cdd:cd05070 163 RQGAKFPIkWTAPEAALYGRFTIKSDVWSFGILLTELVT-KGRVPYPGMNNreVLEQVERGYRMPCPQDCPISLHELMIH 241
                       250
                ....*....|....*
gi 41055987 239 MLCKKPEDRPDVKHI 253
Cdd:cd05070 242 CWKKDPEERPTFEYL 256
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
1-217 6.21e-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: 6.21e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   1 MDGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRtssrRERRA---AEQEAQLLSQLKHPNIVMYRESWEgEDCQL 77
Cdd:cd07872   5 METYIKLEKLGEGTYATVFKGRSKLTENLVALKEIRLE----HEEGApctAIREVSLLKDLKHANIVTLHDIVH-TDKSL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  78 YIVMGFceggdLYHRLKQQK---GELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVL 154
Cdd:cd07872  80 TLVFEY-----LDKDLKQYMddcGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAK 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41055987 155 ENQNDMASTLIGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAF---NAKDMNSLVYRIV 217
Cdd:cd07872 155 SVPTKTYSNEVVTLWYRPPDvLLGSSEYSTQIDMWGVGCIFFEMASGRPLFpgsTVEDELHLIFRLL 221
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
8-256 6.25e-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: 81.89  E-value: 6.25e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKQYV---IKKLNLRTSSRRERRAAEQEAQLLSQLKHPNI-----VMYRESWEGEDCQLYI 79
Cdd:cd05074  15 RMLGKGEFGSVREAQLKSEDGSFQkvaVKMLKADIFSSSDIEEFLREAACMKEFDHPNVikligVSLRSRAKGRLPIPMV 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  80 VMGFCEGGDLYHRLKQQK-GE---LLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLE 155
Cdd:cd05074  95 ILPFMKHGDLHTFLLMSRiGEepfTLPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCMLNENMTVCVADFGLSKKIY 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 156 N----QNDMASTLigtPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYR-IVEGKLPQMPSKYD 229
Cdd:cd05074 175 SgdyyRQGCASKL---PVkWLALESLADNVYTTHSDVWAFGVTMWEIMTRGQTPYAGVENSEIYNyLIKGNRLKQPPDCL 251
                       250       260
                ....*....|....*....|....*..
gi 41055987 230 PQLGELIKRMLCKKPEDRPDVKHILRQ 256
Cdd:cd05074 252 EDVYELMCQCWSPEPKCRPSFQHLRDQ 278
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
4-258 6.76e-17

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: 82.04  E-value: 6.76e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRtssrRERRA---AEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIV 80
Cdd:cd07844   2 YKKLDKLGEGSYATVYKGRSKLTGQLVALKEIRLE----HEEGApftAIREASLLKDLKHANIVTLHDIIHTKK-TLTLV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MGFCEGgDLYHRLKQQKGELLPeRQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDM 160
Cdd:cd07844  77 FEYLDT-DLKQYMDDCGGGLSM-HNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLARAKSVPSKT 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 161 ASTLIGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAF----NAKDMNSLVYRIV----EGKLPQMPSKYD-- 229
Cdd:cd07844 155 YSNEVVTLWYRPPDvLLGSTEYSTSLDMWGVGCIFYEMATGRPLFpgstDVEDQLHKIFRVLgtptEETWPGVSSNPEfk 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 41055987 230 ----------------PQLG------ELIKRMLCKKPEDRPDVKHILRQPY 258
Cdd:cd07844 235 pysfpfypprplinhaPRLDriphgeELALKFLQYEPKKRISAAEAMKHPY 285
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
4-257 9.44e-17

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: 81.51  E-value: 9.44e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKlnlrtsSRRERRAAEQEAQLLSQL-------KHPNIVMYRESWeGEDCQ 76
Cdd:cd14139   2 FLELEKIGVGEFGSVYKCIKRLDGCVYAIKR------SMRPFAGSSNEQLALHEVyahavlgHHPHVVRYYSAW-AEDDH 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  77 LYIVMGFCEGGDLYHRL--KQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTN------------- 141
Cdd:cd14139  75 MIIQNEYCNGGSLQDAIseNTKSGNHFEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIFICHKMqsssgvgeevsne 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 142 ---------IIKVGDLGIARVLENqndmASTLIGTPYYMSPELFSNKpYNY--KSDVWALGCCVyemATLKHAFNAKDMN 210
Cdd:cd14139 155 edeflsanvVYKIGDLGHVTSINK----PQVEEGDSRFLANEILQED-YRHlpKADIFALGLTV---ALAAGAEPLPTNG 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 41055987 211 SLVYRIVEGKLPQMPSKYDPQLGELIKRMLCKKPEDRPDVKHILRQP 257
Cdd:cd14139 227 AAWHHIRKGNFPDVPQELPESFSSLLKNMIQPDPEQRPSATALARHT 273
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
10-197 9.78e-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: 80.77  E-value: 9.78e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLnlrTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEdCQLYIVMGFCEGGDL 89
Cdd:cd14115   1 IGRGRFSIVKKCLHKATRKDVAVKFV---SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESP-TSYILVLELMDDGRL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  90 YHRLKQQKgELLPERqvVEWFVQIAM-ALQYLHEKHILHRDLKTQNIF--LTK-TNIIKVGDLGIARVLENQNDMaSTLI 165
Cdd:cd14115  77 LDYLMNHD-ELMEEK--VAFYIRDIMeALQYLHNCRVAHLDIKPENLLidLRIpVPRVKLIDLEDAVQISGHRHV-HHLL 152
                       170       180       190
                ....*....|....*....|....*....|..
gi 41055987 166 GTPYYMSPELFSNKPYNYKSDVWALGCCVYEM 197
Cdd:cd14115 153 GNPEFAAPEVIQGTPVSLATDIWSIGVLTYVM 184
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
5-247 1.22e-16

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: 82.75  E-value: 1.22e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   5 LFVRV--VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRA-AEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVM 81
Cdd:cd05626   2 MFVKIktLGIGAFGEVCLACKVDTHALYAMKTLRKKDVLNRNQVAhVKAERDILAEADNEWVVKLYYSFQDKD-NLYFVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  82 GFCEGGDLYHRLKQQkgELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIA---------- 151
Cdd:cd05626  81 DYIPGGDMMSLLIRM--EVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLCtgfrwthnsk 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 152 -------------------------------RVLE------NQNDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCV 194
Cdd:cd05626 159 yyqkgshirqdsmepsdlwddvsncrcgdrlKTLEqratkqHQRCLAHSLVGTPNYIAPEVLLRKGYTQLCDWWSVGVIL 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41055987 195 YEMATLKHAFNAKDMNSLVYRIV--EGKLpQMPS--KYDPQLGELIKRmLCKKPEDR 247
Cdd:cd05626 239 FEMLVGQPPFLAPTPTETQLKVInwENTL-HIPPqvKLSPEAVDLITK-LCCSAEER 293
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
4-258 1.32e-16

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: 80.36  E-value: 1.32e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQ----YVIKKLNLRTSSRRERRAAEQEAQLL---SQLKHPNIVMYRESWEGEDCQ 76
Cdd:cd14005   2 YEVGDLLGKGGFGTVYSGVRIRDGLPvavkFVPKSRVTEWAMINGPVPVPLEIALLlkaSKPGVPGVIRLLDWYERPDGF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  77 LyIVMGF---CEggDLYHRLKQqKGELlPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLT-KTNIIKVGDLGIAR 152
Cdd:cd14005  82 L-LIMERpepCQ--DLFDFITE-RGAL-SENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINlRTGEVKLIDFGCGA 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 153 VLENQndMASTLIGTPYYMSPELFSNKPYNYKS-DVWALGCCVYEMATLKHAFNAKDmnslvyRIVEGKlPQMPSKYDPQ 231
Cdd:cd14005 157 LLKDS--VYTDFDGTRVYSPPEWIRHGRYHGRPaTVWSLGILLYDMLCGDIPFENDE------QILRGN-VLFRPRLSKE 227
                       250       260
                ....*....|....*....|....*..
gi 41055987 232 LGELIKRMLCKKPEDRPDVKHILRQPY 258
Cdd:cd14005 228 CCDLISRCLQFDPSKRPSLEQILSHPW 254
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
9-261 1.33e-16

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 1 subunit (PhKG1) is also referred to as the muscle gamma isoform. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 81.11  E-value: 1.33e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   9 VVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRE-------RRAAEQEAQLLSQLK-HPNIVMYRESWEGEDCqLYIV 80
Cdd:cd14182  10 ILGRGVSSVVRRCIHKPTRQEYAVKIIDITGGGSFSpeevqelREATLKEIDILRKVSgHPNIIQLKDTYETNTF-FFLV 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MGFCEGGDLYHRLKQQKgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLEnQNDM 160
Cdd:cd14182  89 FDLMKKGELFDYLTEKV--TLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQLD-PGEK 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 161 ASTLIGTPYYMSPELFS-----NKP-YNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKL----PQMPSKYDp 230
Cdd:cd14182 166 LREVCGTPGYLAPEIIEcsmddNHPgYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGNYqfgsPEWDDRSD- 244
                       250       260       270
                ....*....|....*....|....*....|.
gi 41055987 231 QLGELIKRMLCKKPEDRPDVKHILRQPYIKH 261
Cdd:cd14182 245 TVKDLISRFLVVQPQKRYTAEEALAHPFFQQ 275
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
2-258 1.38e-16

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: 81.42  E-value: 1.38e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGED----CQL 77
Cdd:cd07837   1 DAYEKLEKIGEGTYGKVYKARDKNTGKLVALKKTRLEMEEEGVPSTALREVSLLQMLSQSIYIVRLLDVEHVEengkPLL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  78 YIVMGFCEGG-----DLYHRLKQQKgelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKT-NIIKVGDLGIA 151
Cdd:cd07837  81 YLVFEYLDTDlkkfiDSYGRGPHNP---LPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQkGLLKIADLGLG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 152 RVLENQNDMASTLIGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVE------------ 218
Cdd:cd07837 158 RAFTIPIKSYTHEIVTLWYRAPEvLLGSTHYSTPVDMWSVGCIFAEMSRKQPLFPGDSELQQLLHIFRllgtpneevwpg 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 41055987 219 -GKL----------PQMPSKYDPQLG----ELIKRMLCKKPEDRPDVKHILRQPY 258
Cdd:cd07837 238 vSKLrdwheypqwkPQDLSRAVPDLEpegvDLLTKMLAYDPAKRISAKAALQHPY 292
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
9-248 1.41e-16

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: 80.96  E-value: 1.41e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   9 VVGKGSYGEV---NLVRHKSDRKQYVIKKLNLRTSSRRERRAAeQEAQLLSQLKHPNIV-MYRESWEGEDCQ--LYIVMG 82
Cdd:cd05043  13 LLQEGTFGRIfhgILRDEKGKEEEVLVKTVKDHASEIQVTMLL-QESSLLYGLSHQNLLpILHVCIEDGEKPmvLYPYMN 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FcegGDLYHRLKQ------QKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVL-- 154
Cdd:cd05043  92 W---GNLKLFLQQcrlseaNNPQALSTQQLVHMALQIACGMSYLHRRGVIHKDIAARNCVIDDELQVKITDNALSRDLfp 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 155 -------ENQNdmastligTPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATL-KHAFNAKDMNSLVYRIVEGKLPQMP 225
Cdd:cd05043 169 mdyhclgDNEN--------RPIkWMSLESLVNKEYSSASDVWSFGVLLWELMTLgQTPYVEIDPFEMAAYLKDGYRLAQP 240
                       250       260
                ....*....|....*....|....*.
gi 41055987 226 SKYDPQLGELikrMLC---KKPEDRP 248
Cdd:cd05043 241 INCPDELFAV---MACcwaLDPEERP 263
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
8-248 1.44e-16

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: 80.82  E-value: 1.44e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEV--NLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIV-MYRESWEGEDCQLY----IV 80
Cdd:cd05075   6 KTLGEGEFGSVmeGQLNQDDSVLKVAVKTMKIAICTRSEMEDFLSEAVCMKEFDHPNVMrLIGVCLQNTESEGYpspvVI 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MGFCEGGDL-----YHRLKQQKgELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLE 155
Cdd:cd05075  86 LPFMKHGDLhsfllYSRLGDCP-VYLPTQMLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADFGLSKKIY 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 156 N-----QNDMASTLIGtpyYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVE--GKLPQMPSKY 228
Cdd:cd05075 165 NgdyyrQGRISKMPVK---WIAIESLADRVYTTKSDVWSFGVTMWEIATRGQTPYPGVENSEIYDYLRqgNRLKQPPDCL 241
                       250       260
                ....*....|....*....|
gi 41055987 229 DpQLGELIKRMLCKKPEDRP 248
Cdd:cd05075 242 D-GLYELMSSCWLLNPKDRP 260
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
8-259 1.54e-16

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: 82.48  E-value: 1.54e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKQYVIKKL-----NLrTSSRRERRaaeqEAQLLSQLKH------------PNIVMYREsw 70
Cdd:cd07853   6 RPIGYGAFGVVWSVTDPRDGKRVALKKMpnvfqNL-VSCKRVFR----ELKMLCFFKHdnvlsaldilqpPHIDPFEE-- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  71 egedcqLYIVMGFCEGgDLyHRLKQQKGELLPERqvVEWFV-QIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLG 149
Cdd:cd07853  79 ------IYVVTELMQS-DL-HKIIVSPQPLSSDH--VKVFLyQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFG 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 150 IARVLE--NQNDMASTLIgTPYYMSPELFSNKP-YNYKSDVWALGCCVYEMATLKHAFNAK------------------- 207
Cdd:cd07853 149 LARVEEpdESKHMTQEVV-TQYYRAPEILMGSRhYTSAVDIWSVGCIFAELLGRRILFQAQspiqqldlitdllgtpsle 227
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41055987 208 DMNSL-------VYRIVEgKLPQMPSKY---DPQLGE---LIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd07853 228 AMRSAcegarahILRGPH-KPPSLPVLYtlsSQATHEavhLLCRMLVFDPDKRISAADALAHPYL 291
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
8-248 1.71e-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: 80.66  E-value: 1.71e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRKQYV---IKKLNLRTSSRRERRAAEQEAQLLSQLKHPNI-----VMYRESWEGEDCQLYI 79
Cdd:cd05035   5 KILGEGEFGSVMEAQLKQDDGSQLkvaVKTMKVDIHTYSEIEEFLSEAACMKDFDHPNVmrligVCFTASDLNKPPSPMV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  80 VMGFCEGGDL-----YHRLKQQKgELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVL 154
Cdd:cd05035  85 ILPFMKHGDLhsyllYSRLGGLP-EKLPLQTLLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVCVADFGLSRKI 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 155 ENQNDMASTLIGT-PY-YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEG--KLPQMPSKYDp 230
Cdd:cd05035 164 YSGDYYRQGRISKmPVkWIALESLADNVYTSKSDVWSFGVTMWEIATRGQTPYPGVENHEIYDYLRNgnRLKQPEDCLD- 242
                       250
                ....*....|....*...
gi 41055987 231 QLGELIKRMLCKKPEDRP 248
Cdd:cd05035 243 EVYFLMYFCWTVDPKDRP 260
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
1-197 1.85e-16

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: 82.03  E-value: 1.85e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   1 MDGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRA-AEQEAQLLSQLKHPNIVMYRESWEGEDcQLYI 79
Cdd:cd05627   1 LDDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQVAhIRAERDILVEADGAWVVKMFYSFQDKR-NLYL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  80 VMGFCEGGDLYHRLkqQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVL----- 154
Cdd:cd05627  80 IMEFLPGGDMMTLL--MKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLCTGLkkahr 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41055987 155 ------------------------------ENQNDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEM 197
Cdd:cd05627 158 tefyrnlthnppsdfsfqnmnskrkaetwkKNRRQLAYSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEM 230
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
6-254 2.22e-16

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: 79.92  E-value: 2.22e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   6 FVRVVGKGSYGevnLVRHKSDRKQYVIKKLNLRTSSRRERRAAEqEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCE 85
Cdd:cd05113   8 FLKELGTGQFG---VVKYGKWRGQYDVAIKMIKEGSMSEDEFIE-EAKVMMNLSHEKLVQLYGVCTKQR-PIFIITEYMA 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  86 GGDLYHRLKQQKGELLPErQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIAR-VLENQndmASTL 164
Cdd:cd05113  83 NGCLLNYLREMRKRFQTQ-QLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRyVLDDE---YTSS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 165 IGTPY---YMSPELFSNKPYNYKSDVWALGCCVYEMATL-KHAFNAKDMNSLVYRIVEGKLPQMPSKYDPQLGELIKRML 240
Cdd:cd05113 159 VGSKFpvrWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSLgKMPYERFTNSETVEHVSQGLRLYRPHLASEKVYTIMYSCW 238
                       250
                ....*....|....
gi 41055987 241 CKKPEDRPDVKHIL 254
Cdd:cd05113 239 HEKADERPTFKILL 252
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
2-258 2.32e-16

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: 81.07  E-value: 2.32e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLnlrtssRRE---RRAAEQEAQLLSQLKH------PNIVMYRES--W 70
Cdd:cd14134  12 NRYKILRLLGEGTFGKVLECWDRKRKRYVAVKII------RNVekyREAAKIEIDVLETLAEkdpngkSHCVQLRDWfdY 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  71 EGEDCqlyIVMGFCeGGDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLT------------ 138
Cdd:cd14134  86 RGHMC---IVFELL-GPSLYDFLKKNNYGPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLVdsdyvkvynpkk 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 139 -------KTNIIKVGDLGIArVLENQNDmaSTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMAT----------LK 201
Cdd:cd14134 162 krqirvpKSTDIKLIDFGSA-TFDDEYH--SSIVSTRHYRAPEVILGLGWSYPCDVWSIGCILVELYTgellfqthdnLE 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 202 H---------------AFNAKDMNSLVYR----------------IVEGKLPQMP-----SKYDPQLGELIKRMLCKKPE 245
Cdd:cd14134 239 HlammerilgplpkrmIRRAKKGAKYFYFyhgrldwpegsssgrsIKRVCKPLKRlmllvDPEHRLLFDLIRKMLEYDPS 318
                       330
                ....*....|...
gi 41055987 246 DRPDVKHILRQPY 258
Cdd:cd14134 319 KRITAKEALKHPF 331
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
10-253 2.93e-16

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Unlike other FGFRs, there is only one splice form of FGFR4. It binds FGF1, FGF2, FGF6, FGF19, and FGF23. FGF19 is a selective ligand for FGFR4. Although disruption of FGFR4 in mice causes no obvious phenotype, in vivo inhibition of FGFR4 in cultured skeletal muscle cells resulted in an arrest of muscle progenitor differentiation. FGF6 and FGFR4 are uniquely expressed in myofibers and satellite cells. FGF6/FGFR4 signaling appears to play a key role in the regulation of muscle regeneration. A polymorphism in FGFR4 is found in head and neck squamous cell carcinoma. FGFR4 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 80.78  E-value: 2.93e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEV------NLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQL-KHPNIVmyreSWEG---EDCQLYI 79
Cdd:cd05099  20 LGEGCFGQVvraeayGIDKSRPDQTVTVAVKMLKDNATDKDLADLISEMELMKLIgKHKNII----NLLGvctQEGPLYV 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  80 VMGFCEGGDLYHRLKQQK---------GELLPERQV-----VEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKV 145
Cdd:cd05099  96 IVEYAAKGNLREFLRARRppgpdytfdITKVPEEQLsfkdlVSCAYQVARGMEYLESRRCIHRDLAARNVLVTEDNVMKI 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 146 GDLGIARVLENQNDMASTLIG-TPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLVYRIVEGKLP 222
Cdd:cd05099 176 ADFGLARGVHDIDYYKKTSNGrLPVkWMAPEALFDRVYTHQSDVWSFGILMWEIFTLGGSpYPGIPVEELFKLLREGHRM 255
                       250       260       270
                ....*....|....*....|....*....|.
gi 41055987 223 QMPSKYDPQLGELIKRMLCKKPEDRPDVKHI 253
Cdd:cd05099 256 DKPSNCTHELYMLMRECWHAVPTQRPTFKQL 286
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
10-207 4.71e-16

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: 80.49  E-value: 4.71e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHK--SDRKQYVIKKLNLRTSSRrerrAAEQEAQLLSQLKHPNIVMYRESW-EGEDCQLYIVMGFCEG 86
Cdd:cd07868  25 VGRGTYGHVYKAKRKdgKDDKDYALKQIEGTGISM----SACREIALLRELKHPNVISLQKVFlSHADRKVWLLFDYAEH 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  87 gDLYHRLK-------QQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLT----KTNIIKVGDLGIARV-- 153
Cdd:cd07868 101 -DLWHIIKfhraskaNKKPVQLPRGMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMgegpERGRVKIADMGFARLfn 179
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41055987 154 --LENQNDMASTLIgTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLKHAFNAK 207
Cdd:cd07868 180 spLKPLADLDPVVV-TFWYRAPElLLGARHYTKAIDIWAIGCIFAELLTSEPIFHCR 235
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
10-253 4.74e-16

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkA is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkA to its ligand, nerve growth factor (NGF), results in receptor oligomerization and activation of the catalytic domain. TrkA is expressed mainly in neural-crest-derived sensory and sympathetic neurons of the peripheral nervous system, and in basal forebrain cholinergic neurons of the central nervous system. It is critical for neuronal growth, differentiation and survival. Alternative TrkA splicing has been implicated as a pivotal regulator of neuroblastoma (NB) behavior. Normal TrkA expression is associated with better NB prognosis, while the hypoxia-regulated TrkAIII splice variant promotes NB pathogenesis and progression. Aberrant TrkA expression has also been demonstrated in non-neural tumors including prostate, breast, lung, and pancreatic cancers. The TrkA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 79.24  E-value: 4.74e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVR-----HKSDRKQYVIKKLnlRTSSRRERRAAEQEAQLLSQLKHPNIV-MYRESWEGEdcQLYIVMGF 83
Cdd:cd05092  13 LGEGAFGKVFLAEchnllPEQDKMLVAVKAL--KEATESARQDFQREAELLTVLQHQHIVrFYGVCTEGE--PLIMVFEY 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGGDL----------YHRLKQQKGELLPE---RQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGI 150
Cdd:cd05092  89 MRHGDLnrflrshgpdAKILDGGEGQAPGQltlGQMLQIASQIASGMVYLASLHFVHRDLATRNCLVGQGLVVKIGDFGM 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 151 ARvlenqnDMAStligTPYY------------MSPELFSNKPYNYKSDVWALGCCVYEMATL-KHAFNAKDMNSLVYRIV 217
Cdd:cd05092 169 SR------DIYS----TDYYrvggrtmlpirwMPPESILYRKFTTESDIWSFGVVLWEIFTYgKQPWYQLSNTEAIECIT 238
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 41055987 218 EGKLPQMPSKYDPQLGELIKRMLCKKPEDRPDVKHI 253
Cdd:cd05092 239 QGRELERPRTCPPEVYAIMQGCWQREPQQRHSIKDI 274
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
9-199 6.62e-16

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


Pssm-ID: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 79.34  E-value: 6.62e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   9 VVGKGSYGEV---NLVRHKSDRKQYVIKKLnlrtSSRRERRAAEQEAQLLSQ--LKHPNIVMY---RESWEGEDCQLYIV 80
Cdd:cd14055   2 LVGKGRFAEVwkaKLKQNASGQYETVAVKI----FPYEEYASWKNEKDIFTDasLKHENILQFltaEERGVGLDRQYWLI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MGFCEGGDLYHRLKqqkgellpeRQVVEWFVQIAMA------LQYLHEKH---------ILHRDLKTQNIFLTKTNIIKV 145
Cdd:cd14055  78 TAYHENGSLQDYLT---------RHILSWEDLCKMAgslargLAHLHSDRtpcgrpkipIAHRDLKSSNILVKNDGTCVL 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41055987 146 GDLGIARVLENQ---NDMA-STLIGTPYYMSPELFSNKP--YNYKS----DVWALGCCVYEMAT 199
Cdd:cd14055 149 ADFGLALRLDPSlsvDELAnSGQVGTARYMAPEALESRVnlEDLESfkqiDVYSMALVLWEMAS 212
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
12-253 7.12e-16

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


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 78.59  E-value: 7.12e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  12 KGSYGEVNLVRHKSDRKQYV-------IKKLNLrtsSRRERRAAEQEAQLLSQLKHPNIVMYResweG---EDCQLYIVM 81
Cdd:cd13992   3 CGSGASSHTGEPKYVKKVGVyggrtvaIKHITF---SRTEKRTILQELNQLKELVHDNLNKFI----GiciNPPNIAVVT 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  82 GFCEGGDLYHRLKQQKGELlperqvvEWFVQIAMA------LQYLHEKHI-LHRDLKTQNIFLTKTNIIKVGDLGIARVL 154
Cdd:cd13992  76 EYCTRGSLQDVLLNREIKM-------DWMFKSSFIkdivkgMNYLHSSSIgYHGRLKSSNCLVDSRWVVKLTDFGLRNLL 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 155 ENQNDMASTLIGTPY---YMSPELFSNKPYNY----KSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEG----KLPQ 223
Cdd:cd13992 149 EEQTNHQLDEDAQHKkllWTAPELLRGSLLEVrgtqKGDVYSFAIILYEILFRSDPFALEREVAIVEKVISGgnkpFRPE 228
                       250       260       270
                ....*....|....*....|....*....|...
gi 41055987 224 M---PSKYDPQLGELIKRMLCKKPEDRPDVKHI 253
Cdd:cd13992 229 LavlLDEFPPRLVLLVKQCWAENPEKRPSFKQI 261
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
10-254 7.23e-16

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: 79.29  E-value: 7.23e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVR----HKSDRKQYVIKKLNLRTSSRRERRAAE--QEAQLLSQL-KHPNIVMYRESWEgEDCQLYIVMG 82
Cdd:cd05101  32 LGEGCFGQVVMAEavgiDKDKPKEAVTVAVKMLKDDATEKDLSDlvSEMEMMKMIgKHKNIINLLGACT-QDGPLYVIVE 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FCEGGDLYHRLKQQK--------------GELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDL 148
Cdd:cd05101 111 YASKGNLREYLRARRppgmeysydinrvpEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMKIADF 190
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 149 GIARVLENQNDMASTLIGT-PY-YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLVYRIVEGKLPQMP 225
Cdd:cd05101 191 GLARDINNIDYYKKTTNGRlPVkWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSpYPGIPVEELFKLLKEGHRMDKP 270
                       250       260
                ....*....|....*....|....*....
gi 41055987 226 SKYDPQLGELIKRMLCKKPEDRPDVKHIL 254
Cdd:cd05101 271 ANCTNELYMMMRDCWHAVPSQRPTFKQLV 299
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
10-256 8.41e-16

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: 78.13  E-value: 8.41e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRtssrrERRAAEQEAQllSQLKHPNIV-MYRESWEGEDCQLYIVMGfcEGGD 88
Cdd:cd13995  12 IPRGAFGKVYLAQDTKTKKRMACKLIPVE-----QFKPSDVEIQ--ACFRHENIAeLYGALLWEETVHLFMEAG--EGGS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  89 LYHRLKQQKgellPERQV-VEWFVQ-IAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVgDLGIARVLENQNDMASTLIG 166
Cdd:cd13995  83 VLEKLESCG----PMREFeIIWVTKhVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAVLV-DFGLSVQMTEDVYVPKDLRG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 167 TPYYMSPELFSNKPYNYKSDVWALGCCVYEMAT----LKHAFNAKDMNSLVYrIVEGKLP---QMPSKYDPQLGELIKRM 239
Cdd:cd13995 158 TEIYMSPEVILCRGHNTKADIYSLGATIIHMQTgsppWVRRYPRSAYPSYLY-IIHKQAPpleDIAQDCSPAMRELLEAA 236
                       250
                ....*....|....*..
gi 41055987 240 LCKKPEDRPDVKHILRQ 256
Cdd:cd13995 237 LERNPNHRSSAAELLKH 253
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
87-258 9.15e-16

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: 77.77  E-value: 9.15e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  87 GDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLT--KTNIIKVGDLGIARVLENQNDMASTL 164
Cdd:cd14022  69 GDMHSFVRTCKK--LREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKdeERTRVKLESLEDAYILRGHDDSLSDK 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 165 IGTPYYMSPELF-SNKPYNYKS-DVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLpQMPSKYDPQLGELIKRMLCK 242
Cdd:cd14022 147 HGCPAYVSPEILnTSGSYSGKAaDVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQF-NIPETLSPKAKCLIRSILRR 225
                       170
                ....*....|....*.
gi 41055987 243 KPEDRPDVKHILRQPY 258
Cdd:cd14022 226 EPSERLTSQEILDHPW 241
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
7-197 9.23e-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: 80.08  E-value: 9.23e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   7 VRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRA-AEQEAQLLSQLKHPNIVMYRESWEgEDCQLYIVMGFCE 85
Cdd:cd05628   6 LKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQVGhIRAERDILVEADSLWVVKMFYSFQ-DKLNLYLIMEFLP 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  86 GGDLYHRLkqQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLE---------- 155
Cdd:cd05628  85 GGDMMTLL--MKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCTGLKkahrtefyrn 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41055987 156 -------------------------NQNDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEM 197
Cdd:cd05628 163 lnhslpsdftfqnmnskrkaetwkrNRRQLAFSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEM 229
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
101-255 1.01e-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: 78.60  E-value: 1.01e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 101 LPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTK-TNIIKVGDLGIARVLENQNDMASTLIGTPYYMSPELFSNK 179
Cdd:cd13974 129 LSEREALVIFYDVVRVVEALHKKNIVHRDLKLGNMVLNKrTRKITITNFCLGKHLVSEDDLLKDQRGSPAYISPDVLSGK 208
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41055987 180 PYNYK-SDVWALGCCVYEMATLKHAFNAKDMNSLVYRI--VEGKLPQmPSKYDPQLGELIKRMLCKKPEDRPDVKHILR 255
Cdd:cd13974 209 PYLGKpSDMWALGVVLFTMLYGQFPFYDSIPQELFRKIkaAEYTIPE-DGRVSENTVCLIRKLLVLNPQKRLTASEVLD 286
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
87-259 1.09e-15

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


Pssm-ID: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 77.47  E-value: 1.09e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  87 GDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQN-IFLTKTNI-IKVGDLGIARVLENQNDMASTL 164
Cdd:cd13976  69 GDLHSYVRSRKR--LREPEAARLFRQIASAVAHCHRNGIVLRDLKLRKfVFADEERTkLRLESLEDAVILEGEDDSLSDK 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 165 IGTPYYMSPELF-SNKPYNYK-SDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLpQMPSKYDPQLGELIKRMLCK 242
Cdd:cd13976 147 HGCPAYVSPEILnSGATYSGKaADVWSLGVILYTMLVGRYPFHDSEPASLFAKIRRGQF-AIPETLSPRARCLIRSLLRR 225
                       170
                ....*....|....*..
gi 41055987 243 KPEDRPDVKHILRQPYI 259
Cdd:cd13976 226 EPSERLTAEDILLHPWL 242
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
7-225 1.26e-15

Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER1, ErbB1) is a receptor PTK (RTK) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands for EGFR include EGF, heparin binding EGF-like growth factor (HBEGF), epiregulin, amphiregulin, TGFalpha, and betacellulin. Upon ligand binding, EGFR can form homo- or heterodimers with other EGFR subfamily members. The EGFR signaling pathway is one of the most important pathways regulating cell proliferation, differentiation, survival, and growth. Overexpression and mutation in the kinase domain of EGFR have been implicated in the development and progression of a variety of cancers. A number of monoclonal antibodies and small molecule inhibitors have been developed that target EGFR, including the antibodies Cetuximab and Panitumumab, which are used in combination with other therapies for the treatment of colorectal cancer and non-small cell lung carcinoma (NSCLC). The small molecule inhibitors Gefitinib (Iressa) and Erlotinib (Tarceva), already used for NSCLC, are undergoing clinical trials for other types of cancer including gastrointestinal, breast, head and neck, and bladder. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 78.91  E-value: 1.26e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   7 VRVVGKGSYGEVN----LVRHKSDRKQYVIKKLNLRTSSRRERRAAEqEAQLLSQLKHPNIVMYRESWEGEDCQLYI-VM 81
Cdd:cd05108  12 IKVLGSGAFGTVYkglwIPEGEKVKIPVAIKELREATSPKANKEILD-EAYVMASVDNPHVCRLLGICLTSTVQLITqLM 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  82 GFcegGDLYHRLKQQKgELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVL-----EN 156
Cdd:cd05108  91 PF---GCLLDYVREHK-DNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLgaeekEY 166
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41055987 157 QNDMASTLIGtpyYMSPELFSNKPYNYKSDVWALGCCVYEMATlkhaFNAKDMNSL----VYRIVEG--KLPQMP 225
Cdd:cd05108 167 HAEGGKVPIK---WMALESILHRIYTHQSDVWSYGVTVWELMT----FGSKPYDGIpaseISSILEKgeRLPQPP 234
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
3-197 1.94e-15

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 78.76  E-value: 1.94e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987    3 GYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKlnlrtssrRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDCQLYIVMG 82
Cdd:PHA03209  67 GYTVIKTLTPGSEGRVFVATKPGQPDPVVLKI--------GQKGTTLIEAMLLQNVNHPSVIRMKDTLVSGAITCMVLPH 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   83 FceGGDLYHRLKQQKGELlPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMAS 162
Cdd:PHA03209 139 Y--SSDLYTYLTKRSRPL-PIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLGAAQFPVVAPAFLG 215
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 41055987  163 tLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEM 197
Cdd:PHA03209 216 -LAGTVETNAPEVLARDKYNSKADIWSAGIVLFEM 249
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
4-247 2.01e-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: 78.94  E-value: 2.01e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRA-AEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMG 82
Cdd:cd05625   3 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAhVKAERDILAEADNEWVVRLYYSFQDKD-NLYFVMD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FCEGGDLYHRLKQQKgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIAR---------- 152
Cdd:cd05625  82 YIPGGDMMSLLIRMG--VFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfrwthdsky 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 153 -------------------------------------VLENQNDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVY 195
Cdd:cd05625 160 yqsgdhlrqdsmdfsnewgdpencrcgdrlkplerraARQHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILF 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 41055987 196 EMATLKHAFNAKDMNSLVYRIVEGKLP-QMP--SKYDPQLGELIKRmLCKKPEDR 247
Cdd:cd05625 240 EMLVGQPPFLAQTPLETQMKVINWQTSlHIPpqAKLSPEASDLIIK-LCRGPEDR 293
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
10-254 2.05e-15

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Many FGFR3 splice variants have been reported with the IIIb and IIIc isoforms being the predominant forms. FGFR3 IIIc is the isoform expressed in chondrocytes, the cells affected in dwarfism, while IIIb is expressed in epithelial cells. FGFR3 ligands include FGF1, FGF2, FGF4, FGF8, FGF9, and FGF23. It is a negative regulator of long bone growth. In the cochlear duct and in the lens, FGFR3 is involved in differentiation while it appears to have a role in cell proliferation in epithelial cells. Germline mutations in FGFR3 are associated with skeletal disorders including several forms of dwarfism. Some missense mutations are associated with multiple myeloma and carcinomas of the bladder and cervix. Overexpression of FGFR3 is found in thyroid carcinoma. FGFR3 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 78.52  E-value: 2.05e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQL-------KHPNIVMYRESWEgEDCQLYIVMG 82
Cdd:cd05100  20 LGEGCFGQVVMAEAIGIDKDKPNKPVTVAVKMLKDDATDKDLSDLVSEMemmkmigKHKNIINLLGACT-QDGPLYVLVE 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FCEGGDL--YHRLKQQKGE-------LLPERQV-----VEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDL 148
Cdd:cd05100  99 YASKGNLreYLRARRPPGMdysfdtcKLPEEQLtfkdlVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADF 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 149 GIARVLENQNDMASTLIGT-PY-YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLVYRIVEGKLPQMP 225
Cdd:cd05100 179 GLARDVHNIDYYKKTTNGRlPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSpYPGIPVEELFKLLKEGHRMDKP 258
                       250       260
                ....*....|....*....|....*....
gi 41055987 226 SKYDPQLGELIKRMLCKKPEDRPDVKHIL 254
Cdd:cd05100 259 ANCTHELYMIMRECWHAVPSQRPTFKQLV 287
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
4-218 2.17e-15

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 79.31  E-value: 2.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987    4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLnLRTSSRRERraaeqEAQLLSQLKHPNIVM-----YRESWEGEDCQLY 78
Cdd:PTZ00036  68 YKLGNIIGNGSFGVVYEAICIDTSEKVAIKKV-LQDPQYKNR-----ELLIMKNLNHINIIFlkdyyYTECFKKNEKNIF 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   79 --IVMGFC-EGGDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLT-KTNIIKVGDLGIAR-V 153
Cdd:PTZ00036 142 lnVVMEFIpQTVHKYMKHYARNNHALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDpNTHTLKLCDFGSAKnL 221
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41055987  154 LENQNDMasTLIGTPYYMSPEL-FSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVE 218
Cdd:PTZ00036 222 LAGQRSV--SYICSRFYRAPELmLGATNYTTHIDLWSLGCIIAEMILGYPIFSGQSSVDQLVRIIQ 285
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
44-208 2.39e-15

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 78.88  E-value: 2.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   44 ERRAAEQEAQLLSQLKHPNIVMYRESWEGEDCQLYIVMGFceGGDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEK 123
Cdd:PHA03212 126 QRGGTATEAHILRAINHPSIIQLKGTFTYNKFTCLILPRY--KTDLYCYLAAKRN--IAICDILAIERSVLRAIQYLHEN 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  124 HILHRDLKTQNIFLTKTNIIKVGDLGIA--RVLENQNDMAStLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLK 201
Cdd:PHA03212 202 RIIHRDIKAENIFINHPGDVCLGDFGAAcfPVDINANKYYG-WAGTIATNAPELLARDPYGPAVDIWSAGIVLFEMATCH 280

                 ....*..
gi 41055987  202 HAFNAKD 208
Cdd:PHA03212 281 DSLFEKD 287
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
8-200 2.50e-15

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. 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: 77.53  E-value: 2.50e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVnlVR------HKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQL-KHPNIVMYRESWEGEDCQLYIV 80
Cdd:cd05054  13 KPLGRGAFGKV--IQasafgiDKSATCRTVAVKMLKEGATASEHKALMTELKILIHIgHHLNVVNLLGACTKPGGPLMVI 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MGFCEGGDLYHRLKQQKGELLPERQ------------------------VVEWFVQIAMALQYLHEKHILHRDLKTQNIF 136
Cdd:cd05054  91 VEFCKFGNLSNYLRSKREEFVPYRDkgardveeeedddelykepltledLICYSFQVARGMEFLASRKCIHRDLAARNIL 170
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41055987 137 LTKTNIIKVGDLGIARVLENQND-MASTLIGTPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATL 200
Cdd:cd05054 171 LSENNVVKICDFGLARDIYKDPDyVRKGDARLPLkWMAPESIFDKVYTTQSDVWSFGVLLWEIFSL 236
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
7-200 2.88e-15

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


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 77.46  E-value: 2.88e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   7 VRVVGKGSYGEV------NLVRHKSDRKQYVIKKLnlrtssrrERRAAEQE-AQLLSQL-------KHPNIVMYRESWEG 72
Cdd:cd05053  17 GKPLGEGAFGQVvkaeavGLDNKPNEVVTVAVKML--------KDDATEKDlSDLVSEMemmkmigKHKNIINLLGACTQ 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  73 EDcQLYIVMGFCEGGDL--YHRLKQQKGEL------------LPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLT 138
Cdd:cd05053  89 DG-PLYVVVEYASKGNLreFLRARRPPGEEaspddprvpeeqLTQKDLVSFAYQVARGMEYLASKKCIHRDLAARNVLVT 167
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41055987 139 KTNIIKVGDLGIARVLENQNDMASTLIG-TPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATL 200
Cdd:cd05053 168 EDNVMKIADFGLARDIHHIDYYRKTTNGrLPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTL 231
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
88-248 2.94e-15

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: 76.76  E-value: 2.94e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  88 DLYHRLKqqKGELLPERQVVEwfVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARvleNQNDMASTLIGT 167
Cdd:cd13975  90 DLYTGIK--AGLSLEERLQIA--LDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFCK---PEAMMSGSIVGT 162
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 168 PYYMSPELFSNKpYNYKSDVWALGCCVYEM----ATLKHAFNAKDMNSLVYRIV-EGKLPQMPSKYDPQLGELIKRMLCK 242
Cdd:cd13975 163 PIHMAPELFSGK-YDNSVDVYAFGILFWYLcaghVKLPEAFEQCASKDHLWNNVrKGVRPERLPVFDEECWNLMEACWSG 241

                ....*.
gi 41055987 243 KPEDRP 248
Cdd:cd13975 242 DPSQRP 247
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
77-251 3.24e-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: 3.24e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  77 LYIVMGFCEGGDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLEN 156
Cdd:cd05083  73 LYIVMELMSKGNLVNFLRSRGRALVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAKVGSM 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 157 QNDMASTLIGtpyYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAK-DMNSLVYRIVEGKLPQMPSKYDPQLGEL 235
Cdd:cd05083 153 GVDNSRLPVK---WTAPEALKNKKFSSKSDVWSYGVLLWEVFSYGRAPYPKmSVKEVKEAVEKGYRMEPPEGCPPDVYSI 229
                       170
                ....*....|....*.
gi 41055987 236 IKRMLCKKPEDRPDVK 251
Cdd:cd05083 230 MTSCWEAEPGKRPSFK 245
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
6-256 3.63e-15

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


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 76.79  E-value: 3.63e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   6 FVRVVGKGSYGEVNLVRHK---SDRKQYVIK-KLNLRTSSRRERRAAEQEAQLLSQLKHPNIV-MYRESWEGED-CQLYI 79
Cdd:cd05050   9 YVRDIGQGAFGRVFQARAPgllPYEPFTMVAvKMLKEEASADMQADFQREAALMAEFDHPNIVkLLGVCAVGKPmCLLFE 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  80 VMGFcegGDL-----------YHRLKQQKGEL---LPERQVVEWFVQIAMALQ------YLHEKHILHRDLKTQNIFLTK 139
Cdd:cd05050  89 YMAY---GDLneflrhrspraQCSLSHSTSSArkcGLNPLPLSCTEQLCIAKQvaagmaYLSERKFVHRDLATRNCLVGE 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 140 TNIIKVGDLGIARVL-------ENQNDMASTligtpYYMSPE-LFSNKpYNYKSDVWALGCCVYEMATLK-HAFNAKDMN 210
Cdd:cd05050 166 NMVVKIADFGLSRNIysadyykASENDAIPI-----RWMPPEsIFYNR-YTTESDVWAYGVVLWEIFSYGmQPYYGMAHE 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 41055987 211 SLVYRIVEGKLPQMPSKYDPQLGELIKRMLCKKPEDRP---DVKHILRQ 256
Cdd:cd05050 240 EVIYYVRDGNVLSCPDNCPLELYNLMRLCWSKLPSDRPsfaSINRILQR 288
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
8-200 3.75e-15

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: 76.93  E-value: 3.75e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEV--NLVRHKSDRKQY--VIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEgEDCQLYIVMGF 83
Cdd:cd05045   6 KTLGEGEFGKVvkATAFRLKGRAGYttVAVKMLKENASSSELRDLLSEFNLLKQVNHPHVIKLYGACS-QDGPLLLIVEY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGGDL--YHRLKQQKG--------------------ELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTN 141
Cdd:cd05045  85 AKYGSLrsFLRESRKVGpsylgsdgnrnssyldnpdeRALTMGDLISFAWQISRGMQYLAEMKLVHRDLAARNVLVAEGR 164
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41055987 142 IIKVGDLGIAR-VLENQNDMASTLIGTPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATL 200
Cdd:cd05045 165 KMKISDFGLSRdVYEEDSYVKRSKGRIPVkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTL 225
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
30-258 4.74e-15

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: 76.59  E-value: 4.74e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  30 YVIKKLNLRTSSRRER--------RAAEQeaqlLSQLKHPNIVMYRESWEGED-----------CQLYIVMGfcEGGDLY 90
Cdd:cd14011  27 FVFEKKQLEEYSKRDReqilellkRGVKQ----LTRLRHPRILTVQHPLEESReslafatepvfASLANVLG--ERDNMP 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  91 HRLKQQKGELLPERQVVEWFVQIAMALQYLH-EKHILHRDLKTQNIFLTKTNIIKVGDLGIA-----------RVLENQN 158
Cdd:cd14011 101 SPPPELQDYKLYDVEIKYGLLQISEALSFLHnDVKLVHGNICPESVVINSNGEWKLAGFDFCisseqatdqfpYFREYDP 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 159 DMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEM-ATLKHAFNAKDmNSLVYRIVEGKLPQMP----SKYDPQLG 233
Cdd:cd14011 181 NLPPLAQPNLNYLAPEYILSKTCDPASDMFSLGVLIYAIyNKGKPLFDCVN-NLLSYKKNSNQLRQLSlsllEKVPEELR 259
                       250       260
                ....*....|....*....|....*
gi 41055987 234 ELIKRMLCKKPEDRPDVKHILRQPY 258
Cdd:cd14011 260 DHVKTLLNVTPEVRPDAEQLSKIPF 284
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
8-249 5.37e-15

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


Pssm-ID: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 75.97  E-value: 5.37e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEV---NLVRHKSDRKQYVIKKLNlRTSSRRERRAAEQEAQLLSQLKHPNIV-MYRESWEGEDCQLyIVMGF 83
Cdd:cd05058   1 EVIGKGHFGCVyhgTLIDSDGQKIHCAVKSLN-RITDIEEVEQFLKEGIIMKDFSHPNVLsLLGICLPSEGSPL-VVLPY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGGDLYHRLKQQKGEllPE-RQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIAR-VLEN----- 156
Cdd:cd05058  79 MKHGDLRNFIRSETHN--PTvKDLIGFGLQVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVADFGLARdIYDKeyysv 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 157 QNDMASTLigtPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATlKHAFNAKDMNS--LVYRIVEG-KLPQMPSKYDPqL 232
Cdd:cd05058 157 HNHTGAKL---PVkWMALESLQTQKFTTKSDVWSFGVLLWELMT-RGAPPYPDVDSfdITVYLLQGrRLLQPEYCPDP-L 231
                       250
                ....*....|....*..
gi 41055987 233 GELIKRMLCKKPEDRPD 249
Cdd:cd05058 232 YEVMLSCWHPKPEMRPT 248
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
4-270 7.32e-15

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 77.58  E-value: 7.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987    4 YLFVRVVGKGSYGEVNL-VRHKSDRKQYVIKKLNLRTssrrerRAAEQEAQLLSQLKHPNIV--MYRESWEGEDCQLYIV 80
Cdd:PHA03207  94 YNILSSLTPGSEGEVFVcTKHGDEQRKKVIVKAVTGG------KTPGREIDILKTISHRAIInlIHAYRWKSTVCMVMPK 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   81 MGFceggDLYHRLkqQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDM 160
Cdd:PHA03207 168 YKC----DLFTYV--DRSGPLPLEQAITIQRRLLEALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGAACKLDAHPDT 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  161 ASTL--IGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNS--------------------------L 212
Cdd:PHA03207 242 PQCYgwSGTLETNSPELLALDPYCAKTDIWSAGLVLFEMSVKNVTLFGKQVKSsssqlrsiircmqvhplefpqngstnL 321
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41055987  213 V-----YRIVEGK---LPQMPSKYDPQLGE--LIKRMLCKKPEDRPDVKHILRQPYIKHQISMFLEAT 270
Cdd:PHA03207 322 CkhfkqYAIVLRPpytIPPVIRKYGMHMDVeyLIAKMLTFDQEFRPSAQDILSLPLFTKEPINLLNIT 389
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
10-256 9.43e-15

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


Pssm-ID: 270638 [Multi-domain]  Cd Length: 269  Bit Score: 75.32  E-value: 9.43e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSDRK--QYVIKKLNlRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWeGEDCQLYIVMGFCEGG 87
Cdd:cd05042   3 IGNGWFGKVLLGEIYSGTSvaQVVVKELK-ASANPKEQDTFLKEGQPYRILQHPNILQCLGQC-VEAIPYLLVMEFCDLG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  88 DLYHRLKQQKGELLPERQVV---EWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIA--RVLENQNDMAS 162
Cdd:cd05042  81 DLKAYLRSEREHERGDSDTRtlqRMACEVAAGLAHLHKLNFVHSDLALRNCLLTSDLTVKIGDYGLAhsRYKEDYIETDD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 163 TLIGTPYYMSPELFSNKPYNY-------KSDVWALGCCVYEMATL--KHAFNAKDMNSLVYRIVEGKL----PQMPSKYD 229
Cdd:cd05042 161 KLWFPLRWTAPELVTEFHDRLlvvdqtkYSNIWSLGVTLWELFENgaQPYSNLSDLDVLAQVVREQDTklpkPQLELPYS 240
                       250       260
                ....*....|....*....|....*...
gi 41055987 230 PQLGELIKrmLC-KKPEDRPDVKHILRQ 256
Cdd:cd05042 241 DRWYEVLQ--FCwLSPEQRPAAEDVHLL 266
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
4-259 9.44e-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: 75.01  E-value: 9.44e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRErraAEQEAQLLSQLKHPNIVMYRESWEGEDCQLyIVMGF 83
Cdd:cd14113   9 YSEVAELGRGRFSVVKKCDQRGTKRAVATKFVNKKLMKRDQ---VTHELGVLQSLQHPQLVGLLDTFETPTSYI-LVLEM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGGDLYHRLKQQKGelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTN---IIKVGDLGIARVLeNQNDM 160
Cdd:cd14113  85 ADQGRLLDYVVRWGN--LTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLskpTIKLADFGDAVQL-NTTYY 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 161 ASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLpQMPSKYDPQLGELIKRML 240
Cdd:cd14113 162 IHQLLGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLDF-SFPDDYFKGVSQKAKDFV 240
                       250       260
                ....*....|....*....|...
gi 41055987 241 C----KKPEDRPDVKHILRQPYI 259
Cdd:cd14113 241 CfllqMDPAKRPSAALCLQEQWL 263
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
6-254 1.50e-14

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


Pssm-ID: 133219 [Multi-domain]  Cd Length: 303  Bit Score: 75.42  E-value: 1.50e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   6 FVRVVGKGSYGEVNLVRHKSD--RKQYVIKKLNlRTSSRRERRAAEQEAQLLSQL-KHPNIVMYRESWEGEDcQLYIVMG 82
Cdd:cd05088  11 FQDVIGEGNFGQVLKARIKKDglRMDAAIKRMK-EYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRG-YLYLAIE 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FCEGGDLYHRLKQQK--------------GELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDL 148
Cdd:cd05088  89 YAPHGNLLDFLRKSRvletdpafaianstASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADF 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 149 GIARVLENQndMASTLIGTPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLVYRIVEGKLPQMPS 226
Cdd:cd05088 169 GLSRGQEVY--VKKTMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTpYCGMTCAELYEKLPQGYRLEKPL 246
                       250       260
                ....*....|....*....|....*...
gi 41055987 227 KYDPQLGELIKRMLCKKPEDRPDVKHIL 254
Cdd:cd05088 247 NCDDEVYDLMRQCWREKPYERPSFAQIL 274
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
6-198 1.72e-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: 75.41  E-value: 1.72e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   6 FVRVVGKG--SYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEgEDCQLYIVMGF 83
Cdd:cd08216   2 LLYEIGKCfkGGGVVHLAKHKPTNTLVAVKKINLESDSKEDLKFLQQEILTSRQLQHPNILPYVTSFV-VDNDLYVVTPL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGGDLYHRLKQQKGELLPE-------RQVVEwfvqiamALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLEN 156
Cdd:cd08216  81 MAYGSCRDLLKTHFPEGLPElaiafilRDVLN-------ALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYAYSMVK 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 41055987 157 QNDMASTLIGTP-------YYMSPELF--SNKPYNYKSDVWALG--CCvyEMA 198
Cdd:cd08216 154 HGKRQRVVHDFPksseknlPWLSPEVLqqNLLGYNEKSDIYSVGitAC--ELA 204
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
5-200 1.79e-14

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


Pssm-ID: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 75.07  E-value: 1.79e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   5 LFVRVVGKGSYGEVNLV---------------RHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRes 69
Cdd:cd05051   8 EFVEKLGEGQFGEVHLCeanglsdltsddfigNDNKDEPVLVAVKMLRPDASKNAREDFLKEVKIMSQLKDPNIVRLL-- 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  70 weG---EDCQLYIVMGFCEGGDLYHRLKQQKGE----------LLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIF 136
Cdd:cd05051  86 --GvctRDEPLCMIVEYMENGDLNQFLQKHEAEtqgasatnskTLSYGTLLYMATQIASGMKYLESLNFVHRDLATRNCL 163
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41055987 137 LTKTNIIKVGDLGIARVLENQNdmastligtpYY------------MSPELFSNKPYNYKSDVWALGCCVYEMATL 200
Cdd:cd05051 164 VGPNYTIKIADFGMSRNLYSGD----------YYriegravlpirwMAWESILLGKFTTKSDVWAFGVTLWEILTL 229
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
9-224 1.82e-14

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


Pssm-ID: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 74.66  E-value: 1.82e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   9 VVGKGSYGEVnlvRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEGGD 88
Cdd:cd14153   7 LIGKGRFGQV---YHGRWHGEVAIRLIDIERDNEEQLKAFKREVMAYRQTRHENVVLFMGACMSPP-HLAIITSLCKGRT 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  89 LYHRLKQQKG--ELLPERQVVEwfvQIAMALQYLHEKHILHRDLKTQNIFLT--KTNIIKVGDLGIARVLE--NQNDMAS 162
Cdd:cd14153  83 LYSVVRDAKVvlDVNKTRQIAQ---EIVKGMGYLHAKGILHKDLKSKNVFYDngKVVITDFGLFTISGVLQagRREDKLR 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41055987 163 TLIGTPYYMSPELF--------SNK-PYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLPQM 224
Cdd:cd14153 160 IQSGWLCHLAPEIIrqlspeteEDKlPFSKHSDVFAFGTIWYELHAREWPFKTQPAEAIIWQVGSGMKPNL 230
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
8-255 2.27e-14

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


Pssm-ID: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 74.66  E-value: 2.27e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVR---HKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIV-MYRESWEGEdcQLYIVMGF 83
Cdd:cd05094  11 RELGEGAFGKVFLAEcynLSPTKDKMLVAVKTLKDPTLAARKDFQREAELLTNLQHDHIVkFYGVCGDGD--PLIMVFEY 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGGDLYHRLK---------------QQKGELlPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDL 148
Cdd:cd05094  89 MKHGDLNKFLRahgpdamilvdgqprQAKGEL-GLSQMLHIATQIASGMVYLASQHFVHRDLATRNCLVGANLLVKIGDF 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 149 GIARVLENQN--DMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYR-IVEGKLPQMP 225
Cdd:cd05094 168 GMSRDVYSTDyyRVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLSNTEVIEcITQGRVLERP 247
                       250       260       270
                ....*....|....*....|....*....|
gi 41055987 226 SKYDPQLGELIKRMLCKKPEDRPDVKHILR 255
Cdd:cd05094 248 RVCPKEVYDIMLGCWQREPQQRLNIKEIYK 277
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
2-199 2.33e-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: 74.92  E-value: 2.33e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKklnLRTSSRRERRAAEQEAQLLSQL-----KHP---NIVMYRESWE-- 71
Cdd:cd14136  10 GRYHVVRKLGWGHFSTVWLCWDLQNKRFVALK---VVKSAQHYTEAALDEIKLLKCVreadpKDPgreHVVQLLDDFKht 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  72 GEDCQlYIVMGFCEGGD-LYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEK-HILHRDLKTQNIFLTKTNI-IKVGDL 148
Cdd:cd14136  87 GPNGT-HVCMVFEVLGPnLLKLIKRYNYRGIPLPLVKKIARQVLQGLDYLHTKcGIIHTDIKPENVLLCISKIeVKIADL 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 41055987 149 GIARVLENQ--NDmastlIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMAT 199
Cdd:cd14136 166 GNACWTDKHftED-----IQTRQYRSPEVILGAGYGTPADIWSTACMAFELAT 213
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
9-198 3.13e-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: 74.01  E-value: 3.13e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   9 VVGKGSYGEVnlVRHKSDRKQYVIKKLnlrtsSRRERRAAEQEAQLLS--QLKHPNIVMY---RESWEGEDCQLYIVMGF 83
Cdd:cd13998   2 VIGKGRFGEV--WKASLKNEPVAVKIF-----SSRDKQSWFREKEIYRtpMLKHENILQFiaaDERDTALRTELWLVTAF 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGGDLYHRLKqqkgellpeRQVVEW------FVQIAMALQYLHEKH---------ILHRDLKTQNIFLTKTNIIKVGDL 148
Cdd:cd13998  75 HPNGSL*DYLS---------LHTIDWvslcrlALSVARGLAHLHSEIpgctqgkpaIAHRDLKSKNILVKNDGTCCIADF 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 149 GIARVLE---NQNDMA-STLIGTPYYMSPEL------FSNKPYNYKSDVWALGCCVYEMA 198
Cdd:cd13998 146 GLAVRLSpstGEEDNAnNGQVGTKRYMAPEVlegainLRDFESFKRVDIYAMGLVLWEMA 205
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
60-258 3.72e-14

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: 73.16  E-value: 3.72e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  60 HPNIVMYRESWEGeDCQLYIvmgFCEG--GDLYHRLKQQKgeLLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQN-IF 136
Cdd:cd14023  44 HRNITGIVEVILG-DTKAYV---FFEKdfGDMHSYVRSCK--RLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKfVF 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 137 LTKTNI-IKVGDLGIARVLENQNDMASTLIGTPYYMSPELFSNK-PYNYKS-DVWALGCCVYEMATLKHAFNAKDMNSLV 213
Cdd:cd14023 118 SDEERTqLRLESLEDTHIMKGEDDALSDKHGCPAYVSPEILNTTgTYSGKSaDVWSLGVMLYTLLVGRYPFHDSDPSALF 197
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 41055987 214 YRIVEGKLPqMPSKYDPQLGELIKRMLCKKPEDRPDVKHILRQPY 258
Cdd:cd14023 198 SKIRRGQFC-IPDHVSPKARCLIRSLLRREPSERLTAPEILLHPW 241
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
4-260 4.26e-14

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: 74.37  E-value: 4.26e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVnLVRHKSDRKQYV-IKKLN----LRTSSRRERRaaeqEAQLLSQLKHPNIV----MYRESWEGED 74
Cdd:cd07850   2 YQNLKPIGSGAQGIV-CAAYDTVTGQNVaIKKLSrpfqNVTHAKRAYR----ELVLMKLVNHKNIIgllnVFTPQKSLEE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  75 CQ-LYIVMGFCEggdlyHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARV 153
Cdd:cd07850  77 FQdVYLVMELMD-----ANLCQVIQMDLDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLART 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 154 lENQNDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKD-------------------MNSL-- 212
Cdd:cd07850 152 -AGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIRGTVLFPGTDhidqwnkiieqlgtpsdefMSRLqp 230
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41055987 213 -VYRIVEGKLPQMPSKYD--------------------PQLGELIKRMLCKKPEDRPDVKHILRQPYIK 260
Cdd:cd07850 231 tVRNYVENRPKYAGYSFEelfpdvlfppdseehnklkaSQARDLLSKMLVIDPEKRISVDDALQHPYIN 299
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
112-222 4.73e-14

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: 74.18  E-value: 4.73e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 112 QIAMALQYLHEKHILHRDLKTQNIFLT-KTNIIKVGDLGIArVLENQNDMastligTPY-----YMSPELFSNKPYNYKS 185
Cdd:cd14135 113 QLFLALKHLKKCNILHADIKPDNILVNeKKNTLKLCDFGSA-SDIGENEI------TPYlvsrfYRAPEIILGLPYDYPI 185
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 41055987 186 DVWALGCCVYEMATLKHAFNAKDMNSLVYRIVE--GKLP 222
Cdd:cd14135 186 DMWSVGCTLYELYTGKILFPGKTNNHMLKLMMDlkGKFP 224
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
6-197 5.04e-14

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: 73.45  E-value: 5.04e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   6 FVRVVGKGSYGEVNLVRHKSD--RKQYVIKKLNLrTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEgEDCQLYIVMGF 83
Cdd:cd14206   1 YLQEIGNGWFGKVILGEIFSDytPAQVVVKELRV-SAGPLEQRKFISEAQPYRSLQHPNILQCLGLCT-ETIPFLLIMEF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGGDLYHRLKQQKG------ELLPE--RQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIArvle 155
Cdd:cd14206  79 CQLGDLKRYLRAQRKadgmtpDLPTRdlRTLQRMAYEITLGLLHLHKNNYIHSDLALRNCLLTSDLTVRIGDYGLS---- 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 41055987 156 nQNDMASTLIGTP-------YYMSPELFSNKPYNY-------KSDVWALGCCVYEM 197
Cdd:cd14206 155 -HNNYKEDYYLTPdrlwiplRWVAPELLDELHGNLivvdqskESNVWSLGVTIWEL 209
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
9-198 5.48e-14

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


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 73.46  E-value: 5.48e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   9 VVGKGSYGEVNLVRHksdRKQYVIKKlnlrTSSRRERRAAEQEAQLLSQ--LKHPNIVMY-------RESWEgedcQLYI 79
Cdd:cd14056   2 TIGKGRYGEVWLGKY---RGEKVAVK----IFSSRDEDSWFRETEIYQTvmLRHENILGFiaadiksTGSWT----QLWL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  80 VMGFCEGGDLYHRLkqQKGELLPErQVVEWFVQIAMALQYLH-EKH-------ILHRDLKTQNIFLTKTNIIKVGDLGIA 151
Cdd:cd14056  71 ITEYHEHGSLYDYL--QRNTLDTE-EALRLAYSAASGLAHLHtEIVgtqgkpaIAHRDLKSKNILVKRDGTCCIADLGLA 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41055987 152 RVLENQNDM----ASTLIGTPYYMSPELFSNK--PYN---YK-SDVWALGCCVYEMA 198
Cdd:cd14056 148 VRYDSDTNTidipPNPRVGTKRYMAPEVLDDSinPKSfesFKmADIYSFGLVLWEIA 204
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
7-247 7.99e-14

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


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 72.86  E-value: 7.99e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   7 VRVVGKGSYGEVNlvrhksdRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQ--LKHPNIVMYRES---WEGEDCQLYIVM 81
Cdd:cd14142  10 VECIGKGRYGEVW-------RGQWQGESVAVKIFSSRDEKSWFRETEIYNTvlLRHENILGFIASdmtSRNSCTQLWLIT 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  82 GFCEGGDLYHRLKQQKgelLPERQVVEWFVQIAMALQYLH--------EKHILHRDLKTQNIFLTKTNIIKVGDLGIA-- 151
Cdd:cd14142  83 HYHENGSLYDYLQRTT---LDHQEMLRLALSAASGLVHLHteifgtqgKPAIAHRDLKSKNILVKSNGQCCIADLGLAvt 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 152 -RVLENQNDMAS-TLIGTPYYMSPELFsNKPYNYKS-------DVWALGCCVYEMA----------TLKHAF-------- 204
Cdd:cd14142 160 hSQETNQLDVGNnPRVGTKRYMAPEVL-DETINTDCfesykrvDIYAFGLVLWEVArrcvsggiveEYKPPFydvvpsdp 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 41055987 205 NAKDMNSLVyrIVEGKLPQMPSKY--DPQLGELIKRM---LCKKPEDR 247
Cdd:cd14142 239 SFEDMRKVV--CVDQQRPNIPNRWssDPTLTAMAKLMkecWYQNPSAR 284
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
10-248 8.91e-14

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


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 72.69  E-value: 8.91e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  10 VGKGSYGEVNLVRHKSdrkQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESwegedC----QLYIVMGFCE 85
Cdd:cd14152   8 IGQGRWGKVHRGRWHG---EVAIRLLEIDGNNQDHLKLFKKEVMNYRQTRHENVVLFMGA-----CmhppHLAIITSFCK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  86 GGDLYHRLKQQKGEL--LPERQVVEwfvQIAMALQYLHEKHILHRDLKTQNIFLT--KTNIIKVGDLGIARVL-----EN 156
Cdd:cd14152  80 GRTLYSFVRDPKTSLdiNKTRQIAQ---EIIKGMGYLHAKGIVHKDLKSKNVFYDngKVVITDFGLFGISGVVqegrrEN 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 157 QNDMASTLIgtpYYMSPELFSNK---------PYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGK-LPQMPS 226
Cdd:cd14152 157 ELKLPHDWL---CYLAPEIVREMtpgkdedclPFSKAADVYAFGTIWYELQARDWPLKNQPAEALIWQIGSGEgMKQVLT 233
                       250       260
                ....*....|....*....|....
gi 41055987 227 KYD--PQLGELIKRMLCKKPEDRP 248
Cdd:cd14152 234 TISlgKEVTEILSACWAFDLEERP 257
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
7-225 1.02e-13

Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER4 (ErbB4) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands that bind HER4 fall into two groups, the neuregulins (or heregulins) and some EGFR (HER1) ligands including betacellulin, HBEGF, and epiregulin. All four neuregulins (NRG1-4) interact with HER4. Upon ligand binding, HER4 forms homo- or heterodimers with other HER proteins. HER4 is essential in embryonic development. It is implicated in mammary gland, cardiac, and neural development. As a postsynaptic receptor of NRG1, HER4 plays an important role in synaptic plasticity and maturation. The impairment of NRG1/HER4 signaling may contribute to schizophrenia. The HER4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173655 [Multi-domain]  Cd Length: 303  Bit Score: 72.79  E-value: 1.02e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   7 VRVVGKGSYGEVN----LVRHKSDRKQYVIKKLNlRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDCQLyiVMG 82
Cdd:cd05110  12 VKVLGSGAFGTVYkgiwVPEGETVKIPVAIKILN-ETTGPKANVEFMDEALIMASMDHPHLVRLLGVCLSPTIQL--VTQ 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FCEGGDLYHRLKQQKGELlPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMAS 162
Cdd:cd05110  89 LMPHGCLLDYVHEHKDNI-GSQLLLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLARLLEGDEKEYN 167
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41055987 163 TLIGTP--YYMSPELFSNKPYNYKSDVWALGCCVYEMATlkhaFNAKDMNSLVYRIVEG------KLPQMP 225
Cdd:cd05110 168 ADGGKMpiKWMALECIHYRKFTHQSDVWSYGVTIWELMT----FGGKPYDGIPTREIPDllekgeRLPQPP 234
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
4-172 1.19e-13

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


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 72.10  E-value: 1.19e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIK--KLNLRTSSrrerraAEQEAQLLSQLK-HPNI-VMYresWEGEDCQL-Y 78
Cdd:cd14016   2 YKLVKKIGSGSFGEVYLGIDLKTGEEVAIKieKKDSKHPQ------LEYEAKVYKLLQgGPGIpRLY---WFGQEGDYnV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  79 IVMGFCeGGDLYHrLKQQKGELLPERQVVewfvQIAM----ALQYLHEKHILHRDLKTQNiFLT----KTNIIKVGDLGI 150
Cdd:cd14016  73 MVMDLL-GPSLED-LFNKCGRKFSLKTVL----MLADqmisRLEYLHSKGYIHRDIKPEN-FLMglgkNSNKVYLIDFGL 145
                       170       180
                ....*....|....*....|....*....
gi 41055987 151 A---RVLENQNDMAST----LIGTPYYMS 172
Cdd:cd14016 146 AkkyRDPRTGKHIPYRegksLTGTARYAS 174
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
1-218 2.04e-13

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


Pssm-ID: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 71.80  E-value: 2.04e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   1 MDGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKL-NLRTssRRERRaaeqEAQLLSQLK-HPNIVmyreswegedcQLY 78
Cdd:cd14132  17 QDDYEIIRKIGRGKYSEVFEGINIGNNEKVVIKVLkPVKK--KKIKR----EIKILQNLRgGPNIV-----------KLL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  79 ------------IVMGFCEGGDLYHRLKQqkgelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTN-IIKV 145
Cdd:cd14132  80 dvvkdpqsktpsLIFEYVNNTDFKTLYPT-----LTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDHEKrKLRL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 146 GDLGIA-----------RVlenqndmastliGTPYYMSPE-LFSNKPYNYKSDVWALGCCVYEMATLK-HAFNAKDMNSL 212
Cdd:cd14132 155 IDWGLAefyhpgqeynvRV------------ASRYYKGPElLVDYQYYDYSLDMWSLGCMLASMIFRKePFFHGHDNYDQ 222

                ....*.
gi 41055987 213 VYRIVE 218
Cdd:cd14132 223 LVKIAK 228
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
4-259 2.29e-13

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: 72.37  E-value: 2.29e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIV----MYRESWEGEDCQ-LY 78
Cdd:cd07876  23 YQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRPFQNQTHAKRAYRELVLLKCVNHKNIIsllnVFTPQKSLEEFQdVY 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  79 IVMGFCEGGdlyhrLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVlENQN 158
Cdd:cd07876 103 LVMELMDAN-----LCQVIHMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLART-ACTN 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 159 DMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKD-------------------MNSL---VYRI 216
Cdd:cd07876 177 FMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGSVIFQGTDhidqwnkvieqlgtpsaefMNRLqptVRNY 256
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41055987 217 VEGKlPQMP----------------SKYD----PQLGELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd07876 257 VENR-PQYPgisfeelfpdwifpseSERDklktSQARDLLSKMLVIDPDKRISVDEALRHPYI 318
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
7-225 2.36e-13

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: 71.21  E-value: 2.36e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   7 VRVVGKGSYGEVN----LVRHKSDRKQYVIKKLNLRTSSRRERRAAEqEAQLLSQLKHPNIVMYRESWEGEDCQLyiVMG 82
Cdd:cd05109  12 VKVLGSGAFGTVYkgiwIPDGENVKIPVAIKVLRENTSPKANKEILD-EAYVMAGVGSPYVCRLLGICLTSTVQL--VTQ 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  83 FCEGGDLYHRLKQQKGELlPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLE-NQNDMA 161
Cdd:cd05109  89 LMPYGCLLDYVRENKDRI-GSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDiDETEYH 167
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41055987 162 STLIGTPY-YMSPELFSNKPYNYKSDVWALGCCVYEMATlkhaFNAKDMNSLVYR----IVEG--KLPQMP 225
Cdd:cd05109 168 ADGGKVPIkWMALESILHRRFTHQSDVWSYGVTVWELMT----FGAKPYDGIPAReipdLLEKgeRLPQPP 234
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
6-253 2.42e-13

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


Pssm-ID: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 71.17  E-value: 2.42e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   6 FVRVVGKGSYGEVNL--VRHKSDRKQYVIKKLNLRTSSRRERRAAEqEAQLLSQLKHPNIVMYReSWEGEDCQLYIVMGF 83
Cdd:cd05087   1 YLKEIGHGWFGKVFLgeVNSGLSSTQVVVKELKASASVQDQMQFLE-EAQPYRALQHTNLLQCL-AQCAEVTPYLLVMEF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGGDLYHRLKQQKG--ELLPERQVVEWFV-QIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARvLENQND- 159
Cdd:cd05087  79 CPLGDLKGYLRSCRAaeSMAPDPLTLQRMAcEVACGLLHLHRNNFVHSDLALRNCLLTADLTVKIGDYGLSH-CKYKEDy 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 160 -MASTLIGTPY-YMSPELFSNKPYNY-------KSDVWALGCCVYEMATL--KHAFNAKDMNSLVYRIVEGKL----PQM 224
Cdd:cd05087 158 fVTADQLWVPLrWIAPELVDEVHGNLlvvdqtkQSNVWSLGVTIWELFELgnQPYRHYSDRQVLTYTVREQQLklpkPQL 237
                       250       260       270
                ....*....|....*....|....*....|
gi 41055987 225 PSKYDPQLGELIKrmLC-KKPEDRPDVKHI 253
Cdd:cd05087 238 KLSLAERWYEVMQ--FCwLQPEQRPTAEEV 265
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
106-248 2.82e-13

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


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 71.96  E-value: 2.82e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 106 VVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIAR-VLENQNDMASTLIGTPY-YMSPELFSNKPYNY 183
Cdd:cd14207 182 LISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARdIYKNPDYVRKGDARLPLkWMAPESIFDKIYST 261
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41055987 184 KSDVWALGCCVYEMATLKHA-FNAKDMNS-LVYRIVEGKLPQMPSKYDPQLGELIKRMLCKKPEDRP 248
Cdd:cd14207 262 KSDVWSYGVLLWEIFSLGASpYPGVQIDEdFCSKLKEGIRMRAPEFATSEIYQIMLDCWQGDPNERP 328
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
7-254 5.68e-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: 70.33  E-value: 5.68e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   7 VRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRT-SSRRERRAAEQEAQLLSQLKHPNIVMyreswegedcqlyiVMGFCE 85
Cdd:cd14026   2 LRYLSRGAFGTVSRARHADWRVTVAIKCLKLDSpVGDSERNCLLKEAEILHKARFSYILP--------------ILGICN 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  86 GGDLYHRLKQ-----QKGELLPERQV---VEW------FVQIAMALQYLHEKH--ILHRDLKTQNIFLTKTNIIKVGDLG 149
Cdd:cd14026  68 EPEFLGIVTEymtngSLNELLHEKDIypdVAWplrlriLYEIALGVNYLHNMSppLLHHDLKTQNILLDGEFHVKIADFG 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 150 IA--RVLENQNDMASTLI---GTPYYMSPELFS---NKPYNYKSDVWALGCCVYEMATLKHAF-NAKDMNSLVYRIVEGK 220
Cdd:cd14026 148 LSkwRQLSISQSRSSKSApegGTIIYMPPEEYEpsqKRRASVKHDIYSYAIIMWEVLSRKIPFeEVTNPLQIMYSVSQGH 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 41055987 221 LPQMPSK---YD-PQLGELIKRM---LCKKPEDRPDVKHIL 254
Cdd:cd14026 228 RPDTGEDslpVDiPHRATLINLIesgWAQNPDERPSFLKCL 268
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
8-198 6.88e-13

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


Pssm-ID: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 70.07  E-value: 6.88e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHKSDRkqyVIKKLNLRTSSRRERRAAEQEAQLLsqLKHPNIVMYRES---WEGEDCQLYIVMGFC 84
Cdd:cd14220   1 RQIGKGRYGEVWMGKWRGEK---VAVKVFFTTEEASWFRETEIYQTVL--MRHENILGFIAAdikGTGSWTQLYLITDYH 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  85 EGGDLYHRLKQQKgelLPERQVVEWFVQIAMALQYLHEK--------HILHRDLKTQNIFLTKTNIIKVGDLGIARVLE- 155
Cdd:cd14220  76 ENGSLYDFLKCTT---LDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGTCCIADLGLAVKFNs 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 41055987 156 --NQNDMA-STLIGTPYYMSPELFSN-------KPYnYKSDVWALGCCVYEMA 198
Cdd:cd14220 153 dtNEVDVPlNTRVGTKRYMAPEVLDEslnknhfQAY-IMADIYSFGLIIWEMA 204
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
45-197 2.10e-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: 68.51  E-value: 2.10e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  45 RRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIVMGFCEGGDLYHRL---------------KQQKGELLPErQVVEW 109
Cdd:cd05091  53 REEFRHEAMLRSRLQHPNIVCLLGVVTKEQ-PMSMIFSYCSHGDLHEFLvmrsphsdvgstdddKTVKSTLEPA-DFLHI 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 110 FVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQnDMASTLIGTPY---YMSPELFSNKPYNYKSD 186
Cdd:cd05091 131 VTQIAAGMEYLSSHHVVHKDLATRNVLVFDKLNVKISDLGLFREVYAA-DYYKLMGNSLLpirWMSPEAIMYGKFSIDSD 209
                       170
                ....*....|.
gi 41055987 187 VWALGCCVYEM 197
Cdd:cd05091 210 IWSYGVVLWEV 220
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
112-254 2.60e-12

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: 69.65  E-value: 2.60e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 112 QIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIAR-VLENQNDMASTLIGTPY-YMSPELFSNKPYNYKSDVWA 189
Cdd:cd05107 247 QVANGMEFLASKNCVHRDLAARNVLICEGKLVKICDFGLARdIMRDSNYISKGSTFLPLkWMAPESIFNNLYTTLSDVWS 326
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41055987 190 LGCCVYEMATLKHA-FNAKDMNSLVYR-IVEGKLPQMPSKYDPQLGELIKRMLCKKPEDRPDVKHIL 254
Cdd:cd05107 327 FGILLWEIFTLGGTpYPELPMNEQFYNaIKRGYRMAKPAHASDEIYEIMQKCWEEKFEIRPDFSQLV 393
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
23-259 2.68e-12

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: 67.60  E-value: 2.68e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  23 HKSDRKQYVIKKLNLRtssrrerRAAEQEAQLLSQLKHPNIVMYRESWEGEDcQLYIvmgFCEG--GDLYHRLKQQKGel 100
Cdd:cd14024  14 HYQTEKEYTCKVLSLR-------SYQECLAPYDRLGPHEGVCSVLEVVIGQD-RAYA---FFSRhyGDMHSHVRRRRR-- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 101 LPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLT---KTNIIKVGdLGIARVLENQNDMASTLIGTPYYMSPELFS 177
Cdd:cd14024  81 LSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTdelRTKLVLVN-LEDSCPLNGDDDSLTDKHGCPAYVGPEILS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 178 NK-PYNYK-SDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEGKLpQMPSKYDPQLGELIKRMLCKKPEDRPDVKHILR 255
Cdd:cd14024 160 SRrSYSGKaADVWSLGVCLYTMLLGRYPFQDTEPAALFAKIRRGAF-SLPAWLSPGARCLVSCMLRRSPAERLKASEILL 238

                ....
gi 41055987 256 QPYI 259
Cdd:cd14024 239 HPWL 242
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
6-197 3.20e-12

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: 68.17  E-value: 3.20e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   6 FVRVVGKGSYGEV---NLVRHKSDRK--QYVIKKLNlRTSSRRERRAAEQEAQLLSQLKHPNIVmyreswegedCQLYIV 80
Cdd:cd05048   9 FLEELGEGAFGKVykgELLGPSSEESaiSVAIKTLK-ENASPKTQQDFRREAELMSDLQHPNIV----------CLLGVC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MG---------FCEGGDLYHRLKQQK--------------GELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFL 137
Cdd:cd05048  78 TKeqpqcmlfeYMAHGDLHEFLVRHSphsdvgvssdddgtASSLDQSDFLHIAIQIAAGMEYLSSHHYVHRDLAARNCLV 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41055987 138 TKTNIIKVGDLGIARvlenqnDMAStligTPYY------------MSPELFSNKPYNYKSDVWALGCCVYEM 197
Cdd:cd05048 158 GDGLTVKISDFGLSR------DIYS----SDYYrvqsksllpvrwMPPEAILYGKFTTESDVWSFGVVLWEI 219
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
5-200 3.51e-12

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


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 68.08  E-value: 3.51e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   5 LFVRVVGKGSYGEVNLVR-------------HKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWE 71
Cdd:cd05097   8 RLKEKLGEGQFGEVHLCEaeglaeflgegapEFDGQPVLVAVKMLRADVTKTARNDFLKEIKIMSRLKNPNIIRLLGVCV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  72 GEDcQLYIVMGFCEGGDLYHRLKQQ-------KGELLPE---RQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTN 141
Cdd:cd05097  88 SDD-PLCMITEYMENGDLNQFLSQReiestftHANNIPSvsiANLLYMAVQIASGMKYLASLNFVHRDLATRNCLVGNHY 166
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41055987 142 IIKVGDLGIARVLENQN--DMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATL 200
Cdd:cd05097 167 TIKIADFGMSRNLYSGDyyRIQGRAVLPIRWMAWESILLGKFTTASDVWAFGVTLWEMFTL 227
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
87-253 4.76e-12

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


Pssm-ID: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 68.90  E-value: 4.76e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  87 GDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLENQNDMASTliG 166
Cdd:cd05105 220 SEVKNLLSDDGSEGLTTLDLLSFTYQVARGMEFLASKNCVHRDLAARNVLLAQGKIVKICDFGLARDIMHDSNYVSK--G 297
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 167 TPY----YMSPELFSNKPYNYKSDVWALGCCVYEMATLKHA-FNAKDMNSLVY-RIVEGKLPQMPSKYDPQLGELIKRML 240
Cdd:cd05105 298 STFlpvkWMAPESIFDNLYTTLSDVWSYGILLWEIFSLGGTpYPGMIVDSTFYnKIKSGYRMAKPDHATQEVYDIMVKCW 377
                       170
                ....*....|...
gi 41055987 241 CKKPEDRPDVKHI 253
Cdd:cd05105 378 NSEPEKRPSFLHL 390
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
8-198 5.59e-12

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


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 67.50  E-value: 5.59e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEVNLVRHksdRKQYVIKKLNLRTSSRRERRAAEQEAQLLsqLKHPNIVMYRES---WEGEDCQLYIVMGFC 84
Cdd:cd14144   1 RSVGKGRYGEVWKGKW---RGEKVAVKIFFTTEEASWFRETEIYQTVL--MRHENILGFIAAdikGTGSWTQLYLITDYH 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  85 EGGDLYHRLKqqkGELLPERQVVEWFVQIAMALQYLHEK--------HILHRDLKTQNIFLTKTNIIKVGDLGIA-RVLE 155
Cdd:cd14144  76 ENGSLYDFLR---GNTLDTQSMLKLAYSAACGLAHLHTEifgtqgkpAIAHRDIKSKNILVKKNGTCCIADLGLAvKFIS 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 41055987 156 NQNDM---ASTLIGTPYYMSPELFSN-------KPYNyKSDVWALGCCVYEMA 198
Cdd:cd14144 153 ETNEVdlpPNTRVGTKRYMAPEVLDEslnrnhfDAYK-MADMYSFGLVLWEIA 204
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
4-259 5.85e-12

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK3 is expressed primarily in the brain, and to a lesser extent in the heart and testis. Mice deficient in JNK3 are protected against kainic acid-induced seizures, stroke, sciatic axotomy neural death, and neuronal death due to NGF deprivation, oxidative stress, or exposure to beta-amyloid peptide. This suggests that JNK3 may play roles in the pathogenesis of these diseases. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 68.19  E-value: 5.85e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIV----MYRESWEGEDCQ-LY 78
Cdd:cd07874  19 YQNLKPIGSGAQGIVCAAYDAVLDRNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIIsllnVFTPQKSLEEFQdVY 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  79 IVMGFCEGgDLYHRLKQQkgelLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVlENQN 158
Cdd:cd07874  99 LVMELMDA-NLCQVIQME----LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLART-AGTS 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 159 DMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVE---GKLPQMPSKYDP----- 230
Cdd:cd07874 173 FMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVIEqlgTPCPEFMKKLQPtvrny 252
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41055987 231 ---------------------------------QLGELIKRMLCKKPEDRPDVKHILRQPYI 259
Cdd:cd07874 253 venrpkyagltfpklfpdslfpadsehnklkasQARDLLSKMLVIDPAKRISVDEALQHPYI 314
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
2-197 5.90e-12

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


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 68.19  E-value: 5.90e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   2 DGYLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRErraAEQEAQLLSQLKHPNIVMYR--ESWE-----GED 74
Cdd:cd14228  15 NSYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQ---GQIEVSILSRLSSENADEYNfvRSYEcfqhkNHT 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  75 CQLYIVMGfcegGDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLT----KTNIIKVGDLGI 150
Cdd:cd14228  92 CLVFEMLE----QNLYDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVdpvrQPYRVKVIDFGS 167
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 41055987 151 ARVLENQndMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEM 197
Cdd:cd14228 168 ASHVSKA--VCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAEL 212
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
9-198 7.29e-12

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


Pssm-ID: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 67.08  E-value: 7.29e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   9 VVGKGSYGEVNlvrhksdRKQYVIKKLNLRTSSRRERRAAEQEAQLLS--QLKHPNIVMY-------RESWEgedcQLYI 79
Cdd:cd14143   2 SIGKGRFGEVW-------RGRWRGEDVAVKIFSSREERSWFREAEIYQtvMLRHENILGFiaadnkdNGTWT----QLWL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  80 VMGFCEGGDLYHRLKQQKgelLPERQVVEWFVQIAMALQYLH--------EKHILHRDLKTQNIFLTKTNIIKVGDLGIA 151
Cdd:cd14143  71 VSDYHEHGSLFDYLNRYT---VTVEGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDLKSKNILVKKNGTCCIADLGLA 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41055987 152 RVLENQN---DMAST-LIGTPYYMSPELFS-----NKPYNYK-SDVWALGCCVYEMA 198
Cdd:cd14143 148 VRHDSATdtiDIAPNhRVGTKRYMAPEVLDdtinmKHFESFKrADIYALGLVFWEIA 204
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
6-255 7.50e-12

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: 66.81  E-value: 7.50e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   6 FVRVVGKGSYGEVNL--VRHKSDRKQYVIKKLNLRTSSRrERRAAEQEAQLLSQLKHPNIVMYRESWEgEDCQLYIVMGF 83
Cdd:cd05086   1 YIQEIGNGWFGKVLLgeIYTGTSVARVVVKELKASANPK-EQDDFLQQGEPYYILQHPNILQCVGQCV-EAIPYLLVFEF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  84 CEGGDLYHRLKQQKGELLPERQVVE---WFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGI--ARVLENQN 158
Cdd:cd05086  79 CDLGDLKTYLANQQEKLRGDSQIMLlqrMACEIAAGLAHMHKHNFLHSDLALRNCYLTSDLTVKVGDYGIgfSRYKEDYI 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 159 DMASTLIGTPYYMSPELFSNK-------PYNYKSDVWALGCCVYEM----ATLKHAFNAKDMNSLVYRIVEGKL--PQMP 225
Cdd:cd05086 159 ETDDKKYAPLRWTAPELVTSFqdgllaaEQTKYSNIWSLGVTLWELfenaAQPYSDLSDREVLNHVIKERQVKLfkPHLE 238
                       250       260       270
                ....*....|....*....|....*....|.
gi 41055987 226 SKYDPQLGELIKrmLC-KKPEDRPDVKHILR 255
Cdd:cd05086 239 QPYSDRWYEVLQ--FCwLSPEKRPTAEEVHR 267
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
6-200 9.64e-12

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


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 66.94  E-value: 9.64e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   6 FVRVVGKGSYGEVNLVR----HK-----------SDRKQYVIKKLNLRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESW 70
Cdd:cd05095   9 FKEKLGEGQFGEVHLCEaegmEKfmdkdfalevsENQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIRLLAVC 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  71 EGEDcQLYIVMGFCEGGDLYHRLKQQKGE----LLPERQVVEW------FVQIAMALQYLHEKHILHRDLKTQNIFLTKT 140
Cdd:cd05095  89 ITDD-PLCMITEYMENGDLNQFLSRQQPEgqlaLPSNALTVSYsdlrfmAAQIASGMKYLSSLNFVHRDLATRNCLVGKN 167
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41055987 141 NIIKVGDLGIARVLENQN--DMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATL 200
Cdd:cd05095 168 YTIKIADFGMSRNLYSGDyyRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETLTF 229
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
112-263 1.38e-11

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: 67.24  E-value: 1.38e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 112 QIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIARVLenQNDMASTLIGTPY----YMSPELFSNKPYNYKSDV 187
Cdd:cd05104 222 QVAKGMEFLASKNCIHRDLAARNILLTHGRITKICDFGLARDI--RNDSNYVVKGNARlpvkWMAPESIFECVYTFESDV 299
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41055987 188 WALGCCVYEMATLKHA-FNAKDMNSLVYRIV-EGKLPQMPSKYDPQLGELIKRMLCKKPEDRPDVKHILRQpyIKHQI 263
Cdd:cd05104 300 WSYGILLWEIFSLGSSpYPGMPVDSKFYKMIkEGYRMDSPEFAPSEMYDIMRSCWDADPLKRPTFKQIVQL--IEQQL 375
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
4-227 1.43e-11

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


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 67.08  E-value: 1.43e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEV-NLVRHKSdrKQYVIKKLnLRTSSRRERRAAEqEAQLLSQLKHP------NIVMYRESWEGEDcq 76
Cdd:cd14224  67 YEVLKVIGKGSFGQVvKAYDHKT--HQHVALKM-VRNEKRFHRQAAE-EIRILEHLKKQdkdntmNVIHMLESFTFRN-- 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  77 lYIVMGF-CEGGDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKT--NIIKVGDLGiARV 153
Cdd:cd14224 141 -HICMTFeLLSMNLYELIKKNKFQGFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQgrSGIKVIDFG-SSC 218
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41055987 154 LENQNdmASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIVEgkLPQMPSK 227
Cdd:cd14224 219 YEHQR--IYTYIQSRFYRAPEVILGARYGMPIDMWSFGCILAELLTGYPLFPGEDEGDQLACMIE--LLGMPPQ 288
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
4-197 1.46e-11

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


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 66.70  E-value: 1.46e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRErraAEQEAQLLSQLKHP-----NIVMYRESWEGEDcQLY 78
Cdd:cd14211   1 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQ---GQIEVSILSRLSQEnadefNFVRAYECFQHKN-HTC 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  79 IVMGFCEGgDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNI----IKVGDLGIARVL 154
Cdd:cd14211  77 LVFEMLEQ-NLYDFLKQNKFSPLPLKYIRPILQQVLTALLKLKSLGLIHADLKPENIMLVDPVRqpyrVKVIDFGSASHV 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 41055987 155 ENQndMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEM 197
Cdd:cd14211 156 SKA--VCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAEL 196
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
4-197 2.23e-11

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


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 66.21  E-value: 2.23e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   4 YLFVRVVGKGSYGEVNLVRHKSDRKQYVIKKLNLRTSSRRErraAEQEAQLLSQLKHPN-----IVMYRESWEGED--CQ 76
Cdd:cd14229   2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKILKNHPSYARQ---GQIEVGILARLSNENadefnFVRAYECFQHRNhtCL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  77 LYIVMGfcegGDLYHRLKQQKGELLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLT----KTNIIKVGDLGIAR 152
Cdd:cd14229  79 VFEMLE----QNLYDFLKQNKFSPLPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMLVdpvrQPYRVKVIDFGSAS 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 41055987 153 VLENQndMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEM 197
Cdd:cd14229 155 HVSKT--VCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAEL 197
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
8-254 2.24e-11

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


Pssm-ID: 133193 [Multi-domain]  Cd Length: 277  Bit Score: 65.44  E-value: 2.24e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   8 RVVGKGSYGEV------NLVRHKSDRKqYVIKKLNlRTSSRRERRAAEQEAQLLSQLK-HPNIVMYRESWEGEDCqlYIV 80
Cdd:cd05062  12 RELGQGSFGMVyegiakGVVKDEPETR-VAIKTVN-EAASMRERIEFLNEASVMKEFNcHHVVRLLGVVSQGQPT--LVI 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MGFCEGGDLYHRLKQQKGE--------LLPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIAR 152
Cdd:cd05062  88 MELMTRGDLKSYLRSLRPEmennpvqaPPSLKKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVKIGDFGMTR 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 153 VLENQNDMASTLIG--TPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIV-EGKLPQMPSKYD 229
Cdd:cd05062 168 DIYETDYYRKGGKGllPVRWMSPESLKDGVFTTYSDVWSFGVVLWEIATLAEQPYQGMSNEQVLRFVmEGGLLDKPDNCP 247
                       250       260
                ....*....|....*....|....*
gi 41055987 230 PQLGELIKRMLCKKPEDRPDVKHIL 254
Cdd:cd05062 248 DMLFELMRMCWQYNPKMRPSFLEII 272
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
7-254 2.33e-11

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: 65.38  E-value: 2.33e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987   7 VRVVGKGSYGEV------NLVRHKSDRKqYVIKKLNlRTSSRRERRAAEQEAQLLSQLKHPNIVMYRESWEGEDCQLyIV 80
Cdd:cd05061  11 LRELGQGSFGMVyegnarDIIKGEAETR-VAVKTVN-ESASLRERIEFLNEASVMKGFTCHHVVRLLGVVSKGQPTL-VV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987  81 MGFCEGGDLYHRLKQQK-------GELLPE-RQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLTKTNIIKVGDLGIAR 152
Cdd:cd05061  88 MELMAHGDLKSYLRSLRpeaennpGRPPPTlQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKIGDFGMTR 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 153 vlenqndmasTLIGTPYY------------MSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIV-EG 219
Cdd:cd05061 168 ----------DIYETDYYrkggkgllpvrwMAPESLKDGVFTTSSDMWSFGVVLWEITSLAEQPYQGLSNEQVLKFVmDG 237
                       250       260       270
                ....*....|....*....|....*....|....*
gi 41055987 220 KLPQMPSKYDPQLGELIKRMLCKKPEDRPDVKHIL 254
Cdd:cd05061 238 GYLDQPDNCPERVTDLMRMCWQFNPKMRPTFLEIV 272
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
101-259 2.35e-11

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: 64.99  E-value: 2.35e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 101 LPERQVVEWFVQIAMALQYLHEKHILHRDLKTQNIFLT-KTNIIKVGDLGIARVLenQNDMASTLIGTPYYMSPELFSNK 179
Cdd:cd14100 103 LPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDlNTGELKLIDFGSGALL--KDTVYTDFDGTRVYSPPEWIRFH 180
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055987 180 PYNYKS-DVWALGCCVYEMATLKHAFNAKDmnslvyRIVEGKLpQMPSKYDPQLGELIKRMLCKKPEDRPDVKHILRQPY 258
Cdd:cd14100 181 RYHGRSaAVWSLGILLYDMVCGDIPFEHDE------EIIRGQV-FFRQRVSSECQHLIKWCLALRPSDRPSFEDIQNHPW 253

                .
gi 41055987 259 I 259
Cdd:cd14100 254 M 254
 
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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